|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
100-1503 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 2513.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 100 ENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPM 179
Cdd:TIGR00956 1 EEFNAKAWVKNFRKLIDSDPIYYKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRDTKTFDILKPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 180 DGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLV 259
Cdd:TIGR00956 81 DGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 260 TVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGL 339
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 340 DSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLT 419
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 420 SVTSPSERTLNKDMLKKgihIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDE-ASREAIKEAHIAKQSKRARPSSPYT 498
Cdd:TIGR00956 321 SLTSPAERQIKPGYEKK---VPRTPQEFETYWRNSPEYAQLMKEIDEYLDRCSEsDTKEAYRESHVAKQSKRTRPSSPYT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 499 VSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKIMKkgDTSTFYFRGSAMFFAILFNAFSSLLEIFSL 578
Cdd:TIGR00956 398 VSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPK--NTSDFYSRGGALFFAILFNAFSSLLEIASM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 579 YEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGS 658
Cdd:TIGR00956 476 YEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 659 LTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISST 738
Cdd:TIGR00956 556 VTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYDNLGVT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 739 ESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKK 818
Cdd:TIGR00956 636 NKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 819 RGVLTEKNANDPENVGE--RSDLSSDRKMLQESSEEESDTygeiglskSEAIFHWRNLCYEVQIKAETRRILNNVDGWVK 896
Cdd:TIGR00956 716 AGETSASNKNDIEAGEVlgSTDLTDESDDVNDEKDMEKES--------GEDIFHWRNLTYEVKIKKEKRVILNNVDGWVK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 897 PGTLTALMGASGAGKTTLLDCLAERVTMGVIT-GDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPA 975
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERVTTGVITgGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPK 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 976 EVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKK 1055
Cdd:TIGR00956 868 SVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRK 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1056 LANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGS 1135
Cdd:TIGR00956 948 LADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGA 1027
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1136 HANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIF 1215
Cdd:TIGR00956 1028 HANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIF 1107
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1216 NQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWISFIFAQIFVEVPWNIL 1295
Cdd:TIGR00956 1108 AALFIGFTFFKVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLV 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1296 AGTIAYFIYYYPIGFYSNASAAGQLHERGALFWLFSCAFYVYVGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTT 1375
Cdd:TIGR00956 1188 AGTIFFFIWYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAP 1267
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1376 PSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDVKCADYELLEFTPPSGMTCGQYMEPYLQLAKtGYLTDENATDTCSFC 1455
Cdd:TIGR00956 1268 PSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAG-GYLLNPNATDSCSFC 1346
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|....*...
gi 398365429 1456 QISTTNDYLANVNSFYSERWRNYGIFICYIAFNYIAGVFFYWLARVPK 1503
Cdd:TIGR00956 1347 QYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
148-1400 |
1.18e-153 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 505.92 E-value: 1.18e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 148 TVVNIPYKILKSGLRKFQ-RSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGfDLGADTKISYSGY 226
Cdd:PLN03140 152 TLPNAARNIAESALGMLGiNLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDP-SLKVSGEITYNGY 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 227 SGDDIKKhfRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRI----KGVDRESYANHL--AEV-------AMA---- 289
Cdd:PLN03140 231 RLNEFVP--RKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTRYdllsELARREKDAGIFpeAEVdlfmkatAMEgvks 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 290 ---------TYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALktQADISNT 360
Cdd:PLN03140 309 slitdytlkILGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL--QQIVHLT 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 361 SATV--AIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERT---LNKDMLK 435
Cdd:PLN03140 387 EATVlmSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEqywADRNKPY 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 436 KGIHIPQTPKEMNDYWVKSPNYKELMKEVDQrllnddeasreaikeahiAKQSKRARPSSPYTVSYMMQVKYLLIRNMWR 515
Cdd:PLN03140 467 RYISVSEFAERFKSFHVGMQLENELSVPFDK------------------SQSHKAALVFSKYSVPKMELLKACWDKEWLL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 516 LRNNIGFTLFMILGNCSMALILGSMFFK----IMKKGDTSTFYfrgSAMFFAILFNAFSSLLEIFSLYEARPITEKHRTY 591
Cdd:PLN03140 529 MKRNAFVYVFKTVQIIIVAAIASTVFLRtemhTRNEEDGALYI---GALLFSMIINMFNGFAELALMIQRLPVFYKQRDL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 592 sLYHPS-ADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPA 670
Cdd:PLN03140 606 -LFHPPwTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGG 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 671 SMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFhgikfpcaeYVPRgpaYANISSTESVCTVVGAVpg 750
Cdd:PLN03140 685 ALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEM---------FAPR---WMNKMASDNSTRLGTAV-- 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 751 qdyvlgddfiRGTYQYYHKDKWRGFGIG--MAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNAN 828
Cdd:PLN03140 751 ----------LNIFDVFTDKNWYWIGVGalLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEEDSIPRSLSSA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 829 DPENVGERSDLS-SDRKMLQESSEEESDTYGEIGLSKSEAI------FHWRNLCYEVQIKAETR---------RILNNVD 892
Cdd:PLN03140 821 DGNNTREVAIQRmSNPEGLSKNRDSSLEAANGVAPKRGMVLpftplaMSFDDVNYFVDMPAEMKeqgvtedrlQLLREVT 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 893 GWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIP-RDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYL 971
Cdd:PLN03140 901 GAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFL 980
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 972 RQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAG-EGLNVEQRKRLTIGVELTAKPKLlVFLDEPTSGLDSQTAWSIC 1050
Cdd:PLN03140 981 RLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSI-IFMDEPTSGLDARAAAIVM 1059
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1051 QLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFES-HGAHKCPADANPAEWMLEVV 1129
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAiPGVPKIKEKYNPATWMLEVS 1139
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1130 GAAPGSHANQDYYEVWRNSEEY---RAVQSELdwmerELPKKGsitaAEDKH---EFSQSIIYQTKLVSIRLFQQYWRSP 1203
Cdd:PLN03140 1140 SLAAEVKLGIDFAEHYKSSSLYqrnKALVKEL-----STPPPG----ASDLYfatQYSQSTWGQFKSCLWKQWWTYWRSP 1210
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1204 DYLWSKFILTIFNQLFIGFTFFKAGT------SLQGLQNQMLAVFMFTVIFNPILQQylPSFVQQRDLYeARERPSRTFS 1277
Cdd:PLN03140 1211 DYNLVRFFFTLAAALMVGTIFWKVGTkrsnanDLTMVIGAMYAAVLFVGINNCSTVQ--PMVAVERTVF-YRERAAGMYS 1287
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1278 WISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASaagqlhergALFWL-----FSCAFYVYVGSMGLLVISFNQVA 1352
Cdd:PLN03140 1288 ALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAA---------KFFWFyfisfFSFLYFTYYGMMTVSLTPNQQVA 1358
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*...
