|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
110-1518 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 2353.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 110 DQFSSTAWVQNMANICTSDPDFYKPYSLGCVWKNLSASGDSADVSYQSTFANIVPKLLTKGLRLLKPSKEEDTFQILKPM 189
Cdd:TIGR00956 1 EEFNAKAWVKNFRKLIDSDPIYYKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRDTKTFDILKPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 190 DGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTVYQTLF 269
Cdd:TIGR00956 81 DGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 270 TVARMKTPQNRIKGVDREAYANHVTEVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVAICGARFQCWDNATRGL 349
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 350 DSATALEFIRALKTQADIGKTAATVAIYQCSQDAYDLFDKVCVLDDGYQLYFGPAKDAKKYFQDMGYYCPPRQTTADFLT 429
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 430 SITSPTERIISKEFIEKgtrVPQTPKDMAEYWLQSESYKNLIKDIDSTLEK-NTDEARNIIRDAHHAKQAKRAPPSSPYV 508
Cdd:TIGR00956 321 SLTSPAERQIKPGYEKK---VPRTPQEFETYWRNSPEYAQLMKEIDEYLDRcSESDTKEAYRESHVAKQSKRTRPSSPYT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 509 VNYGMQVKYLLIRNFWRMKQSASVTLWQVIGNSVMAFILGSMFYKVMKknDTSTFYFRGAAMFFAILFNAFSCLLEIFSL 588
Cdd:TIGR00956 398 VSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPK--NTSDFYSRGGALFFAILFNAFSSLLEIASM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 589 YETRPITEKHRTYSLYHPSADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGS 668
Cdd:TIGR00956 476 YEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 669 LTKTLQEAMVPASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLAYLFESLMINEFHDRRFPCAQYIPAGPAYQNITGT 748
Cdd:TIGR00956 556 VTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYDNLGVT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 749 QRVCSAVGAYPGNDYVLGDDFLKESYDYEHKHKWRGFGIGMAYVVFFFFVYLILCEYNEGAKQKGEMVVFLRSKIKQLKK 828
Cdd:TIGR00956 636 NKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 829 EGKLQEKhRPGDIENNAGSSPDSATTEKKILDDSSEgsdsssdnagLGLSKSEAIFHWRDLCYDVPIKGGQRRILNNVDG 908
Cdd:TIGR00956 716 AGETSAS-NKNDIEAGEVLGSTDLTDESDDVNDEKD----------MEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDG 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 909 WVKPGTLTALMGASGAGKTTLLDCLAERVTMGVIT-GNIFVDGRLRDESFPRSIGYCQQQDLHLKTATVRESLRFSAYLR 987
Cdd:TIGR00956 785 WVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITgGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 988 QPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVFLDEPTSGLDSQTAWDTCQL 1067
Cdd:TIGR00956 865 QPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKL 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1068 MRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGGQTVYFGDLGEGCKTMIDYFESKGAHKCPPDANPAEWMLEVVGAA 1147
Cdd:TIGR00956 945 MRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAA 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1148 PGSHATQDYNEVWRNSDEYKAVQEELDWMEKNLPGRSKEPTAEEHKPFAASLYYQFKMVTIRLFQQYWRSPDYLWSKFIL 1227
Cdd:TIGR00956 1025 PGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFL 1104
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1228 TIFNQVFIGFTFFKADRSLQGLQNQMLSIFMYTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWLAFFLSQIIVEIPW 1307
Cdd:TIGR00956 1105 TIFAALFIGFTFFKVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPY 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1308 NILAGTIAYCIYYYAVGFYANASAAGQLHERGALFWLFSIAFYVYIGSMGLLMISFNEVAETAAHMGTLLFTMALSFCGV 1387
Cdd:TIGR00956 1185 NLVAGTIFFFIWYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGV 1264
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1388 MATPKVMPRFWIFMYRVSPLTYMIDALLALGVANVDVKCSNYEMVKFTPPSGTTCGDYMASYIKLAGtGYLSDPSATDIC 1467
Cdd:TIGR00956 1265 LAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAG-GYLLNPNATDSC 1343
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1468 SFCAVSTTNAFLATFSSHYYRRWRNYGIFICYIAFDYIAATFLYWLSRVPK 1518
Cdd:TIGR00956 1344 SFCQYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
170-1415 |
3.92e-144 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 480.11 E-value: 3.92e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 170 GLRLLKPSKeedtFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSN-SHGFKIAKDsiVSYNGLSSSDIRKhyRGE 248
Cdd:PLN03140 169 GINLAKKTK----LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKlDPSLKVSGE--ITYNGYRLNEFVP--RKT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 249 VVYNAESDIHLPHLTVYQTLFTVARMKTPQNRI------------------KGVD--------REAYANHVTEVAMATYG 302
Cdd:PLN03140 241 SAYISQNDVHVGVMTVKETLDFSARCQGVGTRYdllselarrekdagifpeAEVDlfmkatamEGVKSSLITDYTLKILG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 303 LSHTRDTKVGNDLVRGVSGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALktQADIGKTAATV--AIYQCS 380
Cdd:PLN03140 321 LDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL--QQIVHLTEATVlmSLLQPA 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 381 QDAYDLFDKVCVLDDGYQLYFGPAKDAKKYFQDMGYYCPPRQTTADFLTSITSPteriiskefiekgtrvpqtpKDMAEY 460
Cdd:PLN03140 399 PETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSK--------------------KDQEQY 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 461 WLQ-------------SESYK--NLIKDIDSTLEKNTDEARniirdAHHAkqakrAPPSSPYVVNYGMQVKYLLIRNFWR 525
Cdd:PLN03140 459 WADrnkpyryisvsefAERFKsfHVGMQLENELSVPFDKSQ-----SHKA-----ALVFSKYSVPKMELLKACWDKEWLL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 526 MKQSASVTLWQVIGNSVMAFILGSMFYK--VMKKNDTSTFYFRGAAMFFAI--LFNAFSCLleifSLYETR-PITEKHRT 600
Cdd:PLN03140 529 MKRNAFVYVFKTVQIIIVAAIASTVFLRteMHTRNEEDGALYIGALLFSMIinMFNGFAEL----ALMIQRlPVFYKQRD 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 601 YsLYHPS-ADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVP 679
Cdd:PLN03140 605 L-LFHPPwTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTG 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 680 ASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLAYLFESLMINEFHdrrfpcaqyipaGPAYQNITGTQRVCSavgayp 759
Cdd:PLN03140 684 GALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMF------------APRWMNKMASDNSTR------ 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 760 gndyvLGDDFLkESYDYEHKHKWRGFGIG--MAYVVFFFFVYLILCEY-NEGAKQKGEMVVFLRSKIKQLKKEGKLQEKH 836
Cdd:PLN03140 746 -----LGTAVL-NIFDVFTDKNWYWIGVGalLGFTILFNVLFTLALTYlNPLGKKQAIISEETAEEMEGEEDSIPRSLSS 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 837 RPGDIENN-AGSSPDSATTEKKILDDSSEGSDSSSDNAGLGLSKSEAIFHWRDLCY--DVPIKGGQR-------RILNNV 906
Cdd:PLN03140 820 ADGNNTREvAIQRMSNPEGLSKNRDSSLEAANGVAPKRGMVLPFTPLAMSFDDVNYfvDMPAEMKEQgvtedrlQLLREV 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 907 DGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDG-RLRDESFPRSIGYCQQQDLHLKTATVRESLRFSAY 985
Cdd:PLN03140 900 TGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGfPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAF 979
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 986 LRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAG-EGLNVEQRKRLTIGVELAARPKLlVFLDEPTSGLDSQTAWDT 1064
Cdd:PLN03140 980 LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSI-IFMDEPTSGLDARAAAIV 1058
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1065 CQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGGQTVYFGDLGEGCKTMIDYFES-KGAHKCPPDANPAEWMLEV 1143
Cdd:PLN03140 1059 MRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAiPGVPKIKEKYNPATWMLEV 1138
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1144 VGAAPGSHATQDYNEVWRNSDEY---KAVQEELDWMEknlPGRSKEPTAEEhkpFAASLYYQFKMVTIRLFQQYWRSPDY 1220
Cdd:PLN03140 1139 SSLAAEVKLGIDFAEHYKSSSLYqrnKALVKELSTPP---PGASDLYFATQ---YSQSTWGQFKSCLWKQWWTYWRSPDY 1212
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1221 LWSKFILTIFNQVFIGFTFFK--ADRSLQGLQNQMLSIFMYTVIFNPI--LQQYLPSFVQQRDLYeARERPSRTFSWLAF 1296
Cdd:PLN03140 1213 NLVRFFFTLAAALMVGTIFWKvgTKRSNANDLTMVIGAMYAAVLFVGInnCSTVQPMVAVERTVF-YRERAAGMYSALPY 1291
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1297 FLSQIIVEIPWNILAGTIAYCIYYYAVGFYANASaagqlhergALFWLFSIAF--YVYIGSMGLLMISFNEVAETAAHMG 1374
Cdd:PLN03140 1292 AIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAA---------KFFWFYFISFfsFLYFTYYGMMTVSLTPNQQVAAIFA 1362
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|..
gi 6320614 1375 TLLFTMALSFCG-VMATPKVmPRFWIFMYRVSPLTYMIDALL 1415
Cdd:PLN03140 1363 AAFYGLFNLFSGfFIPRPKI-PKWWVWYYWICPVAWTVYGLI 1403
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
883-1109 |
9.61e-110 |
|
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: 345.38 E-value: 9.61e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 883 IFHWRDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGRLRDESFPRSIG 962
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 963 YCQQQDLHLKTATVRESLRFSAYLRqpssvsieeknryveevikilemqqysdavvgvageGLNVEQRKRLTIGVELAAR 1042
Cdd:cd03232 83 YVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1043 PkLLVFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGGQTVYFG 1109
Cdd:cd03232 127 P-SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
898-1329 |
5.72e-79 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 274.23 E-value: 5.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV-ITGNIFVDGRLRDESFPRSI-GYCQQQDLHLKTAT 975
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 976 VRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAG--EGLNVEQRKRLTIGVELAARPKLLvFLDEPT 1053
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLL-FCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1054 SGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKgGQTVYFGDLGEGCKtmidyFESKGAHKCPPD 1133
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE-GRVAYLGSPDQAVP-----FFSDLGHPCPEN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1134 ANPAEWMLEVVGAAPGSHAT--QDYNEVWRN---SDEYKAVQEELDWMEKNLPGRSKEPTAEEHKPFAASLYYQFKMVTI 1208
Cdd:TIGR00955 269 YNPADFYVQVLAVIPGSENEsrERIEKICDSfavSDIGRDMLVNTNLWSGKAGGLVKDSENMEGIGYNASWWTQFYALLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1209 RLFQQYWRSPDYLWSKFILTIFNQVFIGFTFFKADRSLQGLQNQMLSIFMYtvIFNPILQQYLPS---FVQQRDLYeARE 1285
Cdd:TIGR00955 349 RSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLF--LTNMTFQNVFPVinvFTAELPVF-LRE 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 6320614 1286 RPSRTFSWLAFFLSQIIVEIPWNILAGTIAYCIYYYAVGFYANA 1329
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGA 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
174-402 |
5.55e-77 |
|
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: 253.34 E-value: 5.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 174 LKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGfKIAKDSIVSYNGLSSSDIRKHYRGEVVYNA 253
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG-NVSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 254 ESDIHLPHLTVYQTLFTVARMKtpqnrikgvdreayanhvtevamatyglshtrdtkvGNDLVRGVSGGERKRVSIAEVA 333
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 334 ICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATVAIYQCSQDAYDLFDKVCVLDDGYQLYFG 402
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
884-1109 |
1.04e-63 |
|
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: 215.11 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 884 FHWRDLCYDVPIK--GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGR-LRDESFPRS 960
Cdd:cd03213 4 LSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRpLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 961 IGYCQQQDLHLKTATVRESLRFSAYLRqpssvsieeknryveevikilemqqysdavvgvageGLNVEQRKRLTIGVELA 1040
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1041 ARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKgGQTVYFG 1109
Cdd:cd03213 128 SNPSLL-FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
140-740 |
2.90e-57 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 210.29 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 140 VWKNLSAsgdsadvsYQSTFANIVPKLLTKGLRLlKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISS- 218
Cdd:TIGR00955 4 SWRNSDV--------FGRVAQDGSWKQLVSRLRG-CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 219 NSHGFKIAKDsiVSYNG--LSSSDIRKhyRGEVVYnaESDIHLPHLTVYQTLFTVARMKTPQNRIKGVDREAyanhVTEV 296
Cdd:TIGR00955 75 SPKGVKGSGS--VLLNGmpIDAKEMRA--ISAYVQ--QDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRER----VDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 297 AMATyGLSHTRDTKVGN-DLVRGVSGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATVa 375
Cdd:TIGR00955 145 LQAL-GLRKCANTRIGVpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 376 IYQCSQDAYDLFDKVCVLDDGYQLYFGPAKDAKKYFQDMGYYCPPRQTTADFLTSITSpteriiskefIEKGTRvpQTPK 455
Cdd:TIGR00955 223 IHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA----------VIPGSE--NESR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 456 DMAEYWLQSESYKNLIKDIDSTLEKNTDEARNIIRDAhhakqakRAPPSSPYVVNYGMQVKYLLIRnFWR--MKQSAS-- 531
Cdd:TIGR00955 291 ERIEKICDSFAVSDIGRDMLVNTNLWSGKAGGLVKDS-------ENMEGIGYNASWWTQFYALLKR-SWLsvLRDPLLlk 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 532 VTLWQVIgnsVMAFILGSMFYKVmkKNDTSTFYFRGAAMFFAILFNAFSCLLEIFSLYET-RPITEKHRTYSLYHPSADA 610
Cdd:TIGR00955 363 VRLIQTM---MTAILIGLIYLGQ--GLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAeLPVFLRETRSGLYRVSAYF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 611 FASVLSEMPPKLITAVCFNIIFYFLVDFRRNG-GVFFFYFLINVIATFTLS--HLFRCVGSLTKTLQEAMVPASMLLLAI 687
Cdd:TIGR00955 438 LAKTIAELPLFIILPALFTSITYWMIGLRSGAtHFLTFLFLVTLVANVATSfgYLISCAFSSTSMALTVGPPFVIPFLLF 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 688 SmytGFAIPKTKILGWSIWIWYINPLAYLFESLMINEFHD-RRFPCAQYIPAGP 740
Cdd:TIGR00955 518 G---GFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDvDNIECTSANTTGP 568
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
886-1109 |
3.01e-51 |
|
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: 180.54 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 886 WRDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVIT-GNIFVDGRLRD-ESFPRSIGY 963
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKpDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 964 CQQQDLHLKTATVRESLRFSAYLRQPSsvsiEEKNRYVEEVIKILEMQQYSDAVVG-VAGEGLNVEQRKRLTIGVELAAR 1042
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPR----KSSDAIRKKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1043 PKLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGGqTVYFG 1109
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
900-1529 |
9.87e-51 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 197.64 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERV--TMGVITGNIFVDGRLRDE---SFPRSIGYCQQQDLHLKTA 974
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITYDGITPEEikkHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQPSS----VSIEEKNRYVEEVIkileMQQY-----------SDAVVGVAGEglnveQRKRLTIGVEL 1039
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNrpdgVSREEYAKHIADVY----MATYglshtrntkvgNDFVRGVSGG-----ERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1040 AARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAI-LCTIHQPSAILMQQFDRLLFLQKGGQtVYFGDLGEGCKtm 1118
Cdd:TIGR00956 225 LGGAKIQ-CWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQ-IYFGPADKAKQ-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1119 idYFESKGaHKCPPDANPAEWMLEVVGAA-----PGS-----HATQDYNEVWRNSDEYKAVQEELD-WMEKNLPGRSKEP 1187
Cdd:TIGR00956 301 --YFEKMG-FKCPDRQTTADFLTSLTSPAerqikPGYekkvpRTPQEFETYWRNSPEYAQLMKEIDeYLDRCSESDTKEA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1188 TAEEH-----------KPFAASLYYQFKMVTIRLFQQYWRSPDYLWSKFILTIFNQVFIGFTFFKADRSLQGLQNQMlSI 1256
Cdd:TIGR00956 378 YRESHvakqskrtrpsSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRG-GA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1257 FMYTVIFNPI--------LQQYLPSFVQQRDLyeARERPSrtfswlAFFLSQIIVEIPWNILAGTIAYCIYYYAVGFYAN 1328
Cdd:TIGR00956 457 LFFAILFNAFsslleiasMYEARPIVEKHRKY--ALYHPS------ADAIASIISEIPFKIIESVVFNIILYFMVNFRRT 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1329 ASAagqlhergalFWlfsiaFYVYIGSMGLLMIS--FNEVAETA-----AHMGTLLFTMALSFCGVMATPKV-MPRFWIF 1400
Cdd:TIGR00956 529 AGR----------FF-----FYLLILFICTLAMShlFRSIGAVTktlseAMTPAAILLLALSIYTGFAIPRPsMLGWSKW 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1401 MYRVSPLTYMIDALLALGVANVDVKCSNYemvkftPPSGTtcgdymasyiklagtGYLSDPSATDICSFCA-------VS 1473
Cdd:TIGR00956 594 IYYVNPLAYAFESLMVNEFHGRRFECSQY------VPSGG---------------GYDNLGVTNKVCTVVGaepgqdyVD 652
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1474 TTNAFLATFSSHYYRRWRNYGIFICYIAFDYIAATFLYWLSRVPKKNGKISEKPKK 1529
Cdd:TIGR00956 653 GDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRG 708
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1206-1416 |
1.01e-48 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 172.46 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1206 VTIRLFQQYWRSPDYLWSKFILTIFNQVFIGFTFFKADRSLQGLQNQMLSIFMYTVIFNPILQQYLPSFVQQRDLYEaRE 1285
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1286 RPSRTFSWLAFFLSQIIVEIPWNILAGTIAYCIYYYAVGFYANASaagqlheRGALFWLFSIAFYVYIGSMGLLMISFNE 1365
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAG-------RFFLFLLVLLLTALAASSLGLFISALAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1366 VAETAAHMGTLLFTMALSFCGVMATPKVMPRFWIFMYRVSPLTYMIDALLA 1416
Cdd:pfam01061 153 SFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRA 203
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
518-723 |
1.59e-48 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 172.07 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 518 LLIRNFWRMKQSASVTLWQVIGNSVMAFILGSMFYKVmkkNDTSTFYFRGAAMFFAILFNAFSCLLEI-FSLYETRPITE 596
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL---GNQQGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 597 KHRTYSLYHPSADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGSLTKTLQEA 676
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6320614 677 MVPASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLAYLFESLMIN 723
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
736-827 |
3.77e-43 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 152.23 E-value: 3.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 736 IPAGPAYQNITGTQRVCSAVGAYPGNDYVLGDDFLKESYDYEHKHKWRGFGIGMAYVVFFFFVYLILCEYNEGAKQKGEM 815
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
90
....*....|..
gi 6320614 816 VVFLRSKIKQLK 827
Cdd:pfam06422 81 LVFKRGKAPKLK 92
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
175-723 |
2.94e-41 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 163.13 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 175 KPSKEEDTFQ---ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAkDSIVSYNGLSSSDIRKhyrgEVVY 251
Cdd:PLN03211 70 KISDETRQIQertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT-GTILANNRKPTKQILK----RTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 252 NAESDIHLPHLTVYQTLFTVARMKTPQNRIKGVDreayaNHVTEVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAE 331
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEK-----ILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 332 VAICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATvAIYQCSQDAYDLFDKVCVLDDGYQLYFGPAKDAKKYF 411
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVT-SMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 412 QDMGYYCPPRQTTADFLTSITSPTERIISKEFIEKgtrvPQTPKDMAeywlqsESYKNL----IKDIDSTLEKNTDEARN 487
Cdd:PLN03211 299 ESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREK----PNVKQSLV------ASYNTLlapkVKAAIEMSHFPQANARF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 488 IirDAHHAKQAKRAPPSSpyVVNYGMQVKYLLIRNFWRMKQSASVTL--WQVIGNSVMAfilGSMFYkvmkKNDTSTFYF 565
Cdd:PLN03211 369 V--GSASTKEHRSSDRIS--ISTWFNQFSILLQRSLKERKHESFNTLrvFQVIAAALLA---GLMWW----HSDFRDVQD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 566 RGAAMFF-AILFNAFSCLLEIFSLYETRPITEKHRTYSLYHPSADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGV 644
Cdd:PLN03211 438 RLGLLFFiSIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGA 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 645 FFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVPASMLLLAISMYTGFAIpkTKILGWSIWIWYINPLAYLFEsLMIN 723
Cdd:PLN03211 518 FLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYR-LLIN 593
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
899-1325 |
4.89e-41 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 162.36 E-value: 4.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGRLRDESFPRSIGYCQQQDLHLKTATVRE 978
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 979 SLRFSAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAG-EGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLD 1057
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLI-LDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1058 SQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKgGQTVYFGDLGEGcktmIDYFESKGAHKCPPdANPA 1137
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGKGSDA----MAYFESVGFSPSFP-MNPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1138 EWMLEVVGAA-----------PGSHAT--QDYNEVWrnSDEYKAVQEELDWMEKNLPGRSKEPTAEEHKPFAASL---YY 1201
Cdd:PLN03211 313 DFLLDLANGVcqtdgvserekPNVKQSlvASYNTLL--APKVKAAIEMSHFPQANARFVGSASTKEHRSSDRISIstwFN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1202 QFKMVTIRLFQQYwRSPDYLWSKFILTIFNQVFIGFTFFKAD-RSLQglqnQMLSIFMYTVIFNPILQQYLPSFV--QQR 1278
Cdd:PLN03211 391 QFSILLQRSLKER-KHESFNTLRVFQVIAAALLAGLMWWHSDfRDVQ----DRLGLLFFISIFWGVFPSFNSVFVfpQER 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 6320614 1279 DLYeARERPSRTFSWLAFFLSQIIVEIPWNILAGTIAYCIYYYAVGF 1325
Cdd:PLN03211 466 AIF-VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGL 511
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
881-1109 |
1.22e-36 |
|
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: 137.78 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 881 EAIFHWRDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV-ITGNIFVDGRLRDE---S 956
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPYKEfaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 FPRSIGYCQQQDLHLKTATVRESLRFSAYLRqpssvsieeKNRYVeevikilemqqysdavvgvagEGLNVEQRKRLTIG 1036
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCK---------GNEFV---------------------RGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1037 VELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIHQPSAILMQQFDRLLFLqKGGQTVYFG 1109
Cdd:cd03233 131 EALVSRASVL-CWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
180-727 |
1.82e-35 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 148.07 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 180 EDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSIVSynGL-SSSDIRKHYRGevvYNAESDIH 258
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRIS--GFpKKQETFARISG---YCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 259 LPHLTVYQTLFTVARMKTPqnriKGVDREAYANHVTEVaMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVAICGAR 338
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLP----KEVSKEEKMMFVDEV-MELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 339 FQCWDNATRGLDSATALEFIRALKTQADIGKTAaTVAIYQCSQDAYDLFDKVCVLDDGYQ-LYFGP-AKDAKK---YFQD 413
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTV-VCTIHQPSIDIFEAFDELLLMKRGGQvIYSGPlGRNSHKiieYFEA 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 414 MGYY--CPPRQTTADFLTSITSPTERIiskefiekgtrvpQTPKDMAEYWLQSESY---KNLIKDIDSTLEKNTDearni 488
Cdd:PLN03140 1119 IPGVpkIKEKYNPATWMLEVSSLAAEV-------------KLGIDFAEHYKSSSLYqrnKALVKELSTPPPGASD----- 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 489 irdAHHAKQakrappsspYVVNYGMQVKYLLIRNFWRMKQSASVTLWQVIGNSVMAFILGSMFYKV-MKKNDTSTFYFRG 567
Cdd:PLN03140 1181 ---LYFATQ---------YSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVgTKRSNANDLTMVI 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 568 AAMFFAILF---NAFSCLLEIFSLyeTRPITEKHRTYSLYHPSADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGV 644
Cdd:PLN03140 1249 GAMYAAVLFvgiNNCSTVQPMVAV--ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAK 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 645 FFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVPASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLAYLFESLMINE 724
Cdd:PLN03140 1327 FFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQ 1406
|
...