gi 398365429 1353 ESAANLASLLFTMslsFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALL 1400
Cdd:PLN03140 1359 AIFAAAFYGLFNL---FSGFFIPRPKIPKWWVWYYWICPVAWTVYGLI 1403
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
868-1094 |
6.41e-111 |
|
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: 348.46 E-value: 6.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 868 IFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIG 947
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 948 YCQQQDLHLKTATVRESLRFSAYLRqpaevsieeknryveevikilemekyadavvgvageGLNVEQRKRLTIGVELTAK 1027
Cdd:cd03232 83 YVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1028 PkLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFG 1094
Cdd:cd03232 127 P-SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
849-1424 |
4.64e-85 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 291.95 E-value: 4.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 849 SSEEESDTYGEIGLSKSEAIFHWRN-LCYEVQikAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV- 926
Cdd:TIGR00955 3 YSWRNSDVFGRVAQDGSWKQLVSRLrGCFCRE--RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 927 ITGDILVNGIPRDKSFPRSI-GYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGV 1005
Cdd:TIGR00955 81 GSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1006 AG--EGLNVEQRKRLTIGVELTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLF 1083
Cdd:TIGR00955 161 PGrvKGLSGGERKRLAFASELLTDPPLL-FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1084 MQrGGKTVYFGDLGEGCktmiDYFESHGaHKCPADANPAEWMLEVVGAAPGSHAN-----QDYYEVWRNSEEYRAVQSEL 1158
Cdd:TIGR00955 240 MA-EGRVAYLGSPDQAV----PFFSDLG-HPCPENYNPADFYVQVLAVIPGSENEsreriEKICDSFAVSDIGRDMLVNT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1159 DWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQM 1238
Cdd:TIGR00955 314 NLWSGKAGGLVKDSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1239 LAVFMFtvIFNPILQQYLPS---FVQQRDLYeARERPSRTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNAS 1315
Cdd:TIGR00955 394 GALFLF--LTNMTFQNVFPVinvFTAELPVF-LRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGAT 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1316 aagqlherGALFWLFSCAFYVYVG-SMGLL---VISFNQVAESAANLASLLFtmsLSFCGVMTTPSAMPRFWIFMYRVSP 1391
Cdd:TIGR00955 471 --------HFLTFLFLVTLVANVAtSFGYLiscAFSSTSMALTVGPPFVIPF---LLFGGFFINSDSIPVYFKWLSYLSW 539
|
570 580 590
....*....|....*....|....*....|....
gi 398365429 1392 LTYFIQALLAVGVANVDV-KCADYELLEFTPPSG 1424
Cdd:TIGR00955 540 FRYGNEGLLINQWSDVDNiECTSANTTGPCPSSG 573
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
164-392 |
6.82e-80 |
|
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: 261.81 E-value: 6.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 164 FQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFdLGADTKISYSGYSGDDIKKHFRGEVVYNA 243
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 244 EADVHLPHLTVFETLVTVARLKtpqnrikgvdresyanhlaevamatyglshtrntkvGNDIVRGVSGGERKRVSIAEVS 323
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 324 ICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYG 392
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
869-1094 |
1.58e-66 |
|
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: 223.20 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 869 FHWRNLCYEVQIKAET--RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDK-SFPRS 945
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 946 IGYCQQQDLHLKTATVRESLRFSAYLRqpaevsieeknryveevikilemekyadavvgvageGLNVEQRKRLTIGVELT 1025
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1026 AKPKLLvFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRgGKTVYFG 1094
Cdd:cd03213 128 SNPSLL-FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
130-719 |
1.14e-59 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 217.61 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 130 AWKNLSAsgasadvaYQSTVVNIPYKILKSGLRKfQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISS- 208
Cdd:TIGR00955 4 SWRNSDV--------FGRVAQDGSWKQLVSRLRG-CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 209 NTHGFDLGADTKISysgysGDDI-KKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVa 287
Cdd:TIGR00955 75 SPKGVKGSGSVLLN-----GMPIdAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 288 matyGLSHTRNTKVGN-DIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADiSNTSATVAI 366
Cdd:TIGR00955 149 ----GLRKCANTRIGVpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 367 YQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSV--TSPSERTLNKDMLKKGIHIPQTP 444
Cdd:TIGR00955 224 HQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVlaVIPGSENESRERIEKICDSFAVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 445 KEMNDyWVKSPNYKELMkevDQRLLNDDEASreaikeahiakqskrarPSSPYTVSYMMQVKYLLIRNMWRLRNNIGFTL 524
Cdd:TIGR00955 304 DIGRD-MLVNTNLWSGK---AGGLVKDSENM-----------------EGIGYNASWWTQFYALLKRSWLSVLRDPLLLK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 525 FMILGNCSMALILGSMFFKIMKKGDTSTfyFRGSAMFFAILFNAFSSLLEIFSLYEA-RPITEKHRTYSLYHPSADAFAS 603
Cdd:TIGR00955 363 VRLIQTMMTAILIGLIYLGQGLTQKGVQ--NINGALFLFLTNMTFQNVFPVINVFTAeLPVFLRETRSGLYRVSAYFLAK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 604 VLSEIPSKLIIAVCFNIIFYFLVDFRRNG-GVFFFYLLINIVAVFSMS--HLFRCVGSLTKTLSEAMVPASMLLLALSmy 680
Cdd:TIGR00955 441 TIAELPLFIILPALFTSITYWMIGLRSGAtHFLTFLFLVTLVANVATSfgYLISCAFSSTSMALTVGPPFVIPFLLFG-- 518
|
570 580 590
....*....|....*....|....*....|....*....
gi 398365429 681 tGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIK 719
Cdd:TIGR00955 519 -GFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVD 556
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
871-1094 |
1.65e-53 |
|
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: 187.09 E-value: 1.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 871 WRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVIT-GDILVNGIPRDKS-FPRSIGY 948
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKPDqFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 949 CQQQDLHLKTATVRESLRFSAYLRQPAEVSieekNRYVEEVIKILEMEKYADAVVG-VAGEGLNVEQRKRLTIGVELTAK 1027
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1028 PKLLvFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKtVYFG 1094
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1194-1402 |
3.15e-49 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 174.00 E-value: 3.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1194 RLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEaRERPS 1273
Cdd:pfam01061 4 REFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RELAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1274 RTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASaagqlheRGALFWLFSCAFYVYVGSMGLLVISFNQVAE 1353
Cdd:pfam01061 83 PLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAG-------RFFLFLLVLLLTALAASSLGLFISALAPSFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365429 1354 SAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAV 1402
Cdd:pfam01061 156 DASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
508-713 |
3.18e-46 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 165.14 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 508 LLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKImkkGDTSTFYFRGSAMFFAILFNAFSSLLEI-FSLYEARPITE 586
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL---GNQQGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 587 KHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEA 666
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365429 667 MVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLIN 713
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
167-717 |
6.33e-43 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 168.13 E-value: 6.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 167 SKETNTFQ---ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISysgysGDDIKKHFRGEVVYNA 243
Cdd:PLN03211 72 SDETRQIQertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILAN-----NRKPTKQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 244 EADVHLPHLTVFETLVTVARLKTPQNRIKGVDresyaNHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVS 323
Cdd:PLN03211 147 QDDILYPHLTVRETLVFCSLLRLPKSLTKQEK-----ILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 324 ICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATvAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFED 403
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVT-SMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFES 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 404 MGYVCPSRQTTADFLTSVTSpsertlnkdmlkkgiHIPQTPKEMNDywvKSPNYKE-LMKEVDQRLLNDDEASRE----- 477
Cdd:PLN03211 301 VGFSPSFPMNPADFLLDLAN---------------GVCQTDGVSER---EKPNVKQsLVASYNTLLAPKVKAAIEmshfp 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 478 AIKEAHIAKQSKRARPSSPYT--VSYMMQVKYLLIRNMwRLRNNIGFTLFMILGNCSMALILGSMFFkimkKGDTSTFYF 555
Cdd:PLN03211 363 QANARFVGSASTKEHRSSDRIsiSTWFNQFSILLQRSL-KERKHESFNTLRVFQVIAAALLAGLMWW----HSDFRDVQD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 556 RGSAMFF-AILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGV 634
Cdd:PLN03211 438 RLGLLFFiSIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 635 FFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIpkKKILRWSKWIWYINPLAYLFEsLLINE 714
Cdd:PLN03211 518 FLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYR-LLINV 594
|
...
gi 398365429 715 FHG 717
Cdd:PLN03211 595 QYG 597
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
883-1128 |
9.84e-40 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 158.50 E-value: 9.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVR 962
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAG-EGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGL 1041
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLI-LDEPTSGL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1042 DSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRgGKTVYFGDLGEGcktmIDYFESHGAHkcPA-DAN 1120
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGKGSDA----MAYFESVGFS--PSfPMN 310
|
....*...
gi 398365429 1121 PAEWMLEV 1128
Cdd:PLN03211 311 PADFLLDL 318
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
866-1094 |
1.55e-39 |
|
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: 145.87 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 866 EAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV-ITGDILVNGIPRDK---S 941
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPYKEfaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 FPRSIGYCQQQDLHLKTATVRESLRFSAYLRqpaevsieeKNRYVeevikilemekyadavvgvagEGLNVEQRKRLTIG 1021
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCK---------GNEFV---------------------RGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1022 VELTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIHQPSAILMQEFDRLLFMqRGGKTVYFG 1094
Cdd:cd03233 131 EALVSRASVL-CWDNSTRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
176-336 |
2.23e-33 |
|
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: 126.22 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 176 LKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGfDLGadtKISYSGYS-GDDIKKHFRGEVVYNAEADVHLPHLTV 254
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-TEG---TILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 255 FETLVTVARLKTPQNRIKGVDresyanhlAEVAMATYGLSHTRNTKVGNdIVRGVSGGERKRVSIAEVSICGSKFQCWDN 334
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDAR--------AEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
..
gi 398365429 335 AT 336
Cdd:pfam00005 148 PT 149
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
885-1098 |
1.29e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.10 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNGIPRDKSFP---RSIGYCQQQDLHLKT 958
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML-----LGLLRptsGEVRVLGEDVARDPAevrRRIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRqpaEVSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLvFLDEPT 1038
Cdd:COG1131 88 LTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELL-ILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTIHqpsaiLMQE----FDRLLFMqRGGKTVYFGDLGE 1098
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTH-----YLEEaerlCDRVAII-DKGRIVADGTPDE 217
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
726-817 |
2.70e-32 |
|
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: 121.03 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 726 VPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEI 805
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
90
....*....|..