gi 6320614 725 FHD 727
Cdd:PLN03140 1407 YGD 1409
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
169-402 |
1.55e-34 |
|
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: 131.52 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 169 KGLRLLKPSK-EEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDsiVSYNGLSSSDIRkhYRG 247
Cdd:cd03213 7 RNLTVTVKSSpSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGE--VLINGRPLDKRS--FRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 248 EVVYNAESDIHLPHLTVYQTLFTVARMktpqnrikgvdreayanhvtevamatyglshtrdtkvgndlvRGVSGGERKRV 327
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKL------------------------------------------RGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 328 SIAEVAICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATVaIYQCSQDAYDLFDKVCVLDDGYQLYFG 402
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICS-IHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
174-402 |
4.92e-31 |
|
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: 122.38 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 174 LKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSIVsYNGLSSSdiRKHYRGEVVYNA 253
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQIL-FNGQPRK--PDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 254 ESDIHLPHLTVYQTLFTVARMKTPqnrikgvdrEAYANHVTEVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVA 333
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLP---------RKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 334 ICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTaATVAIYQCSQDAYDLFDKVCVLDDGYQLYFG 402
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI-VILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
186-346 |
9.96e-31 |
|
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: 118.90 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 186 LKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGfkiAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTVY 265
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 266 QTLFTVARMKTPQNRIKGVDReayanhvtEVAMATYGLSHTRDTKVGNdLVRGVSGGERKRVSIAEVAICGARFQCWDNA 345
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARA--------EEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
.
gi 6320614 346 T 346
Cdd:pfam00005 149 T 149
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
898-1113 |
3.53e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.17 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDGR--LRDESFPRS-IGYCQQQDLHL 971
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML-----LGLLRptsGEVRVLGEdvARDPAEVRRrIGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLvFLDE 1051
Cdd:COG1131 86 PDLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELL-ILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1052 PTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAIlMQQFDRLLFLqKGGQTVYFGDLGE 1113
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEA-ERLCDRVAII-DKGRIVADGTPDE 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
887-1102 |
2.14e-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: 117.18 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPikGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERvtMGVITGNIFVDGRLRDES----FPRSIG 962
Cdd:cd03225 3 KNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGPTSGEVLVDGKDLTKLslkeLRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 963 YC-QQQDLHLKTATVRESLRFSAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAA 1041
Cdd:cd03225 79 LVfQNPDDQFFGPTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1042 RPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSaILMQQFDRLLFLQKG 1102
Cdd:cd03225 152 DPDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
896-1074 |
3.60e-27 |
|
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: 111.06 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDG---RLRDESFPRSIGYCQQQDLHLK 972
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGysiRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKlLVFLDEP 1052
Cdd:cd03263 89 ELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPS-VLLLDEP 160
|
170 180 190
....*....|....*....|....*....|
gi 6320614 1053 TSGLDSQT---AWDTCQLMRK-----LATH 1074
Cdd:cd03263 161 TSGLDPASrraIWDLILEVRKgrsiiLTTH 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
898-1113 |
4.65e-27 |
|
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: 111.49 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDG---RLRDESFPRSIGYCQQQD-LHlKT 973
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGedvRKEPREARRQIGVLPDERgLY-DR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:COG4555 89 LTVRENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLL-LDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1054 SGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKgGQTVYFGDLGE 1113
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVE-ALCDRVVILHK-GKVVAQGSLDE 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
898-1113 |
2.02e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGRLRDESFPRsIGYCQQQ---DLHL 971
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLL-----KAILGLLpptSGTVRLFGKPPRRARRR-IGYVPQRaevDWDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KtATVRESLRFSAYLRQP--SSVSIEEKNRyVEEVIKILEMQQYSDAVVGvageglnvE----QRKRLTIGVELAARPKL 1045
Cdd:COG1121 91 P-ITVRDVVLMGRYGRRGlfRRPSRADREA-VDEALERVGLEDLADRPIG--------ElsggQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 1046 LVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAIlMQQFDRLLFLQKGgqTVYFGDLGE 1113
Cdd:COG1121 161 LL-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAV-REYFDRVLLLNRG--LVAHGPPEE 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
887-1102 |
2.67e-25 |
|
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: 105.88 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGR-LRDESFP---R 959
Cdd:COG1122 4 ENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLL-----RLLNGLLkptSGEVLVDGKdITKKNLRelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYC-QQQDLHLKTATVRESLRFSayLRQpSSVSIEEKNRYVEEVIKILEMQQYSDAVV-----GvageglnveQRKRL 1033
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEDVAFG--PEN-LGLPREEIRERVEEALELVGLEHLADRPPhelsgG---------QKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1034 TI-GVeLAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:COG1122 144 AIaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVA-ELADRVIVLDDG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
898-1088 |
1.24e-24 |
|
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: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDG---RLRDESFPRSIGYCQQQDlHL 971
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPpsaGEVLWNGepiRDAREDYRRRLAYLGHAD-GL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTA-TVRESLRFSAYLRQPSSVSIEeknryVEEVIKILEMQQYSDAVVGV--AGeglnveQRKRLTIGVELAARPKLLVf 1048
Cdd:COG4133 87 KPElTVRENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQlsAG------QKRRVALARLLLSPAPLWL- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6320614 1049 LDEPTSGLDSQT-AWdTCQLMRKLATHGQAILCTIHQPSAI 1088
Cdd:COG4133 155 LDEPFTALDAAGvAL-LAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
887-1102 |
1.58e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.58 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDG------------RL 952
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVLIDGqdisslserelaRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 953 RDesfpRSIGYcqqQDLHL-KTATVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGvageglnvE--- 1028
Cdd:COG1136 84 RR----RHIGFv-fQFFNLlPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPS--------Qlsg 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1029 -QRKRLTIGVELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIHQPSaiLMQQFDRLLFLQKG 1102
Cdd:COG1136 148 gQQQRVAIARALVNRPKLI-LADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
897-1102 |
5.14e-24 |
|
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: 108.69 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR----LRDESFPRSIGYCQQQDlHLK 972
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVdlsdLDPASWRRQIAWVPQNP-YLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFSAylRQPSSVSIEE--KNRYVEEVIKILEmQQYsDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLD 1050
Cdd:COG4988 424 AGTIRENLRLGR--PDASDEELEAalEAAGLDEFVAALP-DGL-DTPLGEGGRGLSGGQAQRLALARALLRDAPLLL-LD 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQPSaiLMQQFDRLLFLQKG 1102
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLDDG 547
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
903-1054 |
6.27e-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: 99.26 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNIFVDGRLRDESFPRSIGYCQQQDLHLKTATVRESL 980
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAglLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 981 RFSAYLRQPSSvsiEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLvFLDEPTS 1054
Cdd:pfam00005 81 RLGLLLKGLSK---REKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL-LLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
898-1102 |
2.66e-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: 98.24 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDG---RLRDESFPRSIGYCQQQDLHL 971
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII-----LGLLKpdsGEIKVLGkdiKKEPEEVKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAylrqpssvsieeknryveevikilemqqysdavvGvageglnveQRKRLTIGVELAARPKLLvFLDE 1051
Cdd:cd03230 86 ENLTVRENLKLSG----------------------------------G---------MKQRLALAQALLHDPELL-ILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1052 PTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAE-RLCDRVAILNNG 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
890-1109 |
4.78e-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: 98.76 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 890 CYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDGRlRDESFPRSIGYCQQ 966
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLL-----KAILGLLKptsGSIRVFGK-PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 967 QDLHLKT--ATVRE--SLRFSAYLRQPSSVSIEEKNRyVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAAR 1042
Cdd:cd03235 76 RRSIDRDfpISVRDvvLMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGG----QQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1043 PKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAiLMQQFDRLLFLQKGGqtVYFG 1109
Cdd:cd03235 151 PDLLL-LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRTV--VASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
897-1105 |
4.53e-22 |
|
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: 95.79 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGRLRDESFP-RSIGYCQQQ-DLHL 971
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLA-----KILAGLIkesSGSILLNGKPIKAKERrKSIGYVMQDvDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAYLrqpssvsIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVFlDE 1051
Cdd:cd03226 85 FTDSVREELLLGLKE-------LDAGNEQAETVLKDLDLYALKERHPLSLSGG----QKQRLAIAAALLSGKDLLIF-DE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1052 PTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSaILMQQFDRLLFLQKGGQT 1105
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE-FLAKVCDRVLLLANGAIV 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
887-1110 |
9.37e-22 |
|
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: 96.27 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVpikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR----LRDESFPR 959
Cdd:COG1120 5 ENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLKpssGEVLLDGRdlasLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYCQQQDLHLKTATVRESLRFSAY-----LRQPSsvsiEEKNRYVEEVIKILEMQQYSDAVV-----GvageglnveQ 1029
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGRYphlglFGRPS----AEDREAVEEALERTGLEHLADRPVdelsgG---------E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1030 RKRLTIGVELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIHQPSaiLMQQF-DRLLFLqKGGQTVY 1107
Cdd:COG1120 143 RQRVLIARALAQEPPLL-LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLN--LAARYaDRLVLL-KDGRIVA 218
|
...
gi 6320614 1108 FGD 1110
Cdd:COG1120 219 QGP 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
897-1102 |
1.38e-21 |
|
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: 101.83 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR-LRD---ESFPRSIGYCqQQDLH 970
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglYEPT----SGRILIDGIdLRQidpASLRRQIGVV-LQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKTATVRESLRFSAylrqpSSVSIEEknryVEEVIK-------ILEM-QQYsDAVVGVAGEGLNVEQRKRLTIGVELAAR 1042
Cdd:COG2274 560 LFSGTIRENITLGD-----PDATDEE----IIEAARlaglhdfIEALpMGY-DTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1043 PKLLvFLDEPTSGLDSQTAwdtCQLMRKLATHGQAilCTI----HQPSAIlmQQFDRLLFLQKG 1102
Cdd:COG2274 630 PRIL-ILDEATSALDAETE---AIILENLRRLLKG--RTViiiaHRLSTI--RLADRIIVLDKG 685
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
887-1102 |
2.43e-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: 94.09 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRL-------RDESF 957
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVRVDGTDisklsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 958 PR-SIGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIG 1036
Cdd:cd03255 80 RRrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRER---AEELLERVGLGDRLNHYPS----ELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1037 VELAARPKlLVFLDEPTSGLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSaiLMQQFDRLLFLQKG 1102
Cdd:cd03255 153 RALANDPK-IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
903-1079 |
2.99e-21 |
|
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: 94.43 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR----LRdesfPRSIgyCQQ------QDL 969
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-----GFLRptsGSVLFDGEditgLP----PHEI--ARLgigrtfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HL-KTATVRESLRFSAYLRQPSSVSI-------EEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAA 1041
Cdd:cd03219 85 RLfPELTVLENVMVAAQARTGSGLLLararreeREARERAEELLERVGLADLADRPAG----ELSYGQQRRLEIARALAT 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 6320614 1042 RPKLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:cd03219 161 DPKLL-LLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
898-1109 |
1.03e-20 |
|
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: 90.96 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRlrdesfprsigycqqqdlHLKTA 974
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-----GLLkpsSGEILLDGK------------------DLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQpssvsieeknryveeVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLvFLDEPTS 1054
Cdd:cd03214 67 SPKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGG----ERQRVLLARALAQEPPIL-LLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1055 GLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVYFG 1109
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAA-RYADRVILL-KDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
898-1102 |
2.04e-20 |
|
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: 91.43 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFP--RSIGYCQQQDL---H 970
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPD----SGEILIDGRDVTGVPPerRNIGMVFQDYAlfpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LktaTVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVgvagEGLNVEQRKRLTIGVELAARPKLLvFLD 1050
Cdd:cd03259 87 L---TVAENIAFGLKLRGVPKAEIRAR---VRELLELVGLEGLLNRYP----HELSGGQQQRVALARALAREPSLL-LLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKL--ATHGQAILCTIHQPSAILMQqfDRLLFLQKG 1102
Cdd:cd03259 156 EPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALA--DRIAVMNEG 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
887-1102 |
2.16e-20 |
|
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: 97.14 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPikGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGNIFVDGR----LRDESFPR 959
Cdd:COG4987 337 EDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-----LRFLdpqSGSITLGGVdlrdLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYCQQqDLHLKTATVRESLRFSAylrqpSSVSIEEknryVEEVIKILEMQQYS-------DAVVGVAGEGLNVEQRKR 1032
Cdd:COG4987 410 RIAVVPQ-RPHLFDTTLRENLRLAR-----PDATDEE----LWAALERVGLGDWLaalpdglDTWLGEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1033 LTIGVELAARPKLLVfLDEPTSGLDSQTAwdtCQLMRKL--ATHGQAILCTIHQPSAilMQQFDRLLFLQKG 1102
Cdd:COG4987 480 LALARALLRDAPILL-LDEPTEGLDAATE---QALLADLleALAGRTVLLITHRLAG--LERMDRILVLEDG 545
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
898-1107 |
3.95e-20 |
|
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: 90.42 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGRLRDESFPRSIGYC-QQQDLHLKT 973
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTI-----RMILGIIlpdSGEVLFDGKPLDIAARNRIGYLpEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 aTVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVgvagEGLNVEQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:cd03269 86 -KVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLI-LDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 1054 SGLDSQTAWDTCQLMRKLATHGQAILCTIHQpsailMQQF----DRLLFLQKGGQTVY 1107
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQ-----MELVeelcDRVLLLNKGRAVLY 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
898-1102 |
5.92e-20 |
|
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: 88.07 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRDESFPRsigycqqqdlhlkta 974
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-----GLLKptsGEILIDGKDIAKLPLE--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 tvreslrfsAYLRQPSSVSieeknryveevikilemqQYSdavvgvAGeglnveQRKRLTIGVELAARPKLLvFLDEPTS 1054
Cdd:cd00267 70 ---------ELRRRIGYVP------------------QLS------GG------QRQRVALARALLLNPDLL-LLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6320614 1055 GLDSQTAWDTCQLMRKLATHGQAILCTIHQPSaILMQQFDRLLFLQKG 1102
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
912-1102 |
9.50e-20 |
|
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: 89.28 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 912 PGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRDES-----FP---RSIGYC-QQQDL--HLktaTVR 977
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-----GLEKpdgGTIVLNGTVLFDSrkkinLPpqqRKIGLVfQQYALfpHL---NVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 978 ESLRFSAYLRQPSSVSIEeknryVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLD 1057
Cdd:cd03297 94 ENLAFGLKRKRNREDRIS-----VDELLDLLGLDHLLNRYPA----QLSGGEKQRVALARALAAQPELLL-LDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6320614 1058 SQTAWDTCQLMRKLATHGQ--AILCTiHQPSAILMQQfDRLLFLQKG 1102
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNipVIFVT-HDLSEAEYLA-DRIVVMEDG 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
898-1102 |
1.77e-19 |
|
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: 88.43 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITgnIFVDGRLRDESFPRSIG--------Ycqqq 967
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILglIKPDSGEIT--FDGKSYQKNIEALRRIGalieapgfY---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 dLHLktaTVRESLRFSAYLRQpssvsIEEKNryVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLV 1047
Cdd:cd03268 85 -PNL---TARENLRLLARLLG-----IRKKR--IDEVLDVVGLKDSAKKKVK----GFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1048 fLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAIlmQQF-DRLLFLQKG 1102
Cdd:cd03268 150 -LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEI--QKVaDRIGIINKG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
897-1102 |
2.63e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeR---VTmgviTGNIFVDGR-LRD---ESFPRSIGYCqQQDL 969
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL-RfydPT----SGRILIDGVdIRDltlESLRRQIGVV-PQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFSAylrqpSSVSIEEknryVEEVIK-------ILEM-QQYsDAVVGVAGEGLNVEQRKRLTIGVELAA 1041
Cdd:COG1132 424 FLFSGTIRENIRYGR-----PDATDEE----VEEAAKaaqahefIEALpDGY-DTVVGERGVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1042 RPKLLVfLDEPTSGLDSQTAwdtcQL----MRKLaTHGQAILcTI-HQPSAIlmQQFDRLLFLQKG 1102
Cdd:COG1132 494 DPPILI-LDEATSALDTETE----ALiqeaLERL-MKGRTTI-VIaHRLSTI--RNADRILVLDDG 550
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
898-1071 |
3.31e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 88.50 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR----LRDE---SFPRSIGYCQQQ 967
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----GLLRpdsGEILVDGQditgLSEKelyELRRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 -----DLhlktaTVRESLRFsaYLRQPSSVSIEEKNRYVEEVikiLEMqqysdavVGVAGeglnVE----------QRKR 1032
Cdd:COG1127 91 galfdSL-----TVFENVAF--PLREHTDLSEAEIRELVLEK---LEL-------VGLPG----AAdkmpselsggMRKR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6320614 1033 ltigVELA----ARPKLLvFLDEPTSGLDSQTAWDTCQLMRKL 1071
Cdd:COG1127 150 ----VALAralaLDPEIL-LYDEPTAGLDPITSAVIDELIREL 187
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
901-1079 |
3.32e-19 |
|
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: 88.94 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR----LRdesfPRSIgyCQQ------Q 967
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYRptsGRILFDGRditgLP----PHRI--ARLgiartfQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 DLHL-KTATVRESLR-----------FSAYLRQPSSVSIEEKNR-YVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLT 1034
Cdd:COG0411 87 NPRLfPELTVLENVLvaaharlgrglLAALLRLPRARREEREAReRAEELLERVGLADRADEPAG----NLSYGQQRRLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6320614 1035 IGVELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAIL 1079
Cdd:COG0411 163 IARALATEPKLL-LLDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
881-1102 |
4.29e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 92.66 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 881 EAIFHWRDLCYDVPikGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTM-GVITGNIFVDGR----LRDE 955
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHgGRISGEVLLDGRdlleLSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 956 SFPRSIGYC-QQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLT 1034
Cdd:COG1123 80 LRGRRIGMVfQDPMTQLNPVTVGDQIAEALENLGLSRAEARAR---VLELLEAVGLERRLDRYPHQLSGG----QRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1035 IGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:COG1123 153 IAMALALDPDLLI-ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVA-EIADRVVVMDDG 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
897-1099 |
4.58e-19 |
|
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: 92.73 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDGRLRDE----SFPRSIGYCQQQDlHLK 972
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVPLADadadSWRDQIAWVPQHP-FLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFsaYLRQPSSVSIEEKNR--YVEEVIKILEmqQYSDAVVGVAGEGLNVEQRKRLTIGVELaARPKLLVFLD 1050
Cdd:TIGR02857 409 AGTIAENIRL--ARPDASDAEIREALEraGLDEFVAALP--QGLDTPIGEGGAGLSGGQAQRLALARAF-LRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLAThGQAILCTIHQPSaiLMQQFDRLLFL 1099
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
898-1102 |
1.18e-18 |
|
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: 85.32 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDG----RLRDESFP--RSIGYCQQQDL 969
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPD----SGSILIDGedltDLEDELPPlrRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFsaylrqpssvsieeknryveevikilemqqysdavvgvageGLNVEQRKRLTIGVELAARPKLLvFL 1049
Cdd:cd03229 87 LFPHLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVL-LL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPS-AILMQqfDRLLFLQKG 1102
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDeAARLA--DRVVVLRDG 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
897-1102 |
1.39e-18 |
|
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: 84.74 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDGR-LRD---ESFPRSIGYCqQQDL 969
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-----LRLYDptsGEILIDGVdLRDldlESLRKNIAYV-PQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVREslrfsaylrqpssvsieekNryveevikILemqqySdavvgvAGeglnveQRKRLTIGVELAARPKLLVfL 1049
Cdd:cd03228 86 FLFSGTIRE-------------------N--------IL-----S------GG------QRQRIAIARALLRDPPILI-L 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQPSAIlmQQFDRLLFLQKG 1102
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRLSTI--RDADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
902-1103 |
1.70e-18 |
|
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: 86.52 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR-LRD---ESFPRSIGYCqQQDLHLKTATVR 977
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD--VDSGRILIDGHdVRDytlASLRRQIGLV-SQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 978 ESLRFSAylRQPSSVSIEE--KNRYVEEVIKilEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSG 1055
Cdd:cd03251 94 ENIAYGR--PGATREEVEEaaRAANAHEFIM--ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI-LDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6320614 1056 LDSQTAWDTCQLMRKLATHGQAILCTiHQPSAIlmQQFDRLLFLQKGG 1103
Cdd:cd03251 169 LDTESERLVQAALERLMKNRTTFVIA-HRLSTI--ENADRIVVLEDGK 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
896-1102 |
1.45e-17 |
|
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: 83.69 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaerVTMGVIT-GNIFVDGR----LRDESFPRSIGYCQQQDLh 970
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI---QRFYVPEnGRVLVDGHdlalADPAWLRRQVGVVLQENV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKTATVRESLRFSAylRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVFlD 1050
Cdd:cd03252 87 LFNRSIRDNIALAD--PGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF-D 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLAThGQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
887-1109 |
1.47e-17 |
|
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: 83.32 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMG---VITGNIFVDGR-------LRDES 956
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLA-----RAILGllkPTSGSIIFDGKdllklsrRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 FPRSIGYCQQQDLhlkTA-----TVRESLRFSAYLRQPSSVSiEEKNRYVEEVIKILE-----MQQYSDAVVGvageGln 1026
Cdd:cd03257 80 RRKEIQMVFQDPM---SSlnprmTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLVGVGlpeevLNRYPHELSG----G-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1027 veQRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSAIlmQQF-DRLLFLqKGGQ 1104
Cdd:cd03257 150 --QRQRVAIARALALNPKLLI-ADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVV--AKIaDRVAVM-YAGK 223
|
....*
gi 6320614 1105 TVYFG 1109
Cdd:cd03257 224 IVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
892-1113 |
1.48e-17 |
|
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: 83.71 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 892 DVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDG-------RLRDESFPRSI 961
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-----GLLRpdsGEVLIDGedisglsEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 962 GYCQQQ-----DLhlktaTVRESLRFsaYLRQPSSVSIEEKNRYVEEvikILEMqqysdavVGVAGEG------LNVEQR 1030
Cdd:cd03261 80 GMLFQSgalfdSL-----TVFENVAF--PLREHTRLSEEEIREIVLE---KLEA-------VGLRGAEdlypaeLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1031 KRLTIGVELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVYFG 1109
Cdd:cd03261 143 KRVALARALALDPELL-LYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAF-AIADRIAVL-YDGKIVAEG 219
|
....