gi 398365429 806 LVFPRSIVKRMK 817
Cdd:pfam06422 81 LVFKRGKAPKLK 92
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
171-721 |
7.36e-32 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 136.13 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 171 NTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKIsySGYSgddiKKH--FRGEVVYNAEADVH 248
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRI--SGFP----KKQetFARISGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 249 LPHLTVFETLVTVARLKTPqnriKGVDRESYANHLAEVaMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSK 328
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLP----KEVSKEEKMMFVDEV-MELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 329 FQCWDNATRGLDSATALEFIRALKTQADISNTsATVAIYQCSQDAYDLFNKVCVLDDGYQ-IYYGP----ADKAKKYFED 403
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRT-VVCTIHQPSIDIFEAFDELLLMKRGGQvIYSGPlgrnSHKIIEYFEA 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 404 MGYV--CPSRQTTADFLTSVTSPSERtlnkdmLKKGIhipqtpkEMNDYWVKSPNY---KELMKEVdqrllnddEASREA 478
Cdd:PLN03140 1119 IPGVpkIKEKYNPATWMLEVSSLAAE------VKLGI-------DFAEHYKSSSLYqrnKALVKEL--------STPPPG 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 479 IKEAHIAKQskrarpsspYTVSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKI-MKKGDTSTFYFRG 557
Cdd:PLN03140 1178 ASDLYFATQ---------YSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVgTKRSNANDLTMVI 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 558 SAMFFAILF---NAFSSLLEIFSLyeARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGV 634
Cdd:PLN03140 1249 GAMYAAVLFvgiNNCSTVQPMVAV--ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAK 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 635 FFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWskWIWY--INPLAYLFESLLI 712
Cdd:PLN03140 1327 FFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKW--WVWYywICPVAWTVYGLIV 1404
|
....*....
gi 398365429 713 NEFHGIKFP 721
Cdd:PLN03140 1405 SQYGDVEDT 1413
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
159-392 |
2.79e-31 |
|
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: 121.89 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 159 SGLRKFQRSKETN-TFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGfdLGADTKISYSGYSGDdiKKHFRG 237
Cdd:cd03213 7 RNLTVTVKSSPSKsGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTG--LGVSGEVLINGRPLD--KRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 238 EVVYNAEADVHLPHLTVFETLVTVARLktpqnrikgvdresyanhlaevamatyglshtrntkvgndivRGVSGGERKRV 317
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKL------------------------------------------RGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 318 SIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADiSNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYG 392
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
872-1087 |
4.52e-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: 116.03 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQikAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERvtMGVITGDILVNGIPRDKS----FPRSIG 947
Cdd:cd03225 3 KNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGPTSGEVLVDGKDLTKLslkeLRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 948 YC-QQQDLHLKTATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTA 1026
Cdd:cd03225 79 LVfQNPDDQFFGPTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1027 KPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSaILMQEFDRLLFMQRG 1087
Cdd:cd03225 152 DPDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
885-1098 |
7.00e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.88 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGIP---RDKSFPRSIGYCQQQD-LHlKTAT 960
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEDvrkEPREARRQIGVLPDERgLY-DRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSG 1040
Cdd:COG4555 91 VRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLL-LDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1041 LDSQTAWSICQLMKKLANHGQAILCTIHQpsailMQE----FDRLLFMQRgGKTVYFGDLGE 1098
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHI-----MQEvealCDRVVILHK-GKVVAQGSLDE 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
157-392 |
7.83e-28 |
|
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: 113.13 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 157 LKSGLRKFQrsKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKisySG---YSGDDIKK 233
Cdd:cd03234 6 WWDVGLKAK--NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS----GRVEGGGTT---SGqilFNGQPRKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 234 H-FRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESyanhlaevaMATYGLSHTRNTKVGNDIVRGVSGG 312
Cdd:cd03234 77 DqFQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKR---------VEDVLLRDLALTRIGGNLVKGISGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 313 ERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADiSNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYG 392
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
884-1087 |
2.24e-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: 111.44 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGI---PRDKSFPRSIGYCQQQDLHLKTAT 960
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGYsirTDRKAARQSLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKlLVFLDEPTSG 1040
Cdd:cd03263 92 VREHLRFYARLKG---LPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPS-VLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1041 LDSQTAWSICQLMKKLAnHGQAILCTIHQpsailMQEF----DRLLFMQRG 1087
Cdd:cd03263 164 LDPASRRAIWDLILEVR-KGRSIILTTHS-----MDEAealcDRIAIMSDG 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
885-1098 |
6.81e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRDKSFPRsIGYCQQQ---DLHLKt 958
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLL-----KAILGLLpptSGTVRLFGKPPRRARRR-IGYVPQRaevDWDFP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRQPAE--VSIEEKNRyVEEVIKILEMEKYADAVVGvageglnvE----QRKRLTIGVELTAKPKLLV 1032
Cdd:COG1121 92 ITVRDVVLMGRYGRRGLFrrPSRADREA-VDEALERVGLEDLADRPIG--------ElsggQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 1033 fLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlMQEFDRLLFMQRGgkTVYFGDLGE 1098
Cdd:COG1121 163 -LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAV-REYFDRVLLLNRG--LVAHGPPEE 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
872-1095 |
9.04e-27 |
|
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: 110.11 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQikaETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRDKSFP----R 944
Cdd:COG1122 4 ENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLL-----RLLNGLLkptSGEVLVDGKDITKKNLrelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 945 SIGYC-QQQDLHLKTATVRESLRFSayLRQpAEVSIEEKNRYVEEVIKILEMEKYADAVV-----GvageglnveQRKRL 1018
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEDVAFG--PEN-LGLPREEIRERVEEALELVGLEHLADRPPhelsgG---------QKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1019 TI-GVeLTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILmQEFDRLLFMQRgGKTVYFGD 1095
Cdd:COG1122 144 AIaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVA-ELADRVIVLDD-GRIVADGT 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
872-1087 |
1.55e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 106.67 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP------RDKSFP 943
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVLIDGQDisslseRELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 944 R--SIGYcqqQDLHL-KTATVRESLRFSAYLrqpAEVSIEEKNRYVEEVIKILEMEKYADAVVGvageglnvE----QRK 1016
Cdd:COG1136 84 RrrHIGFv-fQFFNLlPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPS--------QlsggQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1017 RLTIGVELTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSaiLMQEFDRLLFMQRG 1087
Cdd:COG1136 152 RVAIARALVNRPKLI-LADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
872-1087 |
1.59e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.03 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP------RDKSFP 943
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVRVDGTDisklseKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 944 R--SIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILE-MEKYADAVVGVageglnveQRKRLTI 1020
Cdd:cd03255 80 RrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDrLNHYPSELSGG--------QQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1021 GVELTAKPKlLVFLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSaiLMQEFDRLLFMQRG 1087
Cdd:cd03255 152 ARALANDPK-IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
885-1082 |
2.11e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 105.64 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDK---SFPRSIGYCQQQDlHLKT 958
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPpsaGEVLWNGEPIRDareDYRRRLAYLGHAD-GLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 A-TVRESLRFSAYLRQPAEVSIEeknryVEEVIKILEMEKYADAVVGV--AGeglnveQRKRLTIGVELTAKPKLLVfLD 1035
Cdd:COG4133 89 ElTVRENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQlsAG------QKRRVALARLLLSPAPLWL-LD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365429 1036 EPTSGLDSQT-AWsICQLMKKLANHGQAILCTIHQPSAIlmqEFDRLL 1082
Cdd:COG4133 157 EPFTALDAAGvAL-LAELIAAHLARGGAVLLTTHQPLEL---AAARVL 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
883-1091 |
8.13e-25 |
|
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: 103.88 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPR-DKSFPRSIGYCQQQ-DLHLK 957
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLA-----KILAGLIkesSGSILLNGKPIkAKERRKSIGYVMQDvDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAYLrqpaevsIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVFlDEP 1037
Cdd:cd03226 86 TDSVREELLLGLKE-------LDAGNEQAETVLKDLDLYALKERHPLSLSGG----QKQRLAIAAALLSGKDLLIF-DEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1038 TSGLDSQTAWSICQLMKKLANHGQAILCTIHQPsailmqEF-----DRLLFMqRGGKTV 1091
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDY------EFlakvcDRVLLL-ANGAIV 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
882-1087 |
1.44e-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: 110.23 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 882 AETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIPRD----KSFPRSIGYCQQQDlHLK 957
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVDLSdldpASWRRQIAWVPQNP-YLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAylrqpAEVSIEEKNR-----YVEEVIKILEmEKYaDAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLV 1032
Cdd:COG4988 424 AGTIRENLRLGR-----PDASDEELEAaleaaGLDEFVAALP-DGL-DTPLGEGGRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1033 fLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTiHQPSaiLMQEFDRLLFMQRG 1087
Cdd:COG4988 497 -LDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLDDG 547
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
888-1039 |
1.98e-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: 100.80 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIP----RDKSFPRSIGYCQQQDLHLKTATVRE 963
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDltddERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 964 SLRFSAYLRqpaEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLvFLDEPTS 1039
Cdd:pfam00005 79 NLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL-LLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
884-1087 |
4.67e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 100.55 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNGIP---RDKSFPRSIGYCQQQDLHLK 957
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII-----LGLLKpdsGEIKVLGKDikkEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAylrqpaevsieeknryveevikilemekyadavvGvageglnveQRKRLTIGVELTAKPKLLvFLDEP 1037
Cdd:cd03230 87 NLTVRENLKLSG----------------------------------G---------MKQRLALAQALLHDPELL-ILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1038 TSGLDSQTAWSICQLMKKLANHGQAILCTIHqpsaiLMQE----FDRLLFMQRG 1087
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSH-----ILEEaerlCDRVAILNNG 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
885-1094 |
1.48e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.60 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNGIPRDKSfPRSIGYCQQQDLHLKT--A 959
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLL-----KAILGLLKptsGSIRVFGKPLEKE-RKRIGYVPQRRSIDRDfpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRE--SLRFSAYLRQPAEVSIEEKNRyVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEP 1037
Cdd:cd03235 86 SVRDvvLMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGG----QQQRVLLARALVQDPDLLL-LDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1038 TSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAiLMQEFDRLLFMQRGGktVYFG 1094
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRTV--VASG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
886-1087 |
4.45e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 96.05 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGIPRDKsfpRSIGYCQQQDL---HLkta 959
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPDSGEILiDGRDVTGVPPER---RNIGMVFQDYAlfpHL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPAEVSIEEKnryVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELTAKPKLLvFLDEPTS 1039
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRAR---VRELLELVGLEGLLNRYP----HELSGGQQQRVALARALAREPSLL-LLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365429 1040 GLDSQTAWSICQLMKKL-ANHG-QAILCTIHQPSAILMQefDRLLFMQRG 1087
Cdd:cd03259 160 ALDAKLREELREELKELqRELGiTTIYVTHDQEEALALA--DRIAVMNEG 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
877-1087 |
6.66e-22 |
|
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: 93.85 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 877 EVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKSFP----RSIGYC 949
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-----GLLKptsGEILIDGKDIAKLPLeelrRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 950 QQqdlhlktatvreslrfsaylrqpaevsieeknryveevikilemekyadavvgvagegLNVEQRKRLTIGVELTAKPK 1029
Cdd:cd00267 79 PQ----------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1030 LLvFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSaILMQEFDRLLFMQRG 1087
Cdd:cd00267 101 LL-LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
887-1087 |
1.18e-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: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIPRDK----SFPRSIGYCqQQDLHLKTAT 960
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglYEPT----SGRILIDGIDLRQidpaSLRRQIGVV-LQDVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAylrqpAEVSIEEknryVEEVIK-------ILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLvF 1033
Cdd:COG2274 565 IRENITLGD-----PDATDEE----IIEAARlaglhdfIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL-I 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLANHgqailCTI----HQPSAIlmQEFDRLLFMQRG 1087
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKG-----RTViiiaHRLSTI--RLADRIIVLDKG 685
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
882-1087 |
6.23e-21 |
|
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: 99.07 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 882 AETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGDILVNGIP----RDKSFPRSIGYCQQqDL 954
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-----LRFLdpqSGSITLGGVDlrdlDEDDLRRRIAVVPQ-RP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 955 HLKTATVRESLRFSAylrqpAEVSIEEknryVEEVIKILEMEKYA-------DAVVGVAGEGLNVEQRKRLTIGVELTAK 1027
Cdd:COG4987 419 HLFDTTLRENLRLAR-----PDATDEE----LWAALERVGLGDWLaalpdglDTWLGEGGRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1028 PKLLVfLDEPTSGLDSQTAWSICQLMKKLAnHGQAILCTIHQPSAilMQEFDRLLFMQRG 1087
Cdd:COG4987 490 APILL-LDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAG--LERMDRILVLEDG 545
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
872-1094 |
1.79e-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: 90.57 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQikaeTRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPrdksfprsigy 948