gi 6320614 1110 DLGE 1113
Cdd:cd03261 220 TPEE 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
898-1113 |
2.07e-17 |
|
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: 83.60 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDgW-VKPGTLTALMGASGAGKTTLLdclaervtmGVITGNIF----VDGRLRDESFP--------RSIGYC 964
Cdd:COG1119 14 GGKTILDDIS-WtVKPGEHWAILGPNGAGKSTLL---------SLITGDLPptygNDVRLFGERRGgedvwelrKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 qQQDLHLK---TATVRESLR--FSAYLRQPSSVSIEEKNRyVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVEL 1039
Cdd:COG1119 84 -SPALQLRfprDETVLDVVLsgFFDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQG----EQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1040 AARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHG--QAILCTiHQPSAILmQQFDRLLFLqKGGQTVYFGDLGE 1113
Cdd:COG1119 158 VKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEEIP-PGITHVLLL-KDGRVVAAGPKEE 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
898-1102 |
3.96e-17 |
|
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: 82.23 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGV-ITGNIFVDGR------LRDESFPRSIGYCQQQD 968
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlNDLIPGApDEGEVLLDGKdiydldVDVLELRRRVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 969 LHLKtATVRESLRFSAYLRQpsSVSIEEKNRYVEEVIKIlemqqysdavVGVAGE--------GLNVEQRKRLTIGVELA 1040
Cdd:cd03260 91 NPFP-GSIYDNVAYGLRLHG--IKLKEELDERVEEALRK----------AALWDEvkdrlhalGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1041 ARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQpsailMQQF----DRLLFLQKG 1102
Cdd:cd03260 158 NEPEVLL-LDEPTSALDPISTAKIEELIAELKKEYTIVIVT-HN-----MQQAarvaDRTAFLLNG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
898-1079 |
6.28e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 81.33 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDGR----LRDESFPRS-IGYCQQQDL 969
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI-----MGLLPprsGSIRFDGRditgLPPHERARAgIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFSAYLRQPSSV--SIEEknryveevikILEM----QQYSDAVVGVAGEGlnveQRKRLTIGVELAARP 1043
Cdd:cd03224 86 IFPELTVEENLLLGAYARRRAKRkaRLER----------VYELfprlKERRKQLAGTLSGG----EQQMLAIARALMSRP 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 6320614 1044 KLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:cd03224 152 KLLL-LDEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
898-1057 |
9.24e-17 |
|
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: 80.70 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGtLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR--LRD-ESFPRSIGYCQQQDLHL 971
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA-----TLTPpssGTIRIDGQdvLKQpQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfLDE 1051
Cdd:cd03264 85 PNFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILI-VDE 156
|
....*.
gi 6320614 1052 PTSGLD 1057
Cdd:cd03264 157 PTAGLD 162
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
910-1109 |
1.20e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 80.49 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGrLRDESFP----RSIGYCQQQDLHLKTATVRESLRF 982
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTL-----RMLAGLLepdAGFATVDG-FDVVKEPaearRRLGFVSDSTGLYDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 983 SAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAW 1062
Cdd:cd03266 102 FAGLY---GLKGDELTARLEELADRLGMEELLDRRVG----GFSTGMRQKVAIARALVHDPPVLL-LDEPTTGLDVMATR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1063 DTCQLMRKLATHGQAILCTIHqpsaiLMQQF----DRLLFLQKgGQTVYFG 1109
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTH-----IMQEVerlcDRVVVLHR-GRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
896-1083 |
1.39e-16 |
|
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: 80.49 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAE--RVTMGviTGNIF-VDGRLRDESFPRSIGYCQQQDLHLK 972
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG--RATVAgHDVVREPREVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFSAYLrqpSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLnveqRKRLTIGVELAARPKLLvFLDEP 1052
Cdd:cd03265 87 ELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 6320614 1053 TSGLDSQT---AWDTCQLMRKlaTHGQAILCTIH 1083
Cdd:cd03265 159 TIGLDPQTrahVWEYIEKLKE--EFGMTILLTTH 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
887-1102 |
1.73e-16 |
|
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: 81.00 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRL----RDESFPRS 960
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPW----SGEVTFDGRPvtrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 961 IGYCQQQ---DLH-LKT--ATVRESLRfsaylrqpssvsIEEKNRYVEEVIKILE--------MQQYSDAVVGvageGln 1026
Cdd:COG1124 81 VQMVFQDpyaSLHpRHTvdRILAEPLR------------IHGLPDREERIAELLEqvglppsfLDRYPHQLSG----G-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1027 veQRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAIlmqQF--DRLLFLQKG 1102
Cdd:COG1124 143 --QRQRVAIARALILEPELLL-LDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVV---AHlcDRVAVMQNG 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
898-1102 |
4.21e-16 |
|
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: 78.73 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GNIFVDGRLRDESFPRS-IGYC-QQQDL--H 970
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINllEEPDSGTIIiDGLKLTDDKKNINELRQkVGMVfQQFNLfpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LktaTVRESLRFSaylrqPSSVSIEEKNRYVEEVIKILEmqqysdaVVGVAGEG------LNVEQRKRLTIGVELAARPK 1044
Cdd:cd03262 91 L---TVLENITLA-----PIKVKGMSKAEAEERALELLE-------KVGLADKAdaypaqLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1045 LLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQpsailMqQF-----DRLLFLQKG 1102
Cdd:cd03262 156 VMLF-DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE-----M-GFarevaDRVIFMDDG 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
887-1085 |
4.85e-16 |
|
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: 83.18 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDG----RLRDESFPR 959
Cdd:TIGR02868 338 RDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-----GLLdplQGEVTLDGvpvsSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYCqQQDLHLKTATVRESLRFSAylrqpSSVSIEEKNRYVEEV---IKILEMQQYSDAVVGVAGEGLNVEQRKRLTIG 1036
Cdd:TIGR02868 410 RVSVC-AQDAHLFDTTVRENLRLAR-----PDATDEELWAALERVglaDWLRALPDGLDTVLGEGGARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6320614 1037 VELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKlATHGQAILCTIHQP 1085
Cdd:TIGR02868 484 RALLADAPILL-LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
47-162 |
4.93e-16 |
|
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins from fungi, plants to higher eukaryotes. It is predicted to be an intracellular domain.
Pssm-ID: 464194 Cd Length: 80 Bit Score: 74.28 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 47 ELARTLTSQSllytansnnssssnhnahnadsrsvfSTDMEGVNPVFTNPDtpgynpklDPNSDqFSSTAWVQNMANICT 126
Cdd:pfam14510 1 ELARILTRQS--------------------------SSSSSSSSPESTDPD--------EEDSE-FDLRKWLKNLRRLID 45
|
90 100 110
....*....|....*....|....*....|....*.
gi 6320614 127 SDPdFYKPYSLGCVWKNLSASGDSADVSYQSTFANI 162
Cdd:pfam14510 46 EDG-YIKPRKLGVAFKNLTVSGVGAGADYQPTVGNA 80
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
891-1106 |
8.92e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.08 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 891 YDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDgrlrDESFPRSigycqqqdlh 970
Cdd:COG2401 34 FGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP----DNQFGRE---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 lktATVRESLrfsaYLRQPssvsieeknryVEEVIKILEMQQYSDAVVGVA--GEgLNVEQRKRLTIGVELAARPKLLVf 1048
Cdd:COG2401 100 ---ASLIDAI----GRKGD-----------FKDAVELLNAVGLSDAVLWLRrfKE-LSTGQKFRFRLALLLAERPKLLV- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKLAT-HG-QAILCTiHQPSAILMQQFDRLLFLQKGGQTV 1106
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARrAGiTLVVAT-HHYDVIDDLQPDLLIFVGYGGVPE 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
158-402 |
1.49e-15 |
|
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: 76.51 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 158 TFANIVPKLLTKGLRLlkpskeedtfQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSIVsyNGLS 237
Cdd:cd03232 5 TWKNLNYTVPVKGGKR----------QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILI--NGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 238 ssdIRKHYRGEVVYNAESDIHLPHLTVYQTLFTVArmktpqnrikgvdreayanhvtevamatyglshtrdtkvgndLVR 317
Cdd:cd03232 73 ---LDKNFQRSTGYVEQQDVHSPNLTVREALRFSA------------------------------------------LLR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 318 GVSGGERKRVSIA-EVAicgAR----FqcWDNATRGLDSATALEFIRALKTQADIGKTAAtVAIYQCSQDAYDLFDKVCV 392
Cdd:cd03232 108 GLSVEQRKRLTIGvELA---AKpsilF--LDEPTSGLDSQAAYNIVRFLKKLADSGQAIL-CTIHQPSASIFEKFDRLLL 181
|
250
....*....|.
gi 6320614 393 LDDGYQL-YFG 402
Cdd:cd03232 182 LKRGGKTvYFG 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
887-1079 |
3.11e-15 |
|
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: 80.72 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQR-RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR---------LRD 954
Cdd:COG1123 264 RNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLglLRPT----SGSILFDGKdltklsrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 955 esFPRSIGY-CQQQDLHL-KTATVRESLRFSayLRQPSSVSIEEKNRYVEEVIkilemqqysDAVvgvageGLNVE---- 1028
Cdd:COG1123 340 --LRRRVQMvFQDPYSSLnPRMTVGDIIAEP--LRLHGLLSRAERRERVAELL---------ERV------GLPPDladr 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1029 --------QRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAIL 1079
Cdd:COG1123 401 yphelsggQRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDLqRELGLTYL 459
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
901-1083 |
4.44e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 75.15 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLRDES------FPRSIGYC-QQQDLH 970
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN-----GLLrpqSGAVLIDGEPLDYSrkglleRRQRVGLVfQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKTATVRESLRFSaylrqPSSV--SIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVf 1048
Cdd:TIGR01166 81 LFAADVDQDVAFG-----PLNLglSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDVLL- 150
|
170 180 190
....*....|....*....|....*....|....*
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
897-1102 |
4.95e-15 |
|
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: 76.11 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDGR----LRDESFPRSIGYCqQQDL 969
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-----MRFYDpqkGQILIDGIdirdISRKSLRSMIGVV-LQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEmQQYsDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfL 1049
Cdd:cd03254 87 FLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLP-NGY-DTVLGENGGNLSQGERQLLAIARAMLRDPKILI-L 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLaTHGQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTI--KNADKILVLDDG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
897-1109 |
5.83e-15 |
|
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: 76.07 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDG---------RLRdeSFPRSIGYC 964
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN-----GLVEptsGSVLIDGtdinklkgkALR--QLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQdLHL-KTATVRESLRFSAYLRQP------SSVSIEEKNRyveeVIKILEMQQYSDAVVGVAGEgLNVEQRKRLTIGV 1037
Cdd:cd03256 84 FQQ-FNLiERLSVLENVLSGRLGRRStwrslfGLFPKEEKQR----ALAALERVGLLDKAYQRADQ-LSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1038 ELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSaILMQQFDRLLFLqKGGQTVYFG 1109
Cdd:cd03256 158 ALMQQPKLIL-ADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVD-LAREYADRIVGL-KDGRIVFDG 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
898-1102 |
9.94e-15 |
|
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: 75.45 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR------LRDesfpRSIGYCQQQDL 969
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPD----SGTILFGGEdatdvpVQE----RNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFSAYLR----QPSSVSIEEKnryVEEVIKILEMQQYSDAVvgvaGEGLNVEQRKRLTIGVELAARPKL 1045
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKprseRPPEAEIRAK---VHELLKLVQLDWLADRY----PAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1046 LVfLDEPTSGLDSQTAWDTCQLMRKL--ATHGQAILCTIHQPSAilMQQFDRLLFLQKG 1102
Cdd:cd03296 158 LL-LDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEA--LEVADRVVVMNKG 213
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
898-1083 |
1.27e-14 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 76.27 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR--LRD-ESFPRSIGYCQQQ---- 967
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLT-----TLLRptsGTARVAGYdvVREpRKVRRSIGIVPQYasvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 -DLhlktaTVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLL 1046
Cdd:TIGR01188 79 eDL-----TGRENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6320614 1047 vFLDEPTSGLDSQTA---WDtcqLMRKLATHGQAILCTIH 1083
Cdd:TIGR01188 147 -FLDEPTTGLDPRTRraiWD---YIRALKEEGVTILLTTH 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
898-1096 |
1.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIfvdgRLRDESFP-------RSIGYCQQQ 967
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTL-----RMLLGLTHpdaGSI----SLCGEPVPsrarharQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 DLHLKTATVRESLR-FSAYLrqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLnveqRKRLTIGVELAARPKLL 1046
Cdd:PRK13537 89 DNLDPDFTVRENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1047 VfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHqpsaiLMQQFDRL 1096
Cdd:PRK13537 161 V-LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH-----FMEEAERL 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
887-1079 |
1.42e-14 |
|
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: 74.43 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITgnifVDGRLRDESfPRSIGYC 964
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAglERPTSGEVL----VDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQDLHLKTATVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDA----VVGvaGeglnveQRKRLTIGVELA 1040
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLSGFENAyphqLSG--G------MRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6320614 1041 ARPKLLvFLDEPTSGLDSQTA---WDtcQLMRKLATHGQAIL 1079
Cdd:cd03293 148 VDPDVL-LLDEPFSALDALTReqlQE--ELLDIWRETGKTVL 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
903-1083 |
2.82e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 73.60 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDG----RLRDESFP---RSIGYCQQQDLHLKTAT 975
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGqdvsDLRGRAIPylrRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 976 VRESLRFSAYLrqpSSVSIEEKNRYVEEVIKILEMQQYSDAVvgvaGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSG 1055
Cdd:cd03292 95 VYENVAFALEV---TGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILI-ADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 6320614 1056 LDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
887-1102 |
3.36e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVpikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRdESFPRsigy 963
Cdd:COG4559 5 ENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-----GELTpssGEVRLNGRPL-AAWSP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 964 cqqQDLhlktATVReslrfsAYLRQPSSVSIEEKnryVEEVI---------------KILE--MQQysdavVGVA----- 1021
Cdd:COG4559 71 ---WEL----ARRR------AVLPQHSSLAFPFT---VEEVValgraphgssaaqdrQIVReaLAL-----VGLAhlagr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1022 -------GEglnvEQRkrltigVELA-----------ARPKLLvFLDEPTSGLD--SQTAwdTCQLMRKLATHGQAILCT 1081
Cdd:COG4559 130 syqtlsgGE----QQR------VQLArvlaqlwepvdGGPRWL-FLDEPTSALDlaHQHA--VLRLARQLARRGGGVVAV 196
|
250 260
....*....|....*....|..
gi 6320614 1082 IHQPSaiLMQQF-DRLLFLQKG 1102
Cdd:COG4559 197 LHDLN--LAAQYaDRILLLHQG 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
900-1102 |
3.43e-14 |
|
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: 73.80 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVtMGVITGNIFVDGR-LRD---ESFPRSIGYCQQqDLHLKTAT 975
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RF-YDVSSGSILIDGQdIREvtlDSLRRAIGVVPQ-DTVLFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 976 VRESLRFSAylrqpSSVSIEEknryVEEVIK-------ILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLvF 1048
Cdd:cd03253 91 IGYNIRYGR-----PDATDEE----VIEAAKaaqihdkIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL-L 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQPSAILmqQFDRLLFLQKG 1102
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIV--NADKIIVLKDG 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
887-1102 |
3.78e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.36 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFPRsIGYC 964
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAglEKPT----SGEVLVDGKPVTGPGPD-RGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQDLHLKTATVRESLRFSAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAVV-----GvageglnveQRKRLTIGVEL 1039
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRG---VPKAERRERARELLELVGLAGFEDAYPhqlsgG---------MRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1040 AARPKLLvFLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPS-AILMQqfDRLLFLQKG 1102
Cdd:COG1116 154 ANDPEVL-LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDeAVFLA--DRVVVLSAR 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
898-1113 |
4.83e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDGRLRDESFPRSIGYcqqqdlhL--- 971
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILApdsGEVLWDGEPLDPEDRRRIGY-------Lpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 ----KTATVRESLRFSAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAvvgvageglNVE------QRKrltigVELAA 1041
Cdd:COG4152 80 rglyPKMKVGEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANK---------KVEelskgnQQK-----VQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1042 ----RPKLLVfLDEPTSGLD---SQTAWDtcqLMRKLATHGQAILCTIHQpsailMQQFDRL---LFLQKGGQTVYFGDL 1111
Cdd:COG4152 143 allhDPELLI-LDEPFSGLDpvnVELLKD---VIRELAAKGTTVIFSSHQ-----MELVEELcdrIVIINKGRKVLSGSV 213
|
..
gi 6320614 1112 GE 1113
Cdd:COG4152 214 DE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
897-1102 |
5.44e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLD--CLAERVTmgviTGNIFVDG----RLRDESFP---RSIGYCqQQ 967
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKllYGEERPT----SGQVLVNGqdlsRLKRREIPylrRRIGVV-FQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 DLHL-KTATVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGV--AGEglnveqRKRLTIGVELAARPK 1044
Cdd:COG2884 87 DFRLlPDRTVYENVALPLRVTGKSRKEIRRR---VREVLDLVGLSDKAKALPHElsGGE------QQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1045 LLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSaiLMQQFD-RLLFLQKG 1102
Cdd:COG2884 158 LLL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
902-1102 |
6.58e-14 |
|
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: 72.12 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA-ErvtMGVITGNIFVdgrlrdesfPRSIGYCQQQDLhLKTATVRESL 980
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgE---LEKLSGSVSV---------PGSIAYVSQEPW-IQNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 981 RFSAYLRQPssvsieeknRYvEEVIKI--LE--MQQYSDA---VVGVAGEGLNVEQRKRLTIgvelaAR----PKLLVFL 1049
Cdd:cd03250 87 LFGKPFDEE---------RY-EKVIKAcaLEpdLEILPDGdltEIGEKGINLSGGQKQRISL-----ARavysDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1050 DEPTSGLDSQTA---WDTCqLMRKLATHGQAILCTiHQPSAILmqQFDRLLFLQKG 1102
Cdd:cd03250 152 DDPLSAVDAHVGrhiFENC-ILGLLLNNKTRILVT-HQLQLLP--HADQIVVLDNG 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
896-1071 |
1.06e-13 |
|
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: 72.23 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR---------LRDesFPRSIGYC 964
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINglERPT----SGSVLVDGTdltllsgkeLRK--ARRRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQDLHLKTATVRESLrfsAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPK 1044
Cdd:cd03258 88 FQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGG----QKQRVGIARALANNPK 160
|
170 180
....*....|....*....|....*..