Cdd:cd03214 3 ENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-----GLLkpsSGEILLDGKD----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 949 cqqqdlhLKTATVRESLRFSAYLRQpaevsieeknryveeVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKP 1028
Cdd:cd03214 63 -------LASLSPKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGG----ERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1029 KLLvFLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIHQPSAILmQEFDRLLFMQrGGKTVYFG 1094
Cdd:cd03214 117 PIL-LLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAA-RYADRVILLK-DGRIVAQG 180
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
884-1084 |
2.06e-20 |
|
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: 96.97 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGIPRD----KSFPRSIGYCQQQDlHLKTA 959
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVPLAdadaDSWRDQIAWVPQHP-FLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILemEKYADAVVGVAGEGLNVEQRKRLTIGVELtAKPKLLVFLDEPTS 1039
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREALERAGLDEFVAAL--PQGLDTPIGEGGAGLSGGQAQRLALARAF-LRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365429 1040 GLDSQTAWSICQLMKKLANhGQAILCTIHQPSaiLMQEFDRLLFM 1084
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
885-1095 |
6.62e-20 |
|
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: 90.87 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIP----RDKSFPRSIGYCQQQDLHLK 957
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLKpssGEVLLDGRDlaslSRRELARRIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAY-----LRQPAEVSIEEknryVEEVIKILEMEKYADAVV-----GvageglnveQRKRLTIGVELTAK 1027
Cdd:COG1120 89 GLTVRELVALGRYphlglFGRPSAEDREA----VEEALERTGLEHLADRPVdelsgG---------ERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1028 PKLLvFLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSaILMQEFDRLLFMqRGGKTVYFGD 1095
Cdd:COG1120 156 PPLL-LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLN-LAARYADRLVLL-KDGRIVAQGP 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
887-1088 |
7.84e-20 |
|
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: 90.37 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIP-RD---KSFPRSIGYCqQQDLHLKTATVR 962
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD--VDSGRILIDGHDvRDytlASLRRQIGLV-SQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAYLRQPAEVSIEEKNRYVEEVIKilEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLD 1042
Cdd:cd03251 94 ENIAYGRPGATREEVEEAARAANAHEFIM--ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI-LDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365429 1043 SQTAWSICQLMKKLANHGQAILCTiHQPSAIlmQEFDRLLFMQRGG 1088
Cdd:cd03251 171 TESERLVQAALERLMKNRTTFVIA-HRLSTI--ENADRIVVLEDGK 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
883-1087 |
9.07e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.23 E-value: 9.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeR---VTmgviTGDILVNGIP-RD---KSFPRSIGYCqQQDLH 955
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL-RfydPT----SGRILIDGVDiRDltlESLRRQIGVV-PQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRFSAylrqpAEVSIEEknryVEEVIK-------ILEMEK-YaDAVVGVAGEGLNVEQRKRLTIGVELTAK 1027
Cdd:COG1132 425 LFSGTIRENIRYGR-----PDATDEE----VEEAAKaaqahefIEALPDgY-DTVVGERGVNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1028 PKLLVfLDEPTSGLDSQTAWSICQLMKKLAnHGQAILcTI-HQPSAIlmQEFDRLLFMQRG 1087
Cdd:COG1132 495 PPILI-LDEATSALDTETEALIQEALERLM-KGRTTI-VIaHRLSTI--RNADRILVLDDG 550
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
888-1087 |
1.03e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.80 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDIL-----VNGIPRDKSFPRSIGYCQQQDLHLKTA 959
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-----GFLRptsGSVLfdgedITGLPPHEIARLGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQP-------AEVSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLv 1032
Cdd:cd03219 91 TVLENVMVAAQARTGsglllarARREEREARERAEELLERVGLADLADRPAG----ELSYGQQRRLEIARALATDPKLL- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1033 FLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlMQEFDRLLFMQRG 1087
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV-MSLADRVTVLDQG 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
872-1087 |
1.38e-19 |
|
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: 87.44 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYevQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNGIP----RDKSFPR 944
Cdd:cd03228 4 KNVSF--SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-----LRLYDptsGEILIDGVDlrdlDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 945 SIGYCqQQDLHLKTATVRESLrFSAylrqpaevsieeknryveevikilemekyadavvGvageglnveQRKRLTIGVEL 1024
Cdd:cd03228 77 NIAYV-PQDPFLFSGTIRENI-LSG----------------------------------G---------QRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1025 TAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTiHQPSAILMqeFDRLLFMQRG 1087
Cdd:cd03228 112 LRDPPILI-LDEATSALDPETEALILEALRALAKGKTVIVIA-HRLSTIRD--ADRIIVLDDG 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
879-1094 |
1.77e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.58 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 879 QIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGI-----PRDKSfpRSIGYCQ 950
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTL-----RMLAGLLepdAGFATVDGFdvvkePAEAR--RRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 951 QQDLHLKTATVRESLRFSAYLR--QPAEVsieeKNRyVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKP 1028
Cdd:cd03266 85 DSTGLYDRLTARENLEYFAGLYglKGDEL----TAR-LEELADRLGMEELLDRRVG----GFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1029 KLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHqpsaiLMQEF----DRLLFMQRgGKTVYFG 1094
Cdd:cd03266 156 PVLL-LDEPTTGLDVMATRALREFIRQLRALGKCILFSTH-----IMQEVerlcDRVVVLHR-GRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
895-1094 |
1.96e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.49 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRDKSFPRSIGYC-QQQDLHLKTaTVRESLRFSAY 970
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTI-----RMILGIIlpdSGEVLFDGKPLDIAARNRIGYLpEERGLYPKM-KVIDQLVYLAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 971 LRqpaEVSIEEKNRYVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSIC 1050
Cdd:cd03269 97 LK---GLKKEEARRRIDEWLERLELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLI-LDEPFSGLDPVNVELLK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365429 1051 QLMKKLANHGQAILCTIHQpsailMQEFDRL---LFMQRGGKTVYFG 1094
Cdd:cd03269 169 DVIRELARAGKTVILSTHQ-----MELVEELcdrVLLLNKGRAVLYG 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
897-1087 |
3.58e-19 |
|
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: 87.74 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 897 PGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKS-----FP---RSIGYC-QQQDL--HLktaTVR 962
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-----GLEKpdgGTIVLNGTVLFDSrkkinLPpqqRKIGLVfQQYALfpHL---NVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAYLRQPAEVSIEeknryVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLD 1042
Cdd:cd03297 94 ENLAFGLKRKRNREDRIS-----VDELLDLLGLDHLLNRYPA----QLSGGEKQRVALARALAAQPELLL-LDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365429 1043 SQTAWSICQLMKKLANHGQ--AILCTiHQPSAILMQEfDRLLFMQRG 1087
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNipVIFVT-HDLSEAEYLA-DRIVVMEDG 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
872-1087 |
5.45e-19 |
|
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: 87.94 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP----RDKSFPRS 945
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPW----SGEVTFDGRPvtrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 946 IGYCQQQ---DLH-LKT--ATVRESLRfsaylrqpaevsIEEKNRYVEEVIKILE--------MEKYADAVVGvageGln 1011
Cdd:COG1124 81 VQMVFQDpyaSLHpRHTvdRILAEPLR------------IHGLPDREERIAELLEqvglppsfLDRYPHQLSG----G-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1012 veQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAIlmqEF--DRLLFMQRG 1087
Cdd:COG1124 143 --QRQRVAIARALILEPELLL-LDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVV---AHlcDRVAVMQNG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
866-1087 |
5.66e-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: 92.27 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 866 EAIFHWRNLcyEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTM-GVITGDILVNGIPRDKSFP- 943
Cdd:COG1123 2 TPLLEVRDL--SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHgGRISGEVLLDGRDLLELSEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 944 ---RSIGYC-QQQDLHLKTATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLT 1019
Cdd:COG1123 80 lrgRRIGMVfQDPMTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGG----QRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1020 IGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAILmQEFDRLLFMQRG 1087
Cdd:COG1123 153 IAMALALDPDLLI-ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVA-EIADRVVVMDDG 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
878-1098 |
7.11e-19 |
|
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: 87.83 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 878 VQIKAETRRILNNVDgW-VKPGTLTALMGASGAGKTTLLdclaervtmGVITGD--------ILVNGIPRDKS--FP--R 944
Cdd:COG1119 9 VTVRRGGKTILDDIS-WtVKPGEHWAILGPNGAGKSTLL---------SLITGDlpptygndVRLFGERRGGEdvWElrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 945 SIGYCQQqDLHLK---TATVRESLR--FSAYLRQPAEVSIEEKNRyVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLT 1019
Cdd:COG1119 79 RIGLVSP-ALQLRfprDETVLDVVLsgFFDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQG----EQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1020 IGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHG--QAILCTiHQPSAILmQEFDRLLFMqRGGKTVYFGDLG 1097
Cdd:COG1119 153 IARALVKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEEIP-PGITHVLLL-KDGRVVAAGPKE 228
|
.
gi 398365429 1098 E 1098
Cdd:COG1119 229 E 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
883-1087 |
1.42e-18 |
|
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: 86.51 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNGIP-RD---KSFPRSIGYCqQQDLH 955
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-----MRFYDpqkGQILIDGIDiRDisrKSLRSMIGVV-LQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILemEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLD 1035
Cdd:cd03254 88 LFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKL--PNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI-LD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLaNHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTI--KNADKILVLDDG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
885-1087 |
3.08e-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: 83.78 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP------RDKSFPRSIGYCQQQDLHL 956
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPD----SGSILIDGEDltdledELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 KTATVRESLRFsaylrqpaevsieeknryveevikilemekyadavvgvageGLNVEQRKRLTIGVELTAKPKLLvFLDE 1036
Cdd:cd03229 89 PHLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVL-LLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1037 PTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPS-AILMQefDRLLFMQRG 1087
Cdd:cd03229 127 PTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDeAARLA--DRVVVLRDG 177
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
885-1042 |
4.46e-18 |
|
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: 84.55 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGtLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNG--IPRDKSFPRS-IGYCQQQDLHLKT 958
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA-----TLTPpssGTIRIDGqdVLKQPQKLRRrIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRqpaEVSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLVfLDEPT 1038
Cdd:cd03264 87 FTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILI-VDEPT 158
|
....
gi 398365429 1039 SGLD 1042
Cdd:cd03264 159 AGLD 162
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
881-1087 |
4.51e-18 |
|
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: 85.23 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaerVTMGVIT-GDILVNG----IPRDKSFPRSIGYCQQQDLh 955
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI---QRFYVPEnGRVLVDGhdlaLADPAWLRRQVGVVLQENV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRfsayLRQPAeVSIEEknryVEEVIK-------ILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKP 1028
Cdd:cd03252 87 LFNRSIRDNIA----LADPG-MSMER----VIEAAKlagahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1029 KLLVFlDEPTSGLDSQTAWSICQLMKKLANhGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:cd03252 158 RILIF-DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
884-1092 |
6.68e-18 |
|
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: 83.81 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGDILVNG--IPRDKSFPRSIG--------Ycq 950
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII-----LGLIkpdSGEITFDGksYQKNIEALRRIGalieapgfY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 951 qqdLHLktaTVRESLRFSAYLRQpaevsIEEKNryVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKL 1030
Cdd:cd03268 85 ---PNL---TARENLRLLARLLG-----IRKKR--IDEVLDVVGLKDSAKKKVK----GFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1031 LVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlMQEFDRLLFMqRGGKTVY 1092
Cdd:cd03268 148 LI-LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEI-QKVADRIGII-NKGKLIE 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
886-1064 |
1.30e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 84.32 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKSFPRSIgyCQQ------QDLHL 956
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYRptsGRILFDGRDITGLPPHRI--ARLgiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 -KTATVRESLR-----------FSAYLRQPAEVSIEEKNR-YVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVE 1023
Cdd:COG0411 91 fPELTVLENVLvaaharlgrglLAALLRLPRARREEREAReRAEELLERVGLADRADEPAG----NLSYGQQRRLEIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398365429 1024 LTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKL-ANHGQAIL 1064
Cdd:COG0411 167 LATEPKLL-LLDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
886-1087 |
1.75e-17 |
|
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: 83.19 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAE--RVTMGVITgdilVNG--IPRD-KSFPRSIGYCQQQDLHLKTAT 960
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSGRAT----VAGhdVVREpREVRRRIGIVFQDLSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLrqpAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLnveqRKRLTIGVELTAKPKLLvFLDEPTSG 1040
Cdd:cd03265 90 GWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1041 LDSQTAWSICQLMKKL-ANHGQAILCTIHqpsaiLMQEF----DRLLFMQRG 1087
Cdd:cd03265 162 LDPQTRAHVWEYIEKLkEEFGMTILLTTH-----YMEEAeqlcDRVAIIDHG 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
883-1056 |
2.28e-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: 82.93 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDK-------SFPRSIGYCQQQ 952
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-----GLLRpdsGEVLIDGEDISGlseaelyRLRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 -----DLhlktaTVRESLRFsaYLRqpaevsieEKNRYVEEVIKILEMEKYadAVVGVAGEG------LNVEQRKRLTIG 1021
Cdd:cd03261 86 galfdSL-----TVFENVAF--PLR--------EHTRLSEEEIREIVLEKL--EAVGLRGAEdlypaeLSGGMKKRVALA 148
|
170 180 190
....*....|....*....|....*....|....*
gi 398365429 1022 VELTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKL 1056
Cdd:cd03261 149 RALALDPELL-LYDEPTAGLDPIASGVIDDLIRSL 182
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
46-152 |
4.06e-17 |
|
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: 77.36 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 46 LARTLTAQSMQNSTQSAPnksdaqsifssgvegVNPIFSDPEAPgydpkldpnsenFSSAAWVKNMAHLSAADPdFYKPY 125
Cdd:pfam14510 2 LARILTRQSSSSSSSSSP---------------ESTDPDEEDSE------------FDLRKWLKNLRRLIDEDG-YIKPR 53
|
90 100
....*....|....*....|....*..