gi 6320614 1045 LLvFLDEPTSGLDSQTAWDTCQLMRKL 1071
Cdd:cd03258 161 VL-LCDEATSALDPETTQSILALLRDI 186
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
897-1104 |
1.13e-13 |
|
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: 70.71 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITgnifVDG----RLRDESFPRSIGYCQQQDLh 970
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILglLRPTSGRVR----LDGadisQWDPNELGDHVGYLPQDDE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKTATVRESlrfsaylrqpssvsieeknryveevikILEmqqysdavvgvAGeglnveQRKRLTIGVELAARPKLLVfLD 1050
Cdd:cd03246 87 LFSGSIAEN---------------------------ILS-----------GG------QRQRLGLARALYGNPRILV-LD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAIlmQQFDRLLFLQKGGQ 1104
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL--ASADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
899-1102 |
1.51e-13 |
|
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: 71.47 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDG---RLRDESFPRS-IGYCqQQDLHL 971
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLL-----KLLAGLYKptsGSVLLDGtdiRQLDPADLRRnIGYV-PQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAylrqpSSVSIEEknryVEEVIKILEMQQYS-------DAVVGVAGEGLNVEQRKRLTIGVELAARPK 1044
Cdd:cd03245 90 FYGTLRDNITLGA-----PLADDER----ILRAAELAGVTDFVnkhpnglDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 1045 LLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQPSaiLMQQFDRLLFLQKG 1102
Cdd:cd03245 161 IL-LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT-HRPS--LLDLVDRIIVMDSG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
898-1106 |
1.64e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMG-VITGNIFVDGRLRDESFPR-SIGYCQQQDLHLKT 973
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGdLIVDGLKVNDPKVDERLIRqEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAylRQPSSVSIEEKNRYVEEVIkilemqqysdAVVGVAGEG------LNVEQRKRLTIGVELAARPKLLV 1047
Cdd:PRK09493 92 LTALENVMFGP--LRVRGASKEEAEKQARELL----------AKVGLAERAhhypseLSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1048 FlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQpSAILMQQFDRLLFLQKGGQTV 1106
Cdd:PRK09493 160 F-DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE-IGFAEKVASRLIFIDKGRIAE 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
193-396 |
2.38e-13 |
|
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: 70.57 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNG--LSSSDIRKHYR--GEVVYNAESDIHLPhlTVYQTL 268
Cdd:cd03225 24 IKKGEFVLIVGPNGSGKSTLLRLLN----GLLGPTSGEVLVDGkdLTKLSLKELRRkvGLVFQNPDDQFFGP--TVEEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 269 -FTVARMKTPQNRIKGVDREayanhvtevAMATYGLSHTRDTKVgNDLvrgvSGGERKRVSIAEVAICGARFQCWDNATR 347
Cdd:cd03225 98 aFGLENLGLPEEEIEERVEE---------ALELVGLEGLRDRSP-FTL----SGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 348 GLDSATALEFIRALKTQADIGKTAATVaiyqcSQD---AYDLFDKVCVLDDG 396
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIV-----THDldlLLELADRVIVLEDG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
916-1059 |
2.72e-13 |
|
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: 73.21 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 916 TALMGASGAGKTTLLDCLA--ERVTMGVIT--GNIFVDGRlRDESFP---RSIGYCQQQDL---HLktaTVRESLRFsAY 985
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAglERPDSGRIRlgGEVLQDSA-RGIFLPphrRRIGYVFQEARlfpHL---SVRGNLLY-GR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 986 LRQPSSVSIEEknryVEEVIKILE----MQQYSDAVVGvaGEglnveqRKRLTIGVELAARPKLLVfLDEPTSGLDSQ 1059
Cdd:COG4148 103 KRAPRAERRIS----FDEVVELLGighlLDRRPATLSG--GE------RQRVAIGRALLSSPRLLL-MDEPLAALDLA 167
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
898-1083 |
3.55e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMgvITGNIFVDGR----LRDESFPRSIGYCQQQDLHLKT 973
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDKpismLSSRQLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVREslrFSAYLRQP-----SSVSIEEKNRyVEEVIKILEMQQYSDAVVgvagEGLNVEQRKRLTIGVELAARPKlLVF 1048
Cdd:PRK11231 91 ITVRE---LVAYGRSPwlslwGRLSAEDNAR-VNQAMEQTRINHLADRRL----TDLSGGQRQRAFLAMVLAQDTP-VVL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
898-1076 |
5.17e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.44 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR--LRDESFPRSIGYCQQQDL---H 970
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPD----SGRILLDGRdvTGLPPEKRNVGMVFQDYAlfpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LktaTVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVV----GvageglnvEQRKRltigVELA----AR 1042
Cdd:COG3842 92 L---TVAENVAFGLRMRGVPKAEIRAR---VAELLELVGLEGLADRYPhqlsG--------GQQQR----VALAralaPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6320614 1043 PKLLvFLDEPTSGLD----SQTAWDTCQLMRKL------ATHGQ 1076
Cdd:COG3842 154 PRVL-LLDEPLSALDaklrEEMREELRRLQRELgitfiyVTHDQ 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
892-1083 |
6.49e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 892 DVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDGRLRDESFPRSIGYcqqqd 968
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLTptaGTVLVAGDDVEALSARAASR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 969 lhlKTATVRE--SLRFSAYLRQ-------PS----SVSIEEKNRYVEEVIKILEMQQYSD-AVVGVAGeglnvEQRKRLT 1034
Cdd:PRK09536 78 ---RVASVPQdtSLSFEFDVRQvvemgrtPHrsrfDTWTETDRAAVERAMERTGVAQFADrPVTSLSG-----GERQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1035 IGVELA-ARPKLLvfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK09536 150 LARALAqATPVLL--LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
910-1150 |
8.19e-13 |
|
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: 73.89 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR--LRDES-FPRSIGYCQQQDLHLKTATVRESLRFSAYL 986
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKsiLTNISdVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 987 RqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKlLVFLDEPTSGLDSQTA---WD 1063
Cdd:TIGR01257 2040 R---GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPP-LVLLDEPTTGMDPQARrmlWN 2111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1064 TcqlMRKLATHGQAILCTIHQpsailMQQFD----RLLFLQKGGQTvyfgdlgegCKTMIDYFESKGAH--------KCP 1131
Cdd:TIGR01257 2112 T---IVSIIREGRAVVLTSHS-----MEECEalctRLAIMVKGAFQ---------CLGTIQHLKSKFGDgyivtmkiKSP 2174
|
250 260
....*....|....*....|....
gi 6320614 1132 -----PDANPAEWMLEvvGAAPGS 1150
Cdd:TIGR01257 2175 kddllPDLNPVEQFFQ--GNFPGS 2196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
898-1056 |
8.75e-13 |
|
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: 69.63 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGNIFVDGR----LRDESFPRS-IGYCQQ--- 966
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI-----SGLLpprSGSIRFDGEditgLPPHRIARLgIGYVPEgrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 967 --QDLhlktaTVRESLRFSAYLRqPSSVSIEEKnryVEEVikiLEM---------QQysdavvgvAGE---GlnveQRKR 1032
Cdd:COG0410 89 ifPSL-----TVEENLLLGAYAR-RDRAEVRAD---LERV---YELfprlkerrrQR--------AGTlsgG----EQQM 144
|
170 180
....*....|....*....|....
gi 6320614 1033 LTIGVELAARPKLLVfLDEPTSGL 1056
Cdd:COG0410 145 LAIGRALMSRPKLLL-LDEPSLGL 167
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
898-1102 |
9.25e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRrILNNVDGWVKPGTLTALMGASGAGKTTLLDC--LAERVTMGVIT-GNIFVDGrlrdesfPRSIGycQQQDLhlkta 974
Cdd:PRK11264 15 GQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDT-------ARSLS--QQKGL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 tVREslrfsayLRQPSSVSIEEKNRY-----VEEVIK---ILEMQQYSDAV---------VGVAGEG------LNVEQRK 1031
Cdd:PRK11264 80 -IRQ-------LRQHVGFVFQNFNLFphrtvLENIIEgpvIVKGEPKEEATararellakVGLAGKEtsyprrLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1032 RLTIGVELAARPKLLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSaILMQQFDRLLFLQKG 1102
Cdd:PRK11264 152 RVAIARALAMRPEVILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS-FARDVADRAIFMDQG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
902-1060 |
1.74e-12 |
|
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: 68.72 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDcLAERVtMGVITGNIFVDG-RLRD---ESFPRSIGYCqQQDLHLKTATVR 977
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVS-LLERF-YDPTSGEILLDGvDIRDlnlRWLRSQIGLV-SQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 978 ESLRFSAYlrQPSSVSIEE--KNRYVEEVIKILeMQQYsDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSG 1055
Cdd:cd03249 95 ENIRYGKP--DATDEEVEEaaKKANIHDFIMSL-PDGY-DTLVGERGSQLSGGQKQRIAIARALLRNPKILL-LDEATSA 169
|
....*
gi 6320614 1056 LDSQT 1060
Cdd:cd03249 170 LDAES 174
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
898-1077 |
2.33e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFP--RSIGYC-QQQDL--H 970
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAglEDPT----SGEILIGGRDVTDLPPkdRNIAMVfQSYALypH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LktaTVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSD----AVVGvaGeglnveQRKRLTIGVELAARPKll 1046
Cdd:COG3839 90 M---TVYENIAFPLKLRKVPKAEIDRR---VREAAELLGLEDLLDrkpkQLSG--G------QRQRVALGRALVREPK-- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6320614 1047 VFL-DEPTSGLDSQTAWDTCQLMRKL----------ATHGQA 1077
Cdd:COG3839 154 VFLlDEPLSNLDAKLRVEMRAEIKRLhrrlgtttiyVTHDQV 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
900-1083 |
2.54e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDgrlrDESFP---------RSIGYCQQQ 967
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTF-----YMVVGIVprdAGNIIID----DEDISllplhararRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 DLHLKTATVRESLRfsAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVvgvaGEGLNVEQRKRLTIGVELAARPKlLV 1047
Cdd:PRK10895 87 ASIFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPK-FI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 6320614 1048 FLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
898-1057 |
3.23e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 67.28 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFP--RSIGYCQQQDLHLKT 973
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPT----SGRIYIGGRDVTDLPPkdRDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDER---VREVAELLQIEHLLDRKPKQLSGG----QRQRVALGRAIVREPKVFL-MDEPL 158
|
....
gi 6320614 1054 SGLD 1057
Cdd:cd03301 159 SNLD 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
887-1102 |
6.89e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.49 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVpikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR-LRDesFPRsigycq 965
Cdd:PRK13548 6 RNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS--PDSGEVRLNGRpLAD--WSP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 966 qQDLhlktATVReslrfsAYLRQPSSVSIEEKnryVEEVIkilEM------------QQYSDAV---VGVA--------- 1021
Cdd:PRK13548 72 -AEL----ARRR------AVLPQHSSLSFPFT---VEEVV---AMgraphglsraedDALVAAAlaqVDLAhlagrdypq 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1022 ---GEglnvEQRkrltigVELA----------ARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIHQPSa 1087
Cdd:PRK13548 135 lsgGE----QQR------VQLArvlaqlwepdGPPRWL-LLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLN- 202
|
250
....*....|....*.
gi 6320614 1088 iLMQQF-DRLLFLQKG 1102
Cdd:PRK13548 203 -LAARYaDRIVLLHQG 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
910-1102 |
8.41e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLaervtMGVI--TGNIFVDGR-LRD---ESFPRSIGYCqQQDLHLKTATVRESLRfs 983
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNAL-----LGFLpyQGSLKINGIeLREldpESWRKHLSWV-GQNPQLPHGTLRDNVL-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 984 ayLRQPsSVSIEE-----KNRYVEEVIKILEmqQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLDS 1058
Cdd:PRK11174 445 --LGNP-DASDEQlqqalENAWVSEFLPLLP--QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL-LDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6320614 1059 QTAWdtcQLMRKL--ATHGQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:PRK11174 519 HSEQ---LVMQALnaASRRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
185-371 |
1.04e-11 |
|
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: 65.96 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 185 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSI---SSNSHGfkiakdsIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPH 261
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILaglLPPSAG-------EVLWNGEPIRDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 262 LTVYQTLFTVARMKTPQnrikgVDREAyanhvTEVAMATYGLSHTRDTKVGNdLvrgvSGGERKRVSIAEVAICGARfqC 341
Cdd:COG4133 90 LTVRENLRFWAALYGLR-----ADREA-----IDEALEAVGLAGLADLPVRQ-L----SAGQKRRVALARLLLSPAP--L 152
|
170 180 190
....*....|....*....|....*....|..
gi 6320614 342 W--DNATRGLDSATALEFIRALKTQADIGKTA 371
Cdd:COG4133 153 WllDEPFTALDAAGVALLAELIAAHLARGGAV 184
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
898-1083 |
1.24e-11 |
|
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: 66.03 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDG----------RLRdesfpRSIGYC 964
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTF-----YMIVGLVkpdSGKILLDGqditklpmhkRAR-----LGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEM-QQYSDAVVGvaGEglnveqRKRLTIGVELAARP 1043
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLrKSKASSLSG--GE------RRRVEIARALATNP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6320614 1044 KLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:cd03218 153 KFL-LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
898-1085 |
1.28e-11 |
|
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: 65.46 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNIFVDGRLRDEsFPRSIGYCQQQDlHLKTA- 974
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAglLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLP-GLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQPSSVSIEEKnryVEEVikilEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEPTS 1054
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDA---LAAV----GLTGFEDLPAAQLSAG----QQRRLALARLWLSRRPLWI-LDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 6320614 1055 GLDSQTAWDTCQLMRKLATHGQAILCTIHQP 1085
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
894-1060 |
1.32e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 894 PIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR---------LRDESfpRSIG 962
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINllERPT----SGSVLVDGVdltalsereLRAAR--RKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 963 YCQQQDLHLKTATVRESLRFSayLRQpSSVSIEEKNRYVEEVIKIlemqqysdavVGVAGEG------LNVEQRKRLTIG 1036
Cdd:COG1135 86 MIFQHFNLLSSRTVAENVALP--LEI-AGVPKAEIRKRVAELLEL----------VGLSDKAdaypsqLSGGQKQRVGIA 152
|
170 180
....*....|....*....|....
gi 6320614 1037 VELAARPKLLvFLDEPTSGLDSQT 1060
Cdd:COG1135 153 RALANNPKVL-LCDEATSALDPET 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
898-1096 |
2.22e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVIT---GNIFVDGR---LRDESFPRSIGYCQQQDLHL 971
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTI-----ARMILGMTSpdaGKITVLGVpvpARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLR-FSAYLRQpssvsieeKNRYVEEVI-KILE---MQQYSDAVVGVAGEGLnveqRKRLTIGVELAARPKLL 1046
Cdd:PRK13536 127 LEFTVRENLLvFGRYFGM--------STREIEAVIpSLLEfarLESKADARVSDLSGGM----KRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1047 VfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHqpsaiLMQQFDRL 1096
Cdd:PRK13536 195 I-LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEEAERL 238
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
898-1085 |
3.25e-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: 64.44 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNIFVDGRLRDeSFPRSIGYCQQQDlHLKTA- 974
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAglSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAP-GIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQPSSVsieeknryvEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEPTS 1054
Cdd:cd03231 89 SVLENLRFWHADHSDEQV---------EEALARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 6320614 1055 GLDSQTAWDTCQLMRKLATHGQAILCTIHQP 1085
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
883-1083 |
5.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.10 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 883 IFHWRDLCYDVPiKGGQrrILNNVDGWVKPGTLTALMGASGAGKTTLLdcLAERVTMGVITGNIFVDGRLRDES------ 956
Cdd:PRK13639 1 ILETRDLKYSYP-DGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLF--LHFNGILKPTSGEVLIKGEPIKYDkkslle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 FPRSIGYC-QQQDLHLKTATVRESLRFSaylrqPSSV--SIEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKRL 1033
Cdd:PRK13639 76 VRKTVGIVfQNPDDQLFAPTVEEDVAFG-----PLNLglSKEEVEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1034 TIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK13639 147 AIAGILAMKPEIIV-LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
144-370 |
5.70e-11 |
|
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: 67.00 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 144 LSASGDSADVSY--QSTFANIVPKLLTKGLRLLKPSKEEdtfqILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnsh 221
Cdd:TIGR02868 311 LDAAGPVAEGSApaAGAVGLGKPTLELRDLSAGYPGAPP----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLA---- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 222 GFKIAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTVYQTLFTVARMKTPQNRIKGVDREAYANHVTEvamaty 301
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRA------ 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 302 gLSHTRDTKVGNDLVRgVSGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALkTQADIGKT 370
Cdd:TIGR02868 457 -LPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRT 522
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
193-353 |
6.89e-11 |
|
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: 63.68 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSIS---SNSHGFkiakdsiVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTVYQTLF 269
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTgelRPTSGT-------AYINGYSIRTDRKAARQSLGYCPQFDALFDELTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 270 TVARmktpqnrIKGVdREAYANHVTEVAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAeVAICGA-RFQCWDNATRG 348
Cdd:cd03263 98 FYAR-------LKGL-PKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLA-IALIGGpSVLLLDEPTSG 163
|
....*
gi 6320614 349 LDSAT 353
Cdd:cd03263 164 LDPAS 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
883-1083 |
1.02e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 883 IFHWRDLCYDVPikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLRDES--- 956
Cdd:PRK13636 5 ILKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN-----GILkpsSGRILFDGKPIDYSrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 ---FPRSIGYC-QQQDLHLKTATVRESLRFSAY-LRQPSsvsiEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRK 1031
Cdd:PRK13636 77 lmkLRESVGMVfQDPDNQLFSASVYQDVSFGAVnLKLPE----DEVRKRVDNALKRTGIEHLKDK----PTHCLSFGQKK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1032 RLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATH-GQAILCTIH 1083
Cdd:PRK13636 149 RVAIAGVLVMEPKVLV-LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
903-1079 |
1.51e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRDESFPR-------SIGYcqqQDLHL- 971
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVYQpdsGEILLDGEPVRFRSPRdaqaagiAIIH---QELNLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfLDE 1051
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSRDARVLI-LDE 166
|
170 180 190
....*....|....*....|....*....|.
gi 6320614 1052 PTSGLDSQtawDTCQL---MRKLATHGQAIL 1079
Cdd:COG1129 167 PTASLTER---EVERLfriIRRLKAQGVAII 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
898-1084 |
1.83e-10 |
|
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: 62.64 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGR--LRDESFPRSIGYC-QQQDL--H 970
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfETPT----SGEILLDGKdiTNLPPHKRPVNTVfQNYALfpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LktaTVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVgvagEGLNVEQRKRLTIGVELAARPKLLVfLD 1050
Cdd:cd03300 87 L---TVFENIAFGLRLKKLPKAEIKER---VAEALDLVQLEGYANRKP----SQLSGGQQQRVAIARALVNEPKVLL-LD 155
|
170 180 190
....*....|....*....|....*....|....
gi 6320614 1051 EPTSGLDsqtawdtcqlmRKLATHGQAILCTIHQ 1084
Cdd:cd03300 156 EPLGALD-----------LKLRKDMQLELKRLQK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
898-1079 |
1.88e-10 |
|
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: 60.91 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRlrdesfPRSIgycqqqdlhlktA 974
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYKpdsGEILVDGK------EVSF------------A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRfsaylrqpssvsieeknryveevikilemqqysdavvgvAGEG----LNVEQRKRLTIGVELAARPKLLVfLD 1050
Cdd:cd03216 68 SPRDARR---------------------------------------AGIAmvyqLSVGERQMVEIARALARNARLLI-LD 107
|
170 180
....*....|....*....|....*....
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVI 136
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
902-1102 |
2.31e-10 |
|
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: 62.13 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVTMgVITGNIFVDG---------RLRdesfpRSIGYCqQQDLHLK 972
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVE-LSSGSILIDGvdiskiglhDLR-----SRISII-PQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLR-FSAYlrqpssvSIEEKNRYVEEV--IKILEMQQYS-DAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVf 1048
Cdd:cd03244 91 SGTIRSNLDpFGEY-------SDEELWQALERVglKEFVESLPGGlDTVVEEGGENLSVGQRQLLCLARALLRKSKILV- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1049 LDEPTSGLDSQTAwdtcQLMRKL---ATHGQAILCTIHQPSAILmqQFDRLLFLQKG 1102
Cdd:cd03244 163 LDEATASVDPETD----ALIQKTireAFKDCTVLTIAHRLDTII--DSDRILVLDKG 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
900-1102 |
3.45e-10 |
|
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: 61.72 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERVTMgVITGNIFVDGrlrdesfpRSIGYCQQQDLHLKTATV-RE 978
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-ENFYQ-PQGGQVLLDG--------KPISQYEHKYLHSKVSLVgQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 979 SLRFSAYLRQPSSVSIEEKN--RYVEEVIK------ILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLD 1050
Cdd:cd03248 97 PVLFARSLQDNIAYGLQSCSfeCVKEAAQKahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI-LD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLATHgQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV--ERADQILVLDGG 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
903-1059 |
4.63e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.32 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGrlRDES----FPRSIGYCQQQDLHLKTATV 976
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPT----AGQIMLDG--VDLShvppYQRPINMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 977 RESLRFSayLRQPSSVSIEEKNRyVEEVIKILEMQQYSdavvGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGL 1056
Cdd:PRK11607 109 EQNIAFG--LKQDKLPKAEIASR-VNEMLGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLL-LDEPMGAL 180
|
...
gi 6320614 1057 DSQ 1059
Cdd:PRK11607 181 DKK 183
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
887-1126 |
5.31e-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: 60.62 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVpikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGrlrdesfprsigycqq 966
Cdd:cd03217 4 KDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 967 QDLhlktatvreslrfsaylrqpSSVSIEEKNRyveevIKILEMQQYSDAVVGVA--------GEGLNVEQRKRLTIGVE 1038
Cdd:cd03217 64 EDI--------------------TDLPPEERAR-----LGIFLAFQYPPEIPGVKnadflryvNEGFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1039 LAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGgqTVyfgdLGEGCKTM 1118
Cdd:cd03217 119 LLLEPDLAI-LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDG--RI----VKSGDKEL 191
|
....*...
gi 6320614 1119 IDYFESKG 1126
Cdd:cd03217 192 ALEIEKKG 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
898-1102 |
5.53e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMGVITGNIFVDGRLRDESfprsiGYCQQQDLH-LKTA 974
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPSEGSIVVNGQTINLVRDKD-----GQLKVADKNqLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAY------------LRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAAR 1042
Cdd:PRK10619 91 RTRLTMVFQHFnlwshmtvlenvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1043 PKLLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQpsailmQQFDR-----LLFLQKG 1102
Cdd:PRK10619 171 PEVLLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE------MGFARhvsshVIFLHQG 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
892-1109 |
7.26e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 892 DVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTM---GVITGNIFVDGR---------LRdesfpR 959
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypeARVSGEVYLDGQdifkmdvieLR-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYCQQQDLHLKTATVRESLRFSAYLRQpssvSIEEKNRYVEEVIKILEMQQYSDAV---VGVAGEGLNVEQRKRLTIG 1036
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNR----LVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1037 VELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFlqkGGQTVYFG 1109
Cdd:PRK14247 159 RALAFQPEVLL-ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLY---KGQIVEWG 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
898-1085 |
7.97e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNifvDGRLRDESFPRSIGYCQQQDLhLKTA- 974
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAglLPPAAGTIKLD---GGDIDDPDVAEACHYLGHRNA-MKPAl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQPSSVSIeeknryvEEVIKILEMQqysdAVVGVAGEGLNVEQRKRLTIgvelaARpkLLVF------ 1048
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDI-------AAALEAVGLA----PLAHLPFGYLSAGQKRRVAL-----AR--LLVSnrpiwi 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6320614 1049 LDEPTSGLDSqtawDTCQLM-----RKLATHGQAILCTiHQP 1085
Cdd:PRK13539 151 LDEPTAALDA----AAVALFaelirAHLAQGGIVIAAT-HIP 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
903-1057 |
8.80e-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: 60.81 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRL---RDESFPRSIGYCQQQ------DLh 970
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-----GLLQptsGEVRVAGLVpwkRRKKFLRRIGVVFGQktqlwwDL- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 lktaTVRESLRFsayLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVgvagEGLNVEQRKRLTIGVELAARPKLLvFLD 1050
Cdd:cd03267 111 ----PVIDSFYL---LAAIYDLPPARFKKRLDELSELLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEIL-FLD 178
|
....*..
gi 6320614 1051 EPTSGLD 1057
Cdd:cd03267 179 EPTIGLD 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
887-1057 |
1.03e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVpikgGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMG-----VITGNIFVDGR--LRDESFPR 959
Cdd:COG0396 4 KNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLA-----KVLMGhpkyeVTSGSILLDGEdiLELSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 S---IGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEM-QQYSDavvgvagEGLNVE----QRK 1031
Cdd:COG0396 75 AragIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLD-------RYVNEGfsggEKK 147
|
170 180
....*....|....*....|....*..
gi 6320614 1032 RLTIgVELAAR-PKLLVfLDEPTSGLD 1057
Cdd:COG0396 148 RNEI-LQMLLLePKLAI-LDETDSGLD 172
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
898-1058 |
1.10e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGrlrDESFPRSIgycQQQDLhlktat 975
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAglEKPT----EGQIFIDG---EDVTHRSI---QQRDI------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 976 vreSLRFSAYLRQPS--------------SVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAA 1041
Cdd:PRK11432 81 ---CMVFQSYALFPHmslgenvgyglkmlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG----QQQRVALARALIL 153
|
170
....*....|....*..
gi 6320614 1042 RPKLLVFlDEPTSGLDS 1058
Cdd:PRK11432 154 KPKVLLF-DEPLSNLDA 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
184-396 |
1.10e-09 |
|
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: 58.80 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 184 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKH-YRGEVVYnaesdihLPHL 262
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA----GLLKPTSGEILIDGKDIAKLPLEeLRRRIGY-------VPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 263 tvyqtlftvarmktpqnrikgvdreayanhvtevamatyglshtrdtkvgndlvrgvSGGERKRVSIAeVAICG-ARFQC 341
Cdd:cd00267 82 ---------------------------------------------------------SGGQRQRVALA-RALLLnPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 342 WDNATRGLDSATALEFIRALKTQADIGKTAATVAIYQcsQDAYDLFDKVCVLDDG 396
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDP--ELAELAADRVIVLKDG 156
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
897-1102 |
1.13e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 897 GGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERV---TMGVITgnifVDG-RLRD---ESFPRSIGYCQQQDL 969
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVfdpQSGRIL----IDGtDIRTvtrASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 hLKTATVRESLRfsayLRQPSSVSieeknryvEEVIKILEMQQYSD----------AVVGVAGEGLNVEQRKRLTIGVEL 1039
Cdd:PRK13657 420 -LFNRSIEDNIR----VGRPDATD--------EEMRAAAERAQAHDfierkpdgydTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1040 AARPKLLVfLDEPTSGLDSQT------AWDTcqLMrklatHGQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:PRK13657 487 LKDPPILI-LDEATSALDVETeakvkaALDE--LM-----KGRTTFIIAHRLSTV--RNADRILVFDNG 545
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
903-1102 |
1.71e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT--GNIFVDGR-LRDESFP---RSIGYCQQQDLHLKTATV 976
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-----GLLPgqGEILLNGRpLSDWSAAelaRHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 977 RESLRfsayLRQPSSVSIEEKNRYVEEVIKILE--------MQQYSdavvgvAGEglnvEQRKRLT-----IGVELAARP 1043
Cdd:COG4138 87 FQYLA----LHQPAGASSEAVEQLLAQLAEALGledklsrpLTQLS------GGE----WQRVRLAavllqVWPTINPEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1044 KLLVfLDEPTSGLD--SQTAWDTcqLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:COG4138 153 QLLL-LDEPMNSLDvaQQAALDR--LLRELCQQGITVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
887-1088 |
1.89e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYdvpIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDG----RLRDESFPR 959
Cdd:PRK13652 7 RDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLF-----RHFNGILKptsGSVLIRGepitKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 960 SIGYC-QQQDLHLKTATVRESLRFSaylrqPSSVSIEE---KNRyVEEVIKILEMQQYSDAVvgvaGEGLNVEQRKRLTI 1035
Cdd:PRK13652 79 FVGLVfQNPDDQIFSPTVEQDIAFG-----PINLGLDEetvAHR-VSSALHMLGLEELRDRV----PHHLSGGEKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1036 GVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIHQPSAI 1088
Cdd:PRK13652 149 AGVIAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDLV 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
901-1102 |
2.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAE--RVTMGVI-TGNIFVDGRLRDESFP---RSIGYC-QQQDLHLKT 973
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVtVGDIVVSSTSKQKEIKpvrKKVGVVfQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAylrQPSSVSIEEKNRYVEEVikiLEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:PRK13643 100 ETVLKDVAFGP---QNFGIPKEKAEKIAAEK---LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV-LDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6320614 1054 SGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAIlMQQFDRLLFLQKG 1102
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDV-ADYADYVYLLEKG 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
910-1057 |
2.51e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR---LRDESFPRSIG--YCQ-QQ---DLhlktaTVR 977
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLT-----GILVptsGEVRVLGYvpfKRRKEFARRIGvvFGQrSQlwwDL-----PAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 978 ESLRfsaYLRQPSSVSIEEKNRYVEEVIKILEMQQYsdavvgvagegLNVEQRKrLTIG----VELAA----RPKLLvFL 1049
Cdd:COG4586 115 DSFR---LLKAIYRIPDAEYKKRLDELVELLDLGEL-----------LDTPVRQ-LSLGqrmrCELAAallhRPKIL-FL 178
|
....*...
gi 6320614 1050 DEPTSGLD 1057
Cdd:COG4586 179 DEPTIGLD 186
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
903-1060 |
3.46e-09 |
|
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: 58.89 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLRDESFP--RSIGY-CQQQDL--HLkta 974
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIkpdSGKILLNGKDITNLPPekRDISYvPQNYALfpHM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKIlemqqysDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLvFLDEPTS 1054
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-------DHLLNRKPETLSGGEQQRVAIARALVVNPKIL-LLDEPFS 158
|
....*.
gi 6320614 1055 GLDSQT 1060
Cdd:cd03299 159 ALDVRT 164
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
902-1102 |
4.36e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.28 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAERVtmgviTGNIFVDG-RLRD---ESFPRSIGYCQQQDLhLKTA 974
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPT-----GGQVLLDGvPLVQydhHYLHRQVALVGQEPV-LFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLrfsAY-LRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:TIGR00958 570 SVRENI---AYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6320614 1054 SGLDSQTAWdTCQLMRKLAthGQAILCTIHQPSAIlmQQFDRLLFLQKG 1102
Cdd:TIGR00958 646 SALDAECEQ-LLQESRSRA--SRTVLLIAHRLSTV--ERADQILVLKKG 689
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
185-370 |
4.46e-09 |
|
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: 58.31 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 185 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGF-KIAKDSIvSYNGLSSSDIRKHYrGEVVYNAESDIHLPhLT 263
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL----GLlKPTSGSI-RVFGKPLEKERKRI-GYVPQRRSIDRDFP-IS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 264 VYQTLFTVA-RMKTPQNRIKGVDREAyanhVTEvAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICGARFQCW 342
Cdd:cd03235 87 VRDVVLMGLyGHKGLFRRLSKADKAK----VDE-ALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLL 156
|
170 180
....*....|....*....|....*...
gi 6320614 343 DNATRGLDSATALEFIRALKTQADIGKT 370
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMT 184
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
196-396 |
4.69e-09 |
|
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: 58.19 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 196 GELLVVLGRPGSGCTTLLKSIssnshgFKIAKDS--IVSYNGLSSSDIRK----HYRGEVVYNAESDIHLPHLTVYQTL- 268
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLI------YKEELPTsgTIRVNGQDVSDLRGraipYLRRKIGVVFQDFRLLPDRNVYENVa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 269 FTVarmktpqnRIKGVDREAYANHVTEvAMATYGLSHTRDTkvgndLVRGVSGGERKRVSIAEVAICGARFQCWDNATRG 348
Cdd:cd03292 101 FAL--------EVTGVPPREIRKRVPA-ALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 349 LDSATALEFIRALKtqaDIGKTAATVAIyqcSQDAYDLFD----KVCVLDDG 396
Cdd:cd03292 167 LDPDTTWEIMNLLK---KINKAGTTVVV---ATHAKELVDttrhRVIALERG 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
181-449 |
4.80e-09 |
|
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: 60.69 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 181 DTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISS-NSHGFKIAKDsiVSYNGLSSSDIRKHYRGEVV--YNAESDI 257
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGlLPHGGRISGE--VLLDGRDLLELSEALRGRRIgmVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 258 HLPHLTVY-QTLFTVarmktpqnRIKGVDREAYANHVTEvAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICG 336
Cdd:COG1123 95 QLNPVTVGdQIAEAL--------ENLGLSRAEARARVLE-LLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 337 ARFQCWDNATRGLDSATALEFIRALKT-QADIGKTAatVAIYQCSQDAYDLFDKVCVLDDGYQLYFGPAKDAKKYFQDMG 415
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElQRERGTTV--LLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6320614 416 yyCPPRQTTADFLTSITSPTERII------SKEFIEKGTR 449
Cdd:COG1123 239 --AVPRLGAARGRAAPAAAAAEPLlevrnlSKRYPVRGKG 276
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
182-396 |
4.97e-09 |
|
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: 58.27 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 182 TFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSnshgfkIAK-DS-IVSYNGLS----SSDIRKHYRGEVV----- 250
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG------LDRpTSgEVRVDGTDisklSEKELAAFRRRHIgfvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 251 -YNAesdihLPHLTVYQTLFTVARMKtpqnRIKGVDREAYANHVTEVAmatyGLSHTRDTKVGNdlvrgVSGGERKRVSI 329
Cdd:cd03255 90 sFNL-----LPDLTALENVELPLLLA----GVPKKERRERAEELLERV----GLGDRLNHYPSE-----LSGGQQQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 330 A-------EVAICgarfqcwDNATRGLDSATALEFIRALKTQADIGKTaaTVAIYQCSQDAYDLFDKVCVLDDG 396
Cdd:cd03255 152 AralandpKIILA-------DEPTGNLDSETGKEVMELLRELNKEAGT--TIVVVTHDPELAEYADRIIELRDG 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
878-1083 |
7.91e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 878 SKSEAIFHWRDLCYDVPikggQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDGR----LR 953
Cdd:PRK10575 6 NHSDTTFALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQplesWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 954 DESFPRSIGYCQQQDLHLKTATVREslrFSAYLRQP-----SSVSIEEKNRyVEEVIKILEMQQYSDAVVgvagEGLNVE 1028
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGMTVRE---LVAIGRYPwhgalGRFGAADREK-VEEAISLVGLKPLAHRLV----DSLSGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1029 QRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIH 1083
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLL-LDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
898-1057 |
9.07e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGRLRdesfprsIGYCQQQdLHLKTA 974
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGLVapdEGVIKRNGKLR-------IGYVPQK-LYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 ---TVRESLRFSAYLRQPSSVSIEEKnryvEEVIKILE--MQQYSdavvgvAGEglnveqRKRLTIGVELAARPKLLVfL 1049
Cdd:PRK09544 82 lplTVNRFLRLRPGTKKEDILPALKR----VQAGHLIDapMQKLS------GGE------TQRVLLARALLNRPQLLV-L 144
|
....*...
gi 6320614 1050 DEPTSGLD 1057
Cdd:PRK09544 145 DEPTQGVD 152
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
167-402 |
9.61e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 57.38 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 167 LTKGLRLLKpskeeDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGL-SSSDIRKHY 245
Cdd:cd03266 7 LTKRFRDVK-----KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA----GLLEPDAGFATVDGFdVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 246 RGEVVYNAESDIHlPHLTVYQTLFTVARMktpqnriKGVDREAYANHVTEVAmATYGLSHTRDTKVGndlvrGVSGGERK 325
Cdd:cd03266 78 RRLGFVSDSTGLY-DRLTARENLEYFAGL-------YGLKGDELTARLEELA-DRLGMEELLDRRVG-----GFSTGMRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 326 RVSIAEVAICGARFQCWDNATRGLD---SATALEFIRALKtqaDIGKTaatvaIYQCS---QDAYDLFDKVCVLDDGYQL 399
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDvmaTRALREFIRQLR---ALGKC-----ILFSThimQEVERLCDRVVVLHRGRVV 215
|
...
gi 6320614 400 YFG 402
Cdd:cd03266 216 YEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
898-1059 |
1.01e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNIFVDGRL--RDesfpRSIGYCQQQDLHLKT 973
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQTSGHIRFHGTDVSRLhaRD----RKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYL----RQPSSVSIEEKnryveeVIKILEMQQYSDAVVGVAGEgLNVEQRKRLTIGVELAARPKLLVfL 1049
Cdd:PRK10851 89 MTVFDNIAFGLTVlprrERPNAAAIKAK------VTQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALAVEPQILL-L 160
|
170
....*....|
gi 6320614 1050 DEPTSGLDSQ 1059
Cdd:PRK10851 161 DEPFGALDAQ 170
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
898-1083 |
1.33e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.40 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVtMGVITGNIFVDGR----------------LRdesfprsi 961
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RL-LPPDSGEVLVDGLdvattpsrelakrlaiLR-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 962 gycqqQDLHLKTA-TVRESLRFSaylRQPSS--VSIEEKNRYVEEVIKILEMQ----QYSDAVVGvaGeglnveQRKRLT 1034
Cdd:COG4604 82 -----QENHINSRlTVRELVAFG---RFPYSkgRLTAEDREIIDEAIAYLDLEdladRYLDELSG--G------QRQRAF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1035 IGVELAARPKlLVFLDEPTSGLDSQTAWDTCQLMRKLA-THGQAILCTIH 1083
Cdd:COG4604 146 IAMVLAQDTD-YVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLH 194
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
193-396 |
1.35e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.98 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISSN---SHGFkiakdsiVSYNG-----LSSSDIRKHYR--GeVVYNaesDIHL-PH 261
Cdd:COG2884 25 IEKGEFVFLTGPSGAGKSTLLKLLYGEerpTSGQ-------VLVNGqdlsrLKRREIPYLRRriG-VVFQ---DFRLlPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 262 LTVYqtlftvarmktpQN-----RIKGVDREAYANHVTEVaMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIA------ 330
Cdd:COG2884 94 RTVY------------ENvalplRVTGKSRKEIRRRVREV-LDLVGLSDKAKALPHE-----LSGGEQQRVAIAralvnr 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 331 -EVAICgarfqcwDNATRGLDSATALEFIRALKtqaDIGKTAATVAIyqcSQDAYDLFDK----VCVLDDG 396
Cdd:COG2884 156 pELLLA-------DEPTGNLDPETSWEIMELLE---EINRRGTTVLI---ATHDLELVDRmpkrVLELEDG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
902-1058 |
1.52e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.50 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFP--RSIGYC-QQQDL--HLkta 974
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDIT----SGDLFIGEKRMNDVPPaeRGVGMVfQSYALypHL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLrqpSSVSIEEKNRYVEEVIKILEMqqysDAVVGVAGEGLNVEQRKRLTIGVELAARPKllVFL-DEPT 1053
Cdd:PRK11000 91 SVAENMSFGLKL---AGAKKEEINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPS--VFLlDEPL 161
|
....*
gi 6320614 1054 SGLDS 1058
Cdd:PRK11000 162 SNLDA 166
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
901-1102 |
1.67e-08 |
|
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: 56.27 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDG---------RLRdesfpRSIGyCQQQDLHL 971
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE--AEEGKIEIDGidistipleDLR-----SSLT-IIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLrfsaylrqpssvsiEEKNRYVEEVIKilemqqysdAVVGVAGEGLNVE--QRKRLTIGVELAARPKLLVfL 1049
Cdd:cd03369 94 FSGTIRSNL--------------DPFDEYSDEEIY---------GALRVSEGGLNLSqgQRQLLCLARALLKRPRVLV-L 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLAThGQAILCTIHQPSAILmqQFDRLLFLQKG 1102
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTII--DYDKILVMDAG 199
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1102 |
2.02e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDG----RLRDESFPRSIG--YcqqQDL 969
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-----GSLppdSGSILIDGkdvtKLPEYKRAKYIGrvF---QDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTA---TVRESLRFsAYLRQPS-----SVSIEEKNRYVEEvIKILEM--QQYSDAVVGVAGEGlnveQRKRLTIGVEL 1039
Cdd:COG1101 90 MMGTApsmTIEENLAL-AYRRGKRrglrrGLTKKRRELFREL-LATLGLglENRLDTKVGLLSGG----QRQALSLLMAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1040 AARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQaiLCTI---HQpsailMQQF----DRLLFLQKG 1102
Cdd:COG1101 164 LTKPKLLL-LDEHTAALDPKTAALVLELTEKIVEENN--LTTLmvtHN-----MEQAldygNRLIMMHEG 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
898-1083 |
2.09e-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: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GNIFVDG----------RLRdesfpRSIGYC 964
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTF-----YMIVGLVKpdsGRIFLDGedithlpmhkRAR-----LGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQQ-----DLhlktaTVRESLRFSAYLRQPSSVSIEEKnryVEEVIKILEMQ----QYSDAVVGvaGEglnveqRKRLTI 1035
Cdd:COG1137 84 PQEasifrKL-----TVEDNILAVLELRKLSKKEREER---LEELLEEFGIThlrkSKAYSLSG--GE------RRRVEI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6320614 1036 GVELAARPKLLvFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:COG1137 148 ARALATNPKFI-LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
887-1102 |
2.29e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.68 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPikGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR-LRD--ESFPRSIGY 963
Cdd:PRK11160 342 NNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQGEILLNGQpIADysEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 964 CQQQDLHLKTATVRESL----------RFSAYLRQpssVSIEeknryveeviKILEMQQYSDAVVGVAGEGLNVEQRKRL 1033
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLllaapnasdeALIEVLQQ---VGLE----------KLLEDDKGLNAWLGEGGRQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1034 TIgvelaARPKL----LVFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTiHQpsAILMQQFDRLLFLQKG 1102
Cdd:PRK11160 485 GI-----ARALLhdapLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HR--LTGLEQFDRICVMDNG 549
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
899-1102 |
2.47e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVITGN-------------IFVDGRL-RDESFPRS-IGY 963
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-----GLITGDksagshiellgrtVQREGRLaRDIRKSRAnTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 964 CQQQDLHLKTATVRESLRFSAYLRQP------SSVSIEEKNRYVEEVIKIlEMQQYSDAVVGVAGEGlnveQRKRLTIGV 1037
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRV-GMVHFAHQRVSTLSGG----QQQRVAIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1038 ELAARPKlLVFLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:PRK09984 166 ALMQQAK-VILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYAL-RYCERIVALRQG 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
910-1113 |
2.75e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRDESFP--R--SIGYcQQQDL--HLktaTVRE-- 978
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIA-----GFLPpdsGRILWNGQDLTALPPaeRpvSMLF-QENNLfpHL---TVAQni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 979 SLRFSAYLRqpssVSIEEKNRyveeVIKILEMqqysdavVGVAG------EGLNVEQRKRltigVELA-----ARPKLLv 1047
Cdd:COG3840 93 GLGLRPGLK----LTAEQRAQ----VEQALER-------VGLAGlldrlpGQLSGGQRQR----VALArclvrKRPILL- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1048 fLDEPTSGLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVYFGDLGE 1113
Cdd:COG3840 153 -LDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAA-RIADRVLLV-ADGRIAADGPTAA 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
898-1062 |
3.57e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRdesfprsIGYCQQQDLHLKTA 974
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-----GELEpdsGEVSIPKGLR-------IGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESL------------RFSAYLRQPSSVSiEEKNRYVEEVIKILEMQQYS-DAVVGVAGEGLNVE------------- 1028
Cdd:COG0488 77 TVLDTVldgdaelraleaELEELEAKLAEPD-EDLERLAELQEEFEALGGWEaEARAEEILSGLGFPeedldrpvselsg 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6320614 1029 -QRKRltigVELA----ARPKLLvFLDEPTSGLDSQT-AW 1062
Cdd:COG0488 156 gWRRR----VALArallSEPDLL-LLDEPTNHLDLESiEW 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
898-1085 |
4.11e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDG----RLRDEsfprsigYcqQQDL- 969
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLL-----RILAGLArpdAGEVLWQGepirRQRDE-------Y--HQDLl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 ---HL---KTA-TVRESLRFSAYLRQPSSvsieeknryVEEVIKILE---MQQYSDAVVGV--AGeglnveQRKRltigV 1037
Cdd:PRK13538 78 ylgHQpgiKTElTALENLRFYQRLHGPGD---------DEALWEALAqvgLAGFEDVPVRQlsAG------QQRR----V 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1038 ELA----ARPKLLVfLDEPTSGLDSQ-TAWDTCQLMRKLATHGQAILcTIHQP 1085
Cdd:PRK13538 139 ALArlwlTRAPLWI-LDEPFTAIDKQgVARLEALLAQHAEQGGMVIL-TTHQD 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
902-1102 |
4.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAErvtmgVITGNIFVDGRLRDES----FPRSIGYC-QQQDLHLKT 973
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLE-----AESGQIIIDGDLLTEEnvwdIRHKIGMVfQNPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAylrQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:PRK13650 97 ATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGG----QKQRVAIAGAVAMRPKIII-LDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 1054 SGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILMQqfDRLLFLQKG 1102
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALS--DRVLVMKNG 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
171-396 |
5.14e-08 |
|
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: 55.22 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 171 LRLLKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRGeVV 250
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA----GLERPDSGEILIDGRDVTGVPPERRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 251 YNAESDIHLPHLTVYQTL-FTVarmktpqnRIKGVDREAYANHVTEVAMATyGLSHTRDTKvgndlVRGVSGGERKRVSI 329
Cdd:cd03259 76 MVFQDYALFPHLTVAENIaFGL--------KLRGVPKAEIRARVRELLELV-GLEGLLNRY-----PHELSGGQQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 330 AEVAICGARFQCWDNATRGLDSATALEFIRALK-TQADIGKTAATVAIYQcsQDAYDLFDKVCVLDDG 396
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKeLQRELGITTIYVTHDQ--EEALALADRIAVMNEG 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
913-1110 |
5.43e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 913 GTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRL---RDESFPRS-IGYC-QQQDLHLKTATVRESLRFSA 984
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLLHLN-----GIYLpqrGRVKVMGREvnaENEKWVRSkVGLVfQDPDDQVFSSTVWDDVAFGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 985 ylrQPSSVSIEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDT 1064
Cdd:PRK13647 106 ---VNMGLDKDEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV-LDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6320614 1065 CQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVYFGD 1110
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVL-KEGRVLAEGD 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
910-1102 |
5.46e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT--GNIFVDGR-LRDESFP---RSIGY-CQQQdlhlKTATVRESLRF 982
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMA-----GLLPgsGSIQFAGQpLEAWSAAelaRHRAYlSQQQ----TPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 983 SAyLRQPSSVSIEEKNRYVEEVIKILEM--------QQYSdavvgvAGEGlnveQRKRLTiGVELAARPKL-----LVFL 1049
Cdd:PRK03695 90 LT-LHQPDKTRTEAVASALNEVAEALGLddklgrsvNQLS------GGEW----QRVRLA-AVVLQVWPDInpagqLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1050 DEPTSGLD--SQTAWDtcQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:PRK03695 158 DEPMNSLDvaQQAALD--RLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
912-1120 |
6.06e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 912 PGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLRDESfPRSIGYCQQQ--------DLHLKTATVRESL 980
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS-----GLLrpqKGAVLWQGKPLDYS-KRGLLALRQQvatvfqdpEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 981 RFSayLRQpSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEPTSGLDSQT 1060
Cdd:PRK13638 100 AFS--LRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG----QKKRVAIAGALVLQARYLL-LDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1061 AWDTCQLMRKLATHGQAILCTIHQPSaiLMQQFDRLLFLQKGGQTVYFGDLGE--GCKTMID 1120
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDID--LIYEISDAVYVLRQGQILTHGAPGEvfACTEAME 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
902-1102 |
6.39e-08 |
|
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: 54.24 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLdclaervtmGVITGNIFVD-GRLRDESFPRSIGYCQ--------QQDLHLK 972
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLL---------QLLTGDLKPQqGEITLDGVPVSDLEKAlsslisvlNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESL--RFSaylrqpssvsieeknryveevikilemqqysdavvgvAGEglnveqRKRLTIgvelaARPKL----L 1046
Cdd:cd03247 88 DTTLRNNLgrRFS-------------------------------------GGE------RQRLAL-----ARILLqdapI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 1047 VFLDEPTSGLDSQTAWdtcQLMRKLATH--GQAILCTIHQPSAilMQQFDRLLFLQKG 1102
Cdd:cd03247 120 VLLDEPTVGLDPITER---QLLSLIFEVlkDKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
899-1102 |
1.03e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--------ERVTMGVITGNIFVDGR--LRdesfPRSIGYCQQQD 968
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgssgEVSLVGQPLHQMDEEARakLR----AKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 969 LHLKTATVRESLRFSAYLRQPSSVSIEEKNRyveEVIKILEMQQYSDAVVGVAGEGlnvEQrKRLTIGVELAARPKLLvF 1048
Cdd:PRK10584 98 MLIPTLNALENVELPALLRGESSRQSRNGAK---ALLEQLGLGKRLDHLPAQLSGG---EQ-QRVALARAFNGRPDVL-F 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSaiLMQQFDRLLFLQKG 1102
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ--LAARCDRRLRLVNG 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
915-1102 |
1.09e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 915 LTALMGASGAGKTTLLDCLAErvTMGVITGNIFVDGRLRDESFP---RSIGYCQQQDLHLKTATVRESLRFSAYLRQPSS 991
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTG--LLPPTSGTVLVGGKDIETNLDavrQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 992 vsiEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLD---SQTAWDtcqLM 1068
Cdd:TIGR01257 1036 ---EEAQLEMEAMLEDTGLHHKRNE----EAQDLSGGMQRKLSVAIAFVGDAKVVV-LDEPTSGVDpysRRSIWD---LL 1104
|
170 180 190
....*....|....*....|....*....|....
gi 6320614 1069 RKLATHGQAILCTIHQPSAILMQqfDRLLFLQKG 1102
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
177-396 |
1.54e-07 |
|
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: 52.79 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 177 SKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFkIAKDS-IVSYNGLSSSDIRKHYRGEVVYNAES 255
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL----GL-LKPDSgEIKVLGKDIKKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 256 DIHLPHLTVYQTLftvarmktpqnrikgvdreayanhvtevamatyglshtrdtkvgnDLvrgvSGGERKRVSIA----- 330
Cdd:cd03230 82 PSLYENLTVRENL---------------------------------------------KL----SGGMKQRLALAqallh 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 331 --EVAIcgarfqcWDNATRGLDSATALEFIRALKTQADIGKTaatvaIYQCS---QDAYDLFDKVCVLDDG 396
Cdd:cd03230 113 dpELLI-------LDEPTSGLDPESRREFWELLRELKKEGKT-----ILLSShilEEAERLCDRVAILNNG 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
896-1060 |
1.60e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRI--LNNVDGWVKPGTLTALMGASGAGKTTLLDC--LAERVTmgviTGNIFVDGR---------LRdeSFPRSIG 962
Cdd:PRK11153 12 PQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT----SGRVLVDGQdltalsekeLR--KARRQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 963 YCQQqdlH---LKTATVRESLRFSAYLrqpSSVSIEEKNRYVEEvikILEMqqysdavVGVA------------Geglnv 1027
Cdd:PRK11153 86 MIFQ---HfnlLSSRTVFDNVALPLEL---AGTPKAEIKARVTE---LLEL-------VGLSdkadrypaqlsgG----- 144
|
170 180 190
....*....|....*....|....*....|...
gi 6320614 1028 eQRKRLTIGVELAARPKLLVfLDEPTSGLDSQT 1060
Cdd:PRK11153 145 -QKQRVAIARALASNPKVLL-CDEATSALDPAT 175
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
185-352 |
1.74e-07 |
|
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: 53.13 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 185 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTV 264
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA----GLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 265 YQTL-FTVARMKTPQNRIkgvdreayanhvtEVAMATYGLSHTRDTkvgndLVRGVSGGERKRVSIAEVAICGARFQCWD 343
Cdd:TIGR01189 91 LENLhFWAAIHGGAQRTI-------------EDALAAVGLTGFEDL-----PAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 6320614 344 NATRGLDSA 352
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
898-1102 |
1.95e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLD--CLAERVTmgviTGNIFVDG----RLRDESFP---RSIGYCQQQD 968
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKliCGIERPS----AGKIWFSGhditRLKNREVPflrRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 969 LHLKTATVRESLRFSAYLrqpSSVSIEEKNRYVEEVI-KILEMQQYSDAVVGVAGeglnvEQRKRLTIGVELAARPKLLV 1047
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALdKVGLLDKAKNFPIQLSG-----GEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1048 fLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFdRLLFLQKG 1102
Cdd:PRK10908 161 -ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSY-RMLTLSDG 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
171-405 |
2.15e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 171 LRLLKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSI------VSYNGLSSSDIRKH 244
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIellgrtVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 245 yRGEVVYNAESDIHLPHLTVYQTLFTVARMKTPQNR-----IKGVDREAYANHVTEVAMATYglSHTRdtkvgndlVRGV 319
Cdd:PRK09984 85 -RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswFTREQKQRALQALTRVGMVHF--AHQR--------VSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 320 SGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALKtqaDIGKTAATVAIYQCSQDAYDL--FDKVCVLDDGY 397
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR---DINQNDGITVVVTLHQVDYALryCERIVALRQGH 230
|
....*...
gi 6320614 398 QLYFGPAK 405
Cdd:PRK09984 231 VFYDGSSQ 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
898-1083 |
2.36e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAErvTMGVITGNIFVDG----RLRDESFPRSIGYCQQQDLHLKT 973
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--LMTPAHGHVWLDGehiqHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYLRQPSSVSIEEKNRyvEEVIKILEMQQYSDaVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPT 1053
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWRKEDE--EAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIML-LDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 6320614 1054 SGLDSQTAWDTCQLMRKL-ATHGQAILCTIH 1083
Cdd:PRK10253 172 TWLDISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
308-397 |
2.49e-07 |
|
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: 53.39 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 308 DTKVGNdlvRGV--SGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALKTQADiGKTAATVA-----IYQCs 380
Cdd:cd03253 128 DTIVGE---RGLklSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAhrlstIVNA- 202
|
90
....*....|....*..
gi 6320614 381 qdaydlfDKVCVLDDGY 397
Cdd:cd03253 203 -------DKIIVLKDGR 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
196-396 |
3.10e-07 |
|
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: 52.88 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 196 GELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIhLPHLTVYQtlfTVARMK 275
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQ---NVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 276 TPQNRIKGVDREAyanhvTEVAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICGARFQCWDNATRGLDSATAL 355
Cdd:cd03298 96 SPGLKLTAEDRQA-----IEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6320614 356 EFIR-ALKTQADIGKTAATVAiyQCSQDAYDLFDKVCVLDDG 396
Cdd:cd03298 166 EMLDlVLDLHAETKMTVLMVT--HQPEDAKRLAQRVVFLDNG 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
898-1092 |
3.11e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.50 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERvtM-----GV-ITGNIFVDGR-LRDES-------------- 956
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NR--MndlipGArVEGEILLDGEdIYDPDvdvvelrrrvgmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 -----FPRSI-----------GYCQQQDLHlktATVRESLRfSAYLrqpssvsIEE-KNRyveevikiLEMQqysdavvg 1019
Cdd:COG1117 99 qkpnpFPKSIydnvayglrlhGIKSKSELD---EIVEESLR-KAAL-------WDEvKDR--------LKKS-------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1020 vaGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHgqailCTI----HqpsaiLMQQ 1092
Cdd:COG1117 152 --ALGLSGGQQQRLCIARALAVEPEVLL-MDEPTSALDPISTAKIEELILELKKD-----YTIvivtH-----NMQQ 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
896-1106 |
3.68e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGNIFVDGRLRDE---SFPRSIGYCQQQDLH 970
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVglESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKTA--TVRESLRfsAYLRQPSSVSIEEKNRYVEEVIKILEMqqySDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVf 1048
Cdd:PRK10419 101 AVNPrkTVREIIR--EPLRHLLSLDKAERLARASEMLRAVDL---DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1049 LDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSaiLMQQFDRLLFLQKGGQTV 1106
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLR--LVERFCQRVMVMDNGQIV 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
903-1066 |
3.80e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTlldcLAERVT--MGVITGNIFVDGR-LRD---ESFPRSIGYCQQQdLHLKTATV 976
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST----IANLLTrfYDIDEGEILLDGHdLRDytlASLRNQVALVSQN-VHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 977 RESLrfsAYLR--QPSSVSIEEKNR--YVEEVIKilEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEP 1052
Cdd:PRK11176 434 ANNI---AYARteQYSREQIEEAARmaYAMDFIN--KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI-LDEA 507
|
170 180
....*....|....*....|
gi 6320614 1053 TSGLDS------QTAWDTCQ 1066
Cdd:PRK11176 508 TSALDTeseraiQAALDELQ 527
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
192-353 |
4.59e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.18 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 192 CLNPGELLVVLGRPGSGCTTLLKSISsnshG-FKIAKDSIvSYNGLSSSDirKHYRGEVVYNAESDIHLPHLTVYQTLFT 270
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIA----GlLPPAAGTI-KLDGGDIDD--PDVAEACHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 271 VArmktpqnRIKGvDREAYAnhvtEVAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICGARFQCWDNATRGLD 350
Cdd:PRK13539 97 WA-------AFLG-GEELDI----AAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
...
gi 6320614 351 SAT 353
Cdd:PRK13539 160 AAA 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
899-1083 |
5.37e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 899 QRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGR-LRDESFPRSIGYCQQQ------- 967
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLN-----GLHVptqGSVRVDDTlITSTSKNKDIKQIRKKvglvfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 -DLHLKTATVRESLRFSAylrQPSSVSIEEKNRYVEEVIkilemqqysdAVVGVAGE-------GLNVEQRKRLTIGVEL 1039
Cdd:PRK13649 94 pESQLFEETVLKDVAFGP---QNFGVSQEEAEALAREKL----------ALVGISESlfeknpfELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6320614 1040 AARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK13649 161 AMEPKILV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
180-361 |
5.49e-07 |
|
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: 54.21 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 180 EDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDI-RKHYRGEVVYNAESdih 258
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL----GFVDPTEGSIAVNGVPLADAdADSWRDQIAWVPQH--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 259 lPHLtVYQTLFTVARMKTPqnrikgvdrEAYANHVTEVAMATY------GLSHTRDTKVGNDlVRGVSGGERKRVSIAEV 332
Cdd:TIGR02857 405 -PFL-FAGTIAENIRLARP---------DASDAEIREALERAGldefvaALPQGLDTPIGEG-GAGLSGGQAQRLALARA 472
|
170 180
....*....|....*....|....*....
gi 6320614 333 AICGARFQCWDNATRGLDSATALEFIRAL 361
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEAL 501
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
900-951 |
7.89e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 7.89e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV------ITGNIFVDGR 951
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGE 71
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
903-1079 |
7.95e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GNIFVDGRLRDesfPRS--------IGYCQQqdlHL 971
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKIL-----YGLYQpdsGEILIDGKPVR---IRSprdaialgIGMVHQ---HF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 K---TATVRESLRFSAYLRQPSSVSIEEKNRYVEEVikileMQQYS-----DAVVgvagEGLNVEQRKRltigVE----L 1039
Cdd:COG3845 90 MlvpNLTVAENIVLGLEPTKGGRLDRKAARARIREL-----SERYGldvdpDAKV----EDLSVGEQQR----VEilkaL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6320614 1040 AARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:COG3845 157 YRGARILI-LDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
900-1060 |
8.11e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDG-RLRDESFPRSIGYcqQQDLHLKTATVRE 978
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGkPVEGPGAERGVVF--QNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 979 SLRFSAYLRqpsSVSIEEKNRYVEEVIKIlemqqysdavVGVAGEG------LNVEQRKRLTIGVELAARPKLLVfLDEP 1052
Cdd:PRK11248 90 NVAFGLQLA---GVEKMQRLEIAHQMLKK----------VGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLL-LDEP 155
|
....*...
gi 6320614 1053 TSGLDSQT 1060
Cdd:PRK11248 156 FGALDAFT 163
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
901-1096 |
8.28e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGrlRDESFPRS---------IGYcqqQD 968
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLL-----KILSGNYqpdAGSILIDG--QEMRFASTtaalaagvaIIY---QE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 969 LHL-KTATVRESLrfsaYLRQ-PSSVSIEEKNRYVEEVIKILEmqqysdavvgvaGEGLNVE---QRKRLTIG----VEL 1039
Cdd:PRK11288 88 LHLvPEMTVAENL----YLGQlPHKGGIVNRRLLNYEAREQLE------------HLGVDIDpdtPLKYLSIGqrqmVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1040 A---ARPKLLVFLDEPTSGLDSQtawDTCQLMR---KLATHGQAILCTIHQpsailMQQFDRL 1096
Cdd:PRK11288 152 AkalARNARVIAFDEPTSSLSAR---EIEQLFRvirELRAEGRVILYVSHR-----MEEIFAL 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
177-330 |
9.83e-07 |
|
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: 51.38 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 177 SKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIssnshgfkiakdsivsyNGL---SSSDIRKHyrGEVVYNA 253
Cdd:cd03262 7 HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-----------------NLLeepDSGTIIID--GLKLTDD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 254 ESDIHL---------------PHLTVYQTLfTVARMKtpqnrIKGVDREAyANHVTEVAMATYGLSHTRDTKVGNdlvrg 318
Cdd:cd03262 68 KKNINElrqkvgmvfqqfnlfPHLTVLENI-TLAPIK-----VKGMSKAE-AEERALELLEKVGLADKADAYPAQ----- 135
|
170
....*....|..
gi 6320614 319 VSGGERKRVSIA 330
Cdd:cd03262 136 LSGGQQQRVAIA 147
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
896-1109 |
1.12e-06 |
|
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: 51.38 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGRLrdeSFPRSIGYCQQQDLhlk 972
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLL-----RLLAGIYppdSGTVTVRGRV---SSLLGLGGGFNPEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 taTVRESLRFSAYLrqpSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDEP 1052
Cdd:cd03220 100 --TGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG----MKARLAFAIATALEPDILL-IDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 1053 TSGLDSQTAwDTCQ-LMRKLATHGQAILCTIHQPSAIlmQQF-DRLLFLQKgGQTVYFG 1109
Cdd:cd03220 170 LAVGDAAFQ-EKCQrRLRELLKQGKTVILVSHDPSSI--KRLcDRALVLEK-GKIRFDG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
178-396 |
1.70e-06 |
|
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: 50.83 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 178 KEEDTFQILKPMDGCLNPGELLVVLGRPGSG-------CTTLLKSISSNSH--GFKIAKDSIvsynglsssDIRKHYrGE 248
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGktttikmLTTLLKPTSGRATvaGHDVVREPR---------EVRRRI-GI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 249 VVYNAESDihlPHLTVYQTLFTVArmktpqnRIKGVDREAYANHVTEVaMATYGLSHTRDtkvgnDLVRGVSGGERKRVS 328
Cdd:cd03265 78 VFQDLSVD---DELTGWENLYIHA-------RLYGVPGAERRERIDEL-LDFVGLLEAAD-----RLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 329 IAEVAICGARFQCWDNATRGLDSATAL---EFIRALKtqADIGKTAATVAIYQcsQDAYDLFDKVCVLDDG 396
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAhvwEYIEKLK--EEFGMTILLTTHYM--EEAEQLCDRVAIIDHG 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
903-1090 |
1.70e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGNIFVDGRLRD-----ESFPRSIGYCQQQDLHLKTA 974
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCL-----FGIYqkdSGSILFQGKEIDfksskEALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSAYLRQpsSVSIEEKNRYvEEVIKIL-EMQQYSDAVVGVAgeGLNVEQRKRLTIGVELAARPKlLVFLDEPT 1053
Cdd:PRK10982 89 SVMDNMWLGRYPTK--GMFVDQDKMY-RDTKAIFdELDIDIDPRAKVA--TLSVSQMQMIEIAKAFSYNAK-IVIMDEPT 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 6320614 1054 SGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILM 1090
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQ 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
900-1102 |
1.80e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 900 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDG----------RLRDESFPRSIGYCQQQDL 969
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIE--IYDSKIKVDGkvlyfgkdifQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 970 HLKTATVRESLRFSayLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfL 1049
Cdd:PRK14246 101 PFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL-M 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLATHgQAILCTIHQPSAIlMQQFDRLLFLQKG 1102
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQV-ARVADYVAFLYNG 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
196-396 |
2.01e-06 |
|
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: 50.33 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 196 GELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDirkhyrgevVYNAESDIHL--------PHLTVYQT 267
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIA----GLEEPTSGRIYIGGRDVTD---------LPPKDRDIAMvfqnyalyPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 268 L-FTVarmktpqnRIKGVDREAYANHVTEVAmATYGLSHTRDTKvgndlVRGVSGGERKRVSIAEVAICGARFQCWDNAT 346
Cdd:cd03301 93 IaFGL--------KLRKVPKDEIDERVREVA-ELLQIEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 347 RGLDSATALEfIRA--LKTQADIGKTaatvAIYQCsQD---AYDLFDKVCVLDDG 396
Cdd:cd03301 159 SNLDAKLRVQ-MRAelKRLQQRLGTT----TIYVT-HDqveAMTMADRIAVMNDG 207
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
902-1057 |
2.11e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGR----LRDE-----------SFPRSI-GYCQ 965
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKdlleLSPEdragegifmafQYPVEIpGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 966 QQDLHLKTATVREslrfsayLRQPSSVSIEEKNRYVEEVIKILEMQQysDAVVGVAGEGLNVEQRKRLTIgVELAARPKL 1045
Cdd:PRK09580 96 QFFLQTALNAVRS-------YRGQEPLDRFDFQDLMEEKIALLKMPE--DLLTRSVNVGFSGGEKKRNDI-LQMAVLEPE 165
|
170
....*....|..
gi 6320614 1046 LVFLDEPTSGLD 1057
Cdd:PRK09580 166 LCILDESDSGLD 177
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
896-1116 |
2.42e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 896 KGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLrdeSFPRSIGYCQQQDLhlk 972
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GILeptSGRVEVNGRV---SALLELGAGFHPEL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 taTVRESLRFSAYLRqpsSVSIEEKNRYVEEVIKILEMQQYSDAVVGV--AGeglnveQRKRLTIGVELAARPKLLVfLD 1050
Cdd:COG1134 104 --TGRENIYLNGRLL---GLSRKEIDEKFDEIVEFAELGDFIDQPVKTysSG------MRARLAFAVATAVDPDILL-VD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1051 EPTS-GldsqtawDT-----C-QLMRKLATHGQAILCTIHQPSAIlmQQF-DRLLFLQKgGQTVYFGDLGEGCK 1116
Cdd:COG1134 172 EVLAvG-------DAafqkkClARIRELRESGRTVIFVSHSMGAV--RRLcDRAIWLEK-GRLVMDGDPEEVIA 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
184-396 |
2.66e-06 |
|
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: 49.36 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 184 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshgfkiakdsivsynGLsssdiRKHYRGEVVYNAESDIHLPHLT 263
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-----------------GL-----LKPSSGEILLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 264 VYQTLFTVarmktPQnrikgvdreayanhvtevAMATYGLSHTRDTKVgNDLvrgvSGGERKRVSIAEVAICGARFQCWD 343
Cdd:cd03214 71 LARKIAYV-----PQ------------------ALELLGLAHLADRPF-NEL----SGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 344 NATRGLD---SATALEFIRALKTQAdiGKTAATVaiyqcSQD---AYDLFDKVCVLDDG 396
Cdd:cd03214 123 EPTSHLDiahQIELLELLRRLARER--GKTVVMV-----LHDlnlAARYADRVILLKDG 174
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
902-1084 |
2.82e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGrlrdESFPRSIGYCQQQDLHL--KTA-- 974
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIA-----GLLnpeKGEILFER----QSIKKDLCTYQKQLCFVghRSGin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 ---TVRESLRFSAYLrqpSSVSIEeknryVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLLVfLDE 1051
Cdd:PRK13540 87 pylTLRENCLYDIHF---SPGAVG-----ITELCRLFSLEHLIDYPCGLLSSG----QKRQVALLRLWMSKAKLWL-LDE 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 6320614 1052 PTSGLDSQTawdTCQLMRKLATH---GQAILCTIHQ 1084
Cdd:PRK13540 154 PLVALDELS---LLTIITKIQEHrakGGAVLLTSHQ 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
881-1059 |
3.90e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 881 EAIFHWRDLCYDVPikGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVI---TGNIFVDGRLRDES- 956
Cdd:PRK13635 3 EEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL-----AKLLNGLLlpeAGTITVGGMVLSEEt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 957 ---FPRSIGYC-QQQDLHLKTATVRESLRFSAylrQPSSVSIEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKR 1032
Cdd:PRK13635 76 vwdVRRQVGMVfQNPDNQFVGATVQDDVAFGL---ENIGVPREEMVERVDQALRQVGMEDFLNR----EPHRLSGGQKQR 148
|
170 180
....*....|....*....|....*..
gi 6320614 1033 LTIGVELAARPKLLVfLDEPTSGLDSQ 1059
Cdd:PRK13635 149 VAIAGVLALQPDIII-LDEATSMLDPR 174
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
892-1100 |
5.72e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.33 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 892 DVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGR----LRDESFPRSIGYCQQQ 967
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PTSGTLLFEGEdistLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 968 DLhLKTATVRESLRFSAYLR--QPSSVSIEEKNRYVEEVIKILemQQYSDAVVGvaGEglnveqRKRLTIGVELAARPKL 1045
Cdd:PRK10247 90 PT-LFGDTVYDNLIFPWQIRnqQPDPAIFLDDLERFALPDTIL--TKNIAELSG--GE------KQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1046 LVfLDEPTSGLDSQTAWDTCQLMRKLAT-HGQAILCTIHQPSAIlmQQFDRLLFLQ 1100
Cdd:PRK10247 159 LL-LDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEI--NHADKVITLQ 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
903-1079 |
6.43e-06 |
|
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: 48.20 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDGRLRDESFPRS-----IGYC----QQQDLH 970
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-----GLRppaSGEITLDGKPVTRRSPRDairagIAYVpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LkTATVRESLRFSAYLrqpssvsieeknryveevikilemqqySdavvgvageGLNveQRKrLTIGVELAARPKLLVfLD 1050
Cdd:cd03215 91 L-DLSVAENIALSSLL---------------------------S---------GGN--QQK-VVLARWLARDPRVLI-LD 129
|
170 180
....*....|....*....|....*....
gi 6320614 1051 EPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
910-1083 |
6.62e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFVDGRLRDESFPRS-IGYC-QQQDLHLKTATVRESL----RFS 983
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNlVAYVpQSEEVDWSFPVLVEDVvmmgRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 984 --AYLRQPSSvsieEKNRYVEEVIKILEMQQYSDAVVGVAGEGlnveQRKRLTIGVELAARPKLlVFLDEPTSGLDSQTA 1061
Cdd:PRK15056 108 hmGWLRRAKK----RDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLARAIAQQGQV-ILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|..
gi 6320614 1062 WDTCQLMRKLATHGQAILCTIH 1083
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTH 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
903-1057 |
6.95e-06 |
|
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: 48.87 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLdcLAERVTMGVITGNIFVDGRLRDESFPR--------SIGYCQQQDLhLKTA 974
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrySVAYAAQKPW-LLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 975 TVRESLRFSaylrqpssvSIEEKNRYvEEVIKILEMQQYSDAV-------VGVAGEGLNVEQRKRLTIGVELAARPKLlV 1047
Cdd:cd03290 94 TVEENITFG---------SPFNKQRY-KAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNI-V 162
|
170
....*....|
gi 6320614 1048 FLDEPTSGLD 1057
Cdd:cd03290 163 FLDDPFSALD 172
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
184-405 |
7.56e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.98 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 184 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIS----SNSHGFKIAKDSIVSYNGLSSSD--IRkHYRGEVVYNAESDI 257
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqPEAGTIRVGDITIDTARSLSQQKglIR-QLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 258 HLPHLTVYQTLftvarMKTPQnRIKGVDREAYANHVTEVaMATYGLSHTRDTkvgndLVRGVSGGERKRVSIAEVAICGA 337
Cdd:PRK11264 96 LFPHRTVLENI-----IEGPV-IVKGEPKEEATARAREL-LAKVGLAGKETS-----YPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 338 RFQCWDNATRGLDSATALEFIRALKTQADIGKTAATVAiYQCSQdAYDLFDKVCVLDDGYQLYFGPAK 405
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSF-ARDVADRAIFMDQGRIVEQGPAK 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
195-375 |
7.72e-06 |
|
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: 49.02 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 195 PGELLVVLGRPGSGCTTLLKSIssnsHGFKIAKDSIVSYNGLSSSDIRKHY-RGEVVYNAESDIhLPHLTVYQTLfTVAR 273
Cdd:cd03252 27 PGEVVGIVGRSGSGKSTLTKLI----QRFYVPENGRVLVDGHDLALADPAWlRRQVGVVLQENV-LFNRSIRDNI-ALAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 274 MKTPQNRIKGVDREAYANHVTEVAMATYglshtrDTKVGNDLVrGVSGGERKRVSIAEVAICGARFQCWDNATRGLDSAT 353
Cdd:cd03252 101 PGMSMERVIEAAKLAGAHDFISELPEGY------DTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180
....*....|....*....|..
gi 6320614 354 ALEFIRALKTQADiGKTAATVA 375
Cdd:cd03252 174 EHAIMRNMHDICA-GRTVIIIA 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
901-1113 |
7.82e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMGVITgnifVDGRLRDESFPR-----SIGYCQQQDLHLKT 973
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLsgIHEPTKGTIT----INNINYNKLDHKlaaqlGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYL-RQPSSVSI---EEKNRYVEEVIKILEMQQYSDAVVGvageGLNVEQRKRLTIGVELAARPKLLVfL 1049
Cdd:PRK09700 95 LTVLENLYIGRHLtKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVII-M 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVYFGDLGE 1113
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR-RICDRYTVM-KDGSSVCSGMVSD 231
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1283-1417 |
8.14e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 48.27 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1283 ARERPSRTF--------SWLAFFLSQIIVEIPWNILAGTIAYCIYYYAVGFYANASAAGQLherGALFWLFSIAFyvyiG 1354
Cdd:COG0842 27 AREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLL---LLVLLLFALAF----S 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 1355 SMGLLMISFNEVAETAAHMGTLLFTMALSFCGVMATPKVMPRFWIFMYRVSPLTYMIDALLAL 1417
Cdd:COG0842 100 GLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRAL 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
898-1102 |
8.21e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVITGNifvDGRLRDESFPrsigycqqqdlhlkTATVR 977
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-----GLETPS---AGELLAGTAP--------------LAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 978 ESLRF---SAYL----RQPSSVSIEEKNRYVEEVIKILEmqqysdaVVGV---AGE---GLNVEQRKRLTIGVELAARPK 1044
Cdd:PRK11247 81 EDTRLmfqDARLlpwkKVIDNVGLGLKGQWRDAALQALA-------AVGLadrANEwpaALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1045 LLVfLDEPTSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPS-AILMQqfDRLLFLQKG 1102
Cdd:PRK11247 154 LLL-LDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSeAVAMA--DRVLLIEEG 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
171-330 |
9.47e-06 |
|
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: 48.77 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 171 LRLLKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRG-EV 249
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETPTSGEILLDGKDITNLPPHKRPvNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 250 VYnaESDIHLPHLTVYQTL-FTVarmktpqnRIKGVDREAYANHVTEvAMATYGLSHTRDTKvgndlVRGVSGGERKRVS 328
Cdd:cd03300 77 VF--QNYALFPHLTVFENIaFGL--------RLKKLPKAEIKERVAE-ALDLVQLEGYANRK-----PSQLSGGQQQRVA 140
|
..
gi 6320614 329 IA 330
Cdd:cd03300 141 IA 142
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
902-1110 |
1.09e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.83 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGNIFVDG-RLRDESFP---RSIGYC-QQQDLHLKT 973
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILT-----GLLkpqSGEIKIDGiTISKENLKeirKKIGIIfQNPDNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLRFSAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAvvgvagEGLNVE--QRKRLTIGVELAARPKLLVFlDE 1051
Cdd:PRK13632 99 ATVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDK------EPQNLSggQKQRVAIASVLALNPEIIIF-DE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1052 PTSGLDSQTAWDTCQLMRKLATHGQAILCTI-HQPSAILMQqfDRLLFLqKGGQTVYFGD 1110
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVF-SEGKLIAQGK 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
185-406 |
1.43e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 185 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSI------SSNSHGFKIAKDsiVSYNG--LSSSDIRKHYRGEVVynaesd 256
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgGGAPRGARVTGD--VTLNGepLAAIDAPRLARLRAV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 257 ihLPHLTVYQTLFTVARM----KTPQNRIKGvdreAYANHVTEVAMATYGLSHTrDTKVGNDlVRGVSGGERKRVSIAEV 332
Cdd:PRK13547 88 --LPQAAQPAFAFSAREIvllgRYPHARRAG----ALTHRDGEIAWQALALAGA-TALVGRD-VTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 333 ---------AICGARFQCWDNATRGLDSA---TALEFIRALKTQADIGktaaTVAIYQCSQDAYDLFDKVCVLDDGYQLY 400
Cdd:PRK13547 160 laqlwpphdAAQPPRYLLLDEPTAALDLAhqhRLLDTVRRLARDWNLG----VLAIVHDPNLAARHADRIAMLADGAIVA 235
|
....*.
gi 6320614 401 FGPAKD 406
Cdd:PRK13547 236 HGAPAD 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
898-1057 |
1.61e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGNIFV---DGRLRD-----ESFPRSI-----GYC 964
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD--AGEVHYrmrDGQLRDlyalsEAERRRLlrtewGFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 965 QQ---QDLHLKT---ATVRESL-----RFSAYLRQPSSVSIEEknryVEevikiLEMQQYSDAVVGVAGeGLnveqRKRL 1033
Cdd:PRK11701 95 HQhprDGLRMQVsagGNIGERLmavgaRHYGDIRATAGDWLER----VE-----IDAARIDDLPTTFSG-GM----QQRL 160
|
170 180
....*....|....*....|....
gi 6320614 1034 TIGVELAARPKLlVFLDEPTSGLD 1057
Cdd:PRK11701 161 QIARNLVTHPRL-VFMDEPTGGLD 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
872-1079 |
1.62e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 872 NAGLGLSKSEAIFHWRDlcydvpIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGV---ITGNIFV 948
Cdd:PRK09700 254 KENVSNLAHETVFEVRN------VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVdkrAGGEIRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 949 DGRlrdESFPRSIGYCQQQDLHLKTATVRESLRFSAY-LRQPSSVSIEEKN----------------RYVEEVIKILEMQ 1011
Cdd:PRK09700 323 NGK---DISPRSPLDAVKKGMAYITESRRDNGFFPNFsIAQNMAISRSLKDggykgamglfhevdeqRTAENQRELLALK 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 1012 QYSdaVVGVAGEGLNVEQRKRLtIGVELAARPKLLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:PRK09700 400 CHS--VNQNITELSGGNQQKVL-ISKWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
903-1107 |
1.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.21 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVItgnIFVDGRLRDESFP---RSIGYC-QQQDLHLKTATV 976
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIgiEKVKSGEI---FYNNQAITDDNFEklrKHIGIVfQNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 977 RESLRFSAylrQPSSVSIEEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGL 1056
Cdd:PRK13648 102 KYDVAFGL---ENHAVPYDEMHRRVSEALKQVDMLERADY----EPNALSGGQKQRVAIAGVLALNPSVII-LDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1057 DSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILmqQFDRLLFLQKGgqTVY 1107
Cdd:PRK13648 174 DPDARQNLLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKG--TVY 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
898-1084 |
3.34e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.28 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGR------LRDESfPRSIGYCQQQDLHL 971
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSplkasnIRDTE-RAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRFSAYLRQPSS-VSIEEKNRYVEEVIKILEMQQYSDA-VVGVAGEGlnveQRKRLTIGVELAARPKLLVfL 1049
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGG----QQQLVEIAKALNKQARLLI-L 165
|
170 180 190
....*....|....*....|....*....|....*
gi 6320614 1050 DEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQ 1084
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
887-1057 |
3.57e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 887 RDLCYDVPIKGG--QR-----RILNNVDGWVKPG-TLtALMGASGAGKTTLLDCLaervtMGVI--TGNIFVDGR----- 951
Cdd:COG4172 279 RDLKVWFPIKRGlfRRtvghvKAVDGVSLTLRRGeTL-GLVGESGSGKSTLGLAL-----LRLIpsEGEIRFDGQdldgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 952 -------LRDE----------SF-PR-SIGycqqqdlhlktATVRESLRFSAylRQPSSVSIEEKnryveeVIKILEmqq 1012
Cdd:COG4172 353 srralrpLRRRmqvvfqdpfgSLsPRmTVG-----------QIIAEGLRVHG--PGLSAAERRAR------VAEALE--- 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1013 ysdAVvgvageGLNVE------------QRKRLTIGVELAARPKLLVfLDEPTSGLD 1057
Cdd:COG4172 411 ---EV------GLDPAarhryphefsggQRQRIAIARALILEPKLLV-LDEPTSALD 457
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
901-1102 |
4.43e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLL---DCLAERVTMGVITGNIFVDGRLRD----ESFPRSIGYC-QQQDLHLK 972
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIqltNGLIISETGQTIVGDYAIPANLKKikevKRLRKEIGLVfQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFSaylrqPSSVSiEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVfLDEP 1052
Cdd:PRK13645 105 QETIEKDIAFG-----PVNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV-LDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1053 TSGLDSQTAWDTCQLMRKL-ATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVL-RIADEVIVMHEG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
898-1060 |
6.06e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.37 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGNIFVDGRLRdesfprsIGYC-QQQD-LHLKtAT 975
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKLGETVK-------IGYFdQHQEeLDPD-KT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 976 VREslrfsaYLRQpssvsiEEKNRYVEEVIKIL-------EMQQysdAVVGV--AGEglnveqRKRLTIGVELAARPKLL 1046
Cdd:COG0488 396 VLD------ELRD------GAPGGTEQEVRGYLgrflfsgDDAF---KPVGVlsGGE------KARLALAKLLLSPPNVL 454
|
170
....*....|....
gi 6320614 1047 VfLDEPTSGLDSQT 1060
Cdd:COG0488 455 L-LDEPTNHLDIET 467
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1223-1424 |
6.83e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 47.00 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1223 SKFILTIFNQVFIGFTFFKADRSLQGLQNQMLSIFMYTVIFNPILqqYLPSFVqqrdlyeARERPSRTFSWL-------- 1294
Cdd:pfam12698 133 VLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAA--IIAVSI-------VEEKESRIKERLlvsgvspl 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1295 AFFLSQIIveipWNILAGTIAYCIY-YYAVGFYANasaagqLHERGALFWLFSIAFYVYIgSMGLLMISFNEVAETAAHM 1373
Cdd:pfam12698 204 QYWLGKIL----GDFLVGLLQLLIIlLLLFGIGIP------FGNLGLLLLLFLLYGLAYI-ALGYLLGSLFKNSEDAQSI 272
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6320614 1374 GTLLFTMALSFCGVMATPKVMPRFWIFMYRVSPLTYMIDALLALGVANVDV 1424
Cdd:pfam12698 273 IGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLW 323
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
890-1057 |
7.63e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 46.23 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 890 CYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTlldcLAERVTMGVI--TGNIFVDG-RLRDES----FPRSIG 962
Cdd:PRK13633 13 KYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALLIpsEGKVYVDGlDTSDEEnlwdIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 963 YC-QQQDLHLKTATVRESLRFSaylrqPSSVSI--EEKNRYVEEVIKILEMQQYSDAvvgvAGEGLNVEQRKRLTIGVEL 1039
Cdd:PRK13633 89 MVfQNPDNQIVATIVEEDVAFG-----PENLGIppEEIRERVDESLKKVGMYEYRRH----APHLLSGGQKQRVAIAGIL 159
|
170
....*....|....*...
gi 6320614 1040 AARPKLLVFlDEPTSGLD 1057
Cdd:PRK13633 160 AMRPECIIF-DEPTAMLD 176
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
179-396 |
9.19e-05 |
|
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: 45.68 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 179 EEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSI------SSNShgfkIAKDSI-VSYNGLSSsdIRKHyrgevVY 251
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvDSGR----ILIDGHdVRDYTLAS--LRRQ-----IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 252 NAESDIHLPHLTVYQTLfTVARMKTPQNRIKGVDREAYAnhvTEVAMatyGLSHTRDTKVGndlVRGV--SGGERKRVSI 329
Cdd:cd03251 80 LVSQDVFLFNDTVAENI-AYGRPGATREEVEEAARAANA---HEFIM---ELPEGYDTVIG---ERGVklSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 330 AEVAICGARFQCWDNATRGLDSATALEFIRALKtQADIGKTAATVAiYQCS--QDAydlfDKVCVLDDG 396
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALE-RLMKNRTTFVIA-HRLStiENA----DRIVVLEDG 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
181-409 |
9.86e-05 |
|
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: 45.74 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 181 DTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshgfkiakdsivsynGLsssdiRKHYRGEVVYNAEsDIHlp 260
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----------------GL-----LRPDSGEILVDGQ-DIT-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 261 HLT-------------VYQT--LFT-------VA---RMKTpqnrikGVDREAYANHVTEV-AMAtyGLSHTRDtKVGND 314
Cdd:COG1127 71 GLSekelyelrrrigmLFQGgaLFDsltvfenVAfplREHT------DLSEAEIRELVLEKlELV--GLPGAAD-KMPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 315 LvrgvSGGERKRVSIA-------EVAICgarfqcwDNATRGLDSATALEF---IRALKTQadIGKTAATVaiyqcSQD-- 382
Cdd:COG1127 142 L----SGGMRKRVALAralaldpEILLY-------DEPTAGLDPITSAVIdelIRELRDE--LGLTSVVV-----THDld 203
|
250 260
....*....|....*....|....*...
gi 6320614 383 -AYDLFDKVCVLDDGYQLYFGPAKDAKK 409
Cdd:COG1127 204 sAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
903-1110 |
1.05e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 903 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERV--TMGVITGnIFVDGRL-----RDESFP----------------- 958
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpDTGTIEW-IFKDEKNkkktkEKEKVLeklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 959 ---RSIGYCQQ-QDLHLKTATVRESLRFSaylrqPSSVSIEeKNRYVEEVIKILEMqqysdavVGVAGE-------GLNV 1027
Cdd:PRK13651 102 eirRRVGVVFQfAEYQLFEQTIEKDIIFG-----PVSMGVS-KEEAKKRAAKYIEL-------VGLDESylqrspfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 1028 EQRKRLTIGVELAARPKLLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLqKGGQTVY 1107
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVF-DEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIFF-KDGKIIK 245
|
...
gi 6320614 1108 FGD 1110
Cdd:PRK13651 246 DGD 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
181-396 |
1.09e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 181 DTFQILKPMDGCLNPGELLVVLGRPGSGCTTL---LKSISSNSHGFKIAKDSIVSYNGLSSSDIRKHYrGEVVYNAESDI 257
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV-GIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 258 HLPhlTVYQTL-FTVARMKTPQNRIKGVDREAYAnhvtEVAMATYglshtrDTKVGNDLvrgvSGGERKRVSIAEVAICG 336
Cdd:PRK13639 92 FAP--TVEEDVaFGPLNLGLSKEEVEKRVKEALK----AVGMEGF------ENKPPHHL----SGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 337 ARFQCWDNATRGLDSATALEFIRALKtqaDIGKTAATVAIYQCSQDAYDLF-DKVCVLDDG 396
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLY---DLNKEGITIIISTHDVDLVPVYaDKVYVMSDG 213
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
556-721 |
1.34e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 45.84 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 556 KKNDTSTFYFRGAAMFFAILFNAFSCLLEIFSLYETRpitEKHRTY-SLYHPSADAFASVLSEMppkLITAVCFNIIFYF 634
Cdd:pfam12698 154 NPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESR---IKERLLvSGVSPLQYWLGKILGDF---LVGLLQLLIILLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 635 LVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVPASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLA 714
Cdd:pfam12698 228 LFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFF 307
|
....*..
gi 6320614 715 YLFESLM 721
Cdd:pfam12698 308 SPIDGLL 314
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
906-1057 |
1.50e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.99 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 906 VDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGNIFVDGRLRDESFP--RSIGYC-QQQDL--HLktaTVRE 978
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAglERIT----SGEIWIGGRVVNELEPadRDIAMVfQNYALypHM---SVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 979 SLrfsAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSD----AVVGvaGeglnveQRKRLTIGVELAARPKllVFL-DEPT 1053
Cdd:PRK11650 96 NM---AYGLKIRGMPKAEIEERVAEAARILELEPLLDrkprELSG--G------QRQRVAMGRAIVREPA--VFLfDEPL 162
|
....
gi 6320614 1054 SGLD 1057
Cdd:PRK11650 163 SNLD 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
898-1106 |
1.53e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMG---VITGNIFVDGR----LRDESFPRSIGYCQQQDLH 970
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL-----MGyypLTEGEIRLDGRplssLSHSVLRQGVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 971 LKtatvrESLRFSAYLRQPSSvsiEEKnryveeVIKILEMQQYSDAV----------VGVAGEGLNVEQRKRLTIGVELA 1040
Cdd:PRK10790 427 LA-----DTFLANVTLGRDIS---EEQ------VWQALETVQLAELArslpdglytpLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320614 1041 ARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHgqAILCTI-HQPSAILmqQFDRLLFLQKgGQTV 1106
Cdd:PRK10790 493 QTPQILI-LDEATANIDSGTEQAIQQALAAVREH--TTLVVIaHRLSTIV--EADTILVLHR-GQAV 553
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
177-330 |
1.80e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.71 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 177 SKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRgevvynaesD 256
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA----GFETPDSGRIMLDGQDITHVPAENR---------H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 257 IH--------LPHLTVYQtlfTVA---RM-KTPQNRIKgvdreayaNHVTEvAMATYGLSHTRDTKvgndlVRGVSGGER 324
Cdd:PRK09452 88 VNtvfqsyalFPHMTVFE---NVAfglRMqKTPAAEIT--------PRVME-ALRMVQLEEFAQRK-----PHQLSGGQQ 150
|
....*.
gi 6320614 325 KRVSIA 330
Cdd:PRK09452 151 QRVAIA 156
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
902-1102 |
1.82e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLL-----------------------DCLAERVTMGVITGNIFVDGRLRdesfp 958
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnglikskygtiqvgdiyigdKKNNHELITNPYSKKIKNFKELR----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 959 RSIGYCQQ-QDLHLKTATVRESLRFSaylrqPSSVSIEeKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGV 1037
Cdd:PRK13631 116 RRVSMVFQfPEYQLFKDTIEKDIMFG-----PVALGVK-KSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1038 ELAARPKLLVFlDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILmQQFDRLLFLQKG 1102
Cdd:PRK13631 190 ILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
892-966 |
2.02e-04 |
|
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: 43.21 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 892 DVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERvtMGVITGNIFVDGRLRdesfprsIGYCQQ 966
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE--LEPDEGIVTWGSTVK-------IGYFEQ 70
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
196-396 |
2.82e-04 |
|
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: 43.33 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 196 GELLVVLGRPGSGCTTLLKSIssnshgfkiakdsivsyNGL---SSSDIRkhYRGEVVyNAESDIHLPHLT----VYQ-- 266
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCI-----------------AGLeepDSGSIL--IDGEDL-TDLEDELPPLRRrigmVFQdf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 267 TLFtvarmktpqnrikgvdreayaNHVTevamatyglshtrdtkVGNDLVRGVSGGERKRVSIAEVAICGARFQCWDNAT 346
Cdd:cd03229 86 ALF---------------------PHLT----------------VLENIALGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6320614 347 RGLDSATALEFIRALKT-QADIGKTAATVaiyqcSQD---AYDLFDKVCVLDDG 396
Cdd:cd03229 129 SALDPITRREVRALLKSlQAQLGITVVLV-----THDldeAARLADRVVVLRDG 177
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
177-374 |
3.18e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.93 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 177 SKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIssNSHGFKIAKDSIVsyNGLSSSDIRKHYRgevvynaesD 256
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIV--DGLKVNDPKVDER---------L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 257 IHLPHLTVYQTLFTVARMKTPQN------RIKGVDREAyANHVTEVAMATYGLSHtRDTKVGNDLvrgvSGGERKRVSIA 330
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENvmfgplRVRGASKEE-AEKQARELLAKVGLAE-RAHHYPSEL----SGGQQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6320614 331 EVAICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATV 374
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIV 192
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
906-941 |
3.37e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 43.52 E-value: 3.37e-04
10 20 30
....*....|....*....|....*....|....*.
gi 6320614 906 VDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV 941
Cdd:pfam13481 26 IKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGK 61
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
898-1082 |
3.80e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.99 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGNIFVDGrlrdESFP---RSigycqqqdlHL 971
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLL-----RLIGGQIapdHGEILFDG----ENIPamsRS---------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 972 KTATVRESLRF-SAYLRQPSSV------SIEEKNRYVEEVIKILEMQQYSdaVVGVAGEG------LNVEQRKRLTIGVE 1038
Cdd:PRK11831 80 YTVRKRMSMLFqSGALFTDMNVfdnvayPLREHTQLPAPLLHSTVMMKLE--AVGLRGAAklmpseLSGGMARRAALARA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6320614 1039 LAARPKLLVFlDEPTSGLDSQTAWDTCQLMRKLaTHGQAILCTI 1082
Cdd:PRK11831 158 IALEPDLIMF-DEPFVGQDPITMGVLVKLISEL-NSALGVTCVV 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
193-368 |
4.26e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.73 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTT---LLKSISSNSHGFKIAKDSIVSYNGLSSsdirKHYRGEVVYNAESDIhLPHLTVYQTLF 269
Cdd:PRK10895 26 VNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLLPLHA----RARRGIGYLPQEASI-FRRLSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 270 TVARMKtpqnriKGVDREAYANHVTEVaMATYGLSHTRDTkvgndLVRGVSGGERKRVSIAEVAICGARFQCWDNATRGL 349
Cdd:PRK10895 101 AVLQIR------DDLSAEQREDRANEL-MEEFHIEHLRDS-----MGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170
....*....|....*....
gi 6320614 350 DSATALEFIRALKTQADIG 368
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSG 187
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
898-1097 |
4.58e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGR--LRDESFPRS---IGYCQQQDLHLK 972
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGEsiLDLEPEERAhlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFSAYLRQPSSvSIEEKN-----RYVEEVIKILEMQQY--SDAVvgvaGEGLNVEQRKRLTIgVELAARPKL 1045
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQ-GLPELDpleflEIINEKLKLVGMDPSflSRNV----NEGFSGGEKKRNEI-LQMALLDSE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6320614 1046 LVFLDEPTSGLDSQTAWDTCQLMRKLATHGQAIlctihqpsaILMQQFDRLL 1097
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSI---------ILITHYQRLL 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
901-1071 |
5.19e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 901 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GNIFVDGRLRDESFP---RSIG-YCQQQDLHL-K 972
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVPpdsGTLEIGGNPCARLTPakaHQLGiYLVPQEPLLfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 TATVRESLRFsaylRQPSSVSIEEKnryVEEVIKILEMQQYSDAVVGVagegLNVEQRKRLTIGVELAARPKLLVfLDEP 1052
Cdd:PRK15439 100 NLSVKENILF----GLPKRQASMQK---MKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILI-LDEP 167
|
170
....*....|....*....
gi 6320614 1053 TSGLdsqTAWDTCQLMRKL 1071
Cdd:PRK15439 168 TASL---TPAETERLFSRI 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
173-396 |
6.04e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 173 LLKPSKEEDTFQILKPMDG-CLN--PGELLVVLGRPGSGCTTLLKSISsnshgfkiakdsivsynGLSSSDI-RKHYRG- 247
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGaALNvyPGRVMALVGENGAGKSTMMKVLT-----------------GIYTRDAgSILYLGk 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 248 EVVYNAESD--------IH-----LPHLTVYQTLFtVARMKTpqNRIKGVD-REAYANhvTEVAMATYGLSHTRDTKVGn 313
Cdd:PRK10762 67 EVTFNGPKSsqeagigiIHqelnlIPQLTIAENIF-LGREFV--NRFGRIDwKKMYAE--ADKLLARLNLRFSSDKLVG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 314 DLvrgvSGGERKRVSIAEVAICGARFQCWDNATRGL-DSATALEF--IRALKTQAdigktAATVAIYQCSQDAYDLFDKV 390
Cdd:PRK10762 141 EL----SIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFrvIRELKSQG-----RGIVYISHRLKEIFEICDDV 211
|
....*.
gi 6320614 391 CVLDDG 396
Cdd:PRK10762 212 TVFRDG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
181-329 |
6.05e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 181 DTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSnshgfKIAKDS-IVSYNGLSSSDIR-KHYRGEVVYNAESdih 258
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS-----LISPTSgTLLFEGEDISTLKpEIYRQQVSYCAQT--- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 259 lPHL---TVYQTLftvarmKTP-QNRIKGVDREAYANhvtevAMATYGLSHTRDTKVGNDLvrgvSGGERKRVSI 329
Cdd:PRK10247 90 -PTLfgdTVYDNL------IFPwQIRNQQPDPAIFLD-----DLERFALPDTILTKNIAEL----SGGEKQRISL 148
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
181-409 |
7.33e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 43.30 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 181 DTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKS---ISSNSHGFKIAKDSIVSYNGLSSSDIRKHYrGEVVynAESDI 257
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNlngILKPSSGRILFDGKPIDYSRKGLMKLRESV-GMVF--QDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 258 HLPHLTVYQTL-FTVARMKTPQNRI-KGVDReayanhvtevAMATYGLSHTRDTKVgndlvRGVSGGERKRVSIAEVAIC 335
Cdd:PRK13636 94 QLFSASVYQDVsFGAVNLKLPEDEVrKRVDN----------ALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320614 336 GARFQCWDNATRGLDSATALEFIRALK-TQADIGktaATVAIYQCSQDAYDLF-DKVCVLDDGYQLYFGPAKD--AKK 409
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVeMQKELG---LTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEvfAEK 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
902-1101 |
7.40e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 902 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmgvitgnifvdGRLRDESfprsigycQQQDLHLKTATVRESLR 981
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLA---------------GLLHVES--------GQIQIDGKTATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 982 FSAYLRQ----PSSVSIEEKNRYVEEVIKILEMQQYSDA--VVGVAG------EGLNVEQRKRLTIGvELAARPKLLVFL 1049
Cdd:PRK13543 83 FMAYLGHlpglKADLSTLENLHFLCGLHGRRAKQMPGSAlaIVGLAGyedtlvRQLSAGQKKRLALA-RLWLSPAPLWLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 1050 DEPTSGLDSQtawDTCQLMRKLATH---GQAILCTIHQPSAILMQQfDRLLFLQK 1101
Cdd:PRK13543 162 DEPYANLDLE---GITLVNRMISAHlrgGGAALVTTHGAYAAPPVR-TRMLTLEA 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
898-1093 |
7.77e-04 |
|
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: 44.13 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 898 GQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaerVTMGVITGNIFVDGRLRD----ESFPRSIGYCQQQdLHLKT 973
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEGEIQIDGVSWNsvtlQTWRKAFGVIPQK-VFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 974 ATVRESLrfSAYLRQpssvSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEG---LNVEQRKRLTIGVELAARPKLLVfLD 1050
Cdd:TIGR01271 1306 GTFRKNL--DPYEQW----SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILL-LD 1378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6320614 1051 EPTSGLDSQTAwdtcQLMRKLATHGQA----ILCTiHQPSAIL-MQQF 1093
Cdd:TIGR01271 1379 EPSAHLDPVTL----QIIRKTLKQSFSnctvILSE-HRVEALLeCQQF 1421
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
193-330 |
7.81e-04 |
|
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: 43.55 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISsnshgfkiakdsivsynGLSSSD---IRkhYRGEVVYNAESDIHLP--------- 260
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIA-----------------GLERPDsgrIR--LGGEVLQDSARGIFLPphrrrigyv 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320614 261 --------HLTVYQTL-FTVARMKTPQNRIKgvdreayANHVTEVamatYGLSHTRDTKVGNdlvrgVSGGERKRVSIA 330
Cdd:COG4148 83 fqearlfpHLSVRGNLlYGRKRAPRAERRIS-------FDEVVEL----LGIGHLLDRRPAT-----LSGGERQRVAIG 145
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
178-370 |
7.88e-04 |
|
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: 42.63 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 178 KEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGlssSDIRKHYRGEVVYNAESDi 257
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA----GLIKESSGSILLNG---KPIKAKERRKSIGYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 258 hlphltVYQTLF--TVARMKTPQNRIKGVDREayanhVTEVAMATYGLSHTRDtkvgnDLVRGVSGGERKRVSIAEVAIC 335
Cdd:cd03226 80 ------VDYQLFtdSVREELLLGLKELDAGNE-----QAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190
....*....|....*....|....*....|....*
gi 6320614 336 GARFQCWDNATRGLDSATALEFIRALKTQADIGKT 370
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
910-1079 |
9.44e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 910 VKPGTLTALMGASGAGKTTLLDCL-AERVTMGvitGNIFVDGRlrdESFPRSIGYC------------QQQDLHLK---- 972
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLyGLRPARG---GRIMLNGK---EINALSTAQRlarglvylpedrQSSGLYLDapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 973 --------------TATVRESLRFSAYLRQPSsvsieeknryveevIKILEMQQysdAVVGVAGEglnvEQRKRLtIGVE 1038
Cdd:PRK15439 360 wnvcalthnrrgfwIKPARENAVLERYRRALN--------------IKFNHAEQ---AARTLSGG----NQQKVL-IAKC 417
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6320614 1039 LAARPKLLVfLDEPTSGLDSQTAWDTCQLMRKLATHGQAIL 1079
Cdd:PRK15439 418 LEASPQLLI-VDEPTRGVDVSARNDIYQLIRSIAAQNVAVL 457
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
199-396 |
9.76e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 199 LVVLGRPGSGCTTLLKSI------SSNS---HGFKIAKDSIvsynglssSDIRKhYRGEVVYNAESDIHLPhlTVYQTL- 268
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFngilkpTSGSvliRGEPITKENI--------REVRK-FVGLVFQNPDDQIFSP--TVEQDIa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 269 FTVARMktpqnrikGVDREAYANHVTEvAMATYGLSHTRDtKVGNDLvrgvSGGERKRVSIAEVAICGARFQCWDNATRG 348
Cdd:PRK13652 102 FGPINL--------GLDEETVAHRVSS-ALHMLGLEELRD-RVPHHL----SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6320614 349 LDSATALEFIRALKtqaDIGKTAATVAIYQCSQDAY--DLFDKVCVLDDG 396
Cdd:PRK13652 168 LDPQGVKELIDFLN---DLPETYGMTVIFSTHQLDLvpEMADYIYVMDKG 214
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
622-720 |
1.49e-03 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 41.72 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 622 LITAVCFNIIFYFLVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVPASMLLLAISMYTGFAIPKTKIL 701
Cdd:COG0842 61 LLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLP 140
|
90
....*....|....*....
gi 6320614 702 GWSIWIWYINPLAYLFESL 720
Cdd:COG0842 141 GWLQAIAYLNPLTYFVEAL 159
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
193-330 |
1.85e-03 |
|
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: 41.69 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHyRGeVVYnaESDIHLPHLTVYqtlftva 272
Cdd:cd03293 27 VEEGEFVALVGPSGCGKSTLLRIIA----GLERPTSGEVLVDGEPVTGPGPD-RG-YVF--QQDALLPWLTVL------- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320614 273 rmktpQN-----RIKGVDREAYANHVTEvAMATYGLSHTRDtKVGNDLvrgvSGGERKRVSIA 330
Cdd:cd03293 92 -----DNvalglELQGVPKAEARERAEE-LLELVGLSGFEN-AYPHQL----SGGMRQRVALA 143
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
920-1057 |
1.86e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 920 GASGAGKTTlldclaervTMGVITG---------NIF---VDGRlrDESFPRSIGYCQQ-----QDLhlktaTVRESLRF 982
Cdd:NF033858 299 GSNGCGKST---------TMKMLTGllpasegeaWLFgqpVDAG--DIATRRRVGYMSQafslyGEL-----TVRQNLEL 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320614 983 SAYLRQpssVSIEEKNRYVEEVIKILEMQQYSDAVvgvaGEGLNVEQRKRLTIGVELAARPKLLVfLDEPTSGLD 1057
Cdd:NF033858 363 HARLFH---LPAAEIAARVAEMLERFDLADVADAL----PDSLPLGIRQRLSLAVAVIHKPELLI-LDEPTSGVD 429
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
184-406 |
2.03e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 184 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISS---NSHGFKIAKDsiVSYNGLSSSDIRKHYRGeVVYNAESDIHlp 260
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihePTKGTITINN--INYNKLDHKLAAQLGIG-IIYQELSVID-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 261 HLTVYQTLFtVARMktPQNRIKGVDREAYA--NHVTEVAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICGAR 338
Cdd:PRK09700 94 ELTVLENLY-IGRH--LTKKVCGVNIIDWRemRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320614 339 FQCWDNATRGL-DSATALEF--IRALKTQadiGKtaATVAIYQCSQDAYDLFDKVCVLDDGYQLYFGPAKD 406
Cdd:PRK09700 166 VIIMDEPTSSLtNKEVDYLFliMNQLRKE---GT--AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
193-368 |
2.09e-03 |
|
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: 41.32 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDIRKHYRGEVVYnaesdihLPHLTVYQTLFTVA 272
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILA----GLSPPLAGRVLLNGGPLDFQRDSIARGLLY-------LGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 273 RMKTPQNRIKGVDReayanhvTEVAMATYGLSHTRDTKVGNdlvrgVSGGERKRVSIAEVAICGARFQCWDNATRGLDSA 352
Cdd:cd03231 92 ENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170
....*....|....*.
gi 6320614 353 TALEFIRALKTQADIG 368
Cdd:cd03231 160 GVARFAEAMAGHCARG 175
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1083-1126 |
2.48e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 42.20 E-value: 2.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 6320614 1083 HQPSAILMQQFDRLLFLQKGGQTVYFGDLgegcKTMIDYFESKG 1126
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPV----KKVEEYFAGLG 40
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
918-946 |
3.95e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 40.43 E-value: 3.95e-03
10 20 30
....*....|....*....|....*....|...
gi 6320614 918 LMGASGAGKTTLL----DCLAERVTMGVITGNI 946
Cdd:COG0378 18 LMGSPGSGKTTLLektiRALKDRLRIAVIEGDI 50
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
906-940 |
4.69e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 41.04 E-value: 4.69e-03
10 20 30
....*....|....*....|....*....|....*
gi 6320614 906 VDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMG 940
Cdd:COG3598 6 VPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAG 40
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
184-396 |
4.80e-03 |
|
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: 40.29 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 184 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnshGFKIAKDSIVSYNGLSSSDI-RKHYRGEVVYNAESDIHLPhl 262
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLM----RFYDPQKGQILIDGIDIRDIsRKSLRSMIGVVLQDTFLFS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 263 tvyQTLFTVARMKTPQNRIKGVDREAYANHVTEVAMAtygLSHTRDTKVGNdlvRG--VSGGERKRVSIAEVAICGARFQ 340
Cdd:cd03254 91 ---GTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMK---LPNGYDTVLGE---NGgnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320614 341 CWDNATRGLDSAT------ALEFIRALKTQADIGKTAATVaiyqcsQDAydlfDKVCVLDDG 396
Cdd:cd03254 162 ILDEATSNIDTETekliqeALEKLMKGRTSIIIAHRLSTI------KNA----DKILVLDDG 213
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
1453-1510 |
6.49e-03 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 37.44 E-value: 6.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320614 1453 AGTGYLSDPSATDICSFC-AV--STT---NAFLATfSSHYYR--RWRNYGIFICYIAFdYIAATFL 1510
Cdd:pfam06422 3 SGPGYENVSGANQVCAVVgAVpgQTFvsgDDYLAA-SYGYSYshLWRNFGILIAFWIF-FLALYLI 66
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
182-396 |
7.06e-03 |
|
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: 40.96 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 182 TFQILKPMDGC---LNPGELLVVLGRPGSGCTTLLKSISS-NSHGfkiAKDSIVSYNG--LSSSDIRKHYRGEVVYNAES 255
Cdd:TIGR02633 10 TFGGVKALDGIdleVRPGECVGLCGENGAGKSTLMKILSGvYPHG---TWDGEIYWSGspLKASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 256 DIHLPHLTVYQTLFTVARMKTPQNRIKgvDREAYanHVTEVAMATYGLSHTRDTKVGNDLvrgvSGGERKRVSIAEVAIC 335
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEITLPGGRMA--YNAMY--LRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320614 336 GARFQCWDNATRGLDSATA---LEFIRALKTqadigKTAATVAIYQCSQDAYDLFDKVCVLDDG 396
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETeilLDIIRDLKA-----HGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
193-362 |
8.38e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.47 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 193 LNPGELLVVLGRPGSGCTTLLKSISSNshgFKIAKDSIvSYNGLSSSDIR-KHYRGEVVynaesdihlphlTVYQTLF-- 269
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRH---FDVSEGDI-RFHDIPLTKLQlDSWRSRLA------------VVSQTPFlf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320614 270 --TVA------RMKTPQNRIKGVDREAyanhvtEVAMATYGLSHTRDTKVGNdlvRGV--SGGERKRVSIAEVAICGARF 339
Cdd:PRK10789 402 sdTVAnnialgRPDATQQEIEHVARLA------SVHDDILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEI 472
|
170 180
....*....|....*....|...
gi 6320614 340 QCWDNATRGLDSATALEFIRALK 362
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLR 495
|
|
| |