gi 398365429 126 SLGCAWKNLSASGASADVAYQSTVVNI 152
Cdd:pfam14510 54 KLGVAFKNLTVSGVGAGADYQPTVGNA 80
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
887-1098 |
4.48e-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: 81.71 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNG--IPRDKSFPRS---IGYCQQQDLHLKT 958
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI-----MGLLPprsGSIRFDGrdITGLPPHERAragIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRQPAEV--SIEEknryVEEVIKILEmEKYADAvvgvAGE---GlnveQRKRLTIGVELTAKPKLLVf 1033
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRkaRLER----VYELFPRLK-ERRKQL----AGTlsgG----EQQMLAIARALMSRPKLLL- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLANHGQAILcTIHQPSAILMQEFDRLLFMQRgGKTVYFGDLGE 1098
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLER-GRVVLEGTAAE 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
872-1094 |
5.58e-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: 81.78 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT---GDILVNGIPRDKSFPRSI 946
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILglLKPTSGSIIfdgKDLLKLSRRLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 947 GYCQQQDLhlkTA-----TVRESLRFSAYLRQPAEVSiEEKNRYVEEVIKILE-----MEKYADAVVGvageGlnveQRK 1016
Cdd:cd03257 85 QMVFQDPM---SSlnprmTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLVGVGlpeevLNRYPHELSG----G----QRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1017 RLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIHQPSAIlmQEF-DRLLFMQrGGKTVYFG 1094
Cdd:cd03257 153 RVAIARALALNPKLLI-ADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVV--AKIaDRVAVMY-AGKIVEEG 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
886-1070 |
5.99e-17 |
|
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: 85.88 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIP----RDKSFPRSIGYCqQQDLHLKT 958
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-----GLLdplQGEVTLDGVPvsslDQDEVRRRVSVC-AQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAylrqpAEVSIEEKNRYVEEV---IKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLD 1035
Cdd:TIGR02868 423 TTVRENLRLAR-----PDATDEELWAALERVglaDWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL-LD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKlANHGQAILCTIHQP 1070
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
885-1056 |
7.48e-17 |
|
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: 81.56 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDK-------SFPRSIGYCQQQ-- 952
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----GLLRpdsGEILVDGQDITGlsekelyELRRRIGMLFQGga 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 ---DLhlktaTVRESLRFsaYLRQPAEVSIEEKNRYVEEVikiLEMekyadavVGVAGeglnVE----------QRKRLT 1019
Cdd:COG1127 93 lfdSL-----TVFENVAF--PLREHTDLSEAEIRELVLEK---LEL-------VGLPG----AAdkmpselsggMRKRVA 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365429 1020 IGVELTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKL 1056
Cdd:COG1127 152 LARALALDPEIL-LYDEPTAGLDPITSAVIDELIREL 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
865-1081 |
4.58e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 865 SEAIFHWRNlcyeVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNG--IPRD 939
Cdd:PRK13537 4 SVAPIDFRN----VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTL-----RMLLGLTHpdaGSISLCGepVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 940 KSFPRS-IGYCQQQDLHLKTATVRESLR-FSAYLRQPAEvsieEKNRYVEEVIKILEMEKYADAVVGVAGEGLnveqRKR 1017
Cdd:PRK13537 75 ARHARQrVGVVPQFDNLDPDFTVRENLLvFGRYFGLSAA----AARALVPPLLEFAKLENKADAKVGELSGGM----KRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1018 LTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHqpsaiLMQEFDRL 1081
Cdd:PRK13537 147 LTLARALVNDPDVLV-LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH-----FMEEAERL 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
887-1087 |
5.03e-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: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIPRDKSFP------RSIGYC-QQQDL--H 955
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINllEEPD----SGTIIIDGLKLTDDKKninelrQKVGMVfQQFNLfpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LktaTVRESLRFSaylrqPAEVSIEEKNRYVEEVIKILE---MEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLV 1032
Cdd:cd03262 91 L---TVLENITLA-----PIKVKGMSKAEAEERALELLEkvgLADKADAYPAQLSGG----QQQRVAIARALAMNPKVML 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1033 FlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQpsailMQeF-----DRLLFMQRG 1087
Cdd:cd03262 159 F-DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE-----MG-FarevaDRVIFMDDG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
872-1087 |
5.63e-16 |
|
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: 83.03 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYE-VQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP-------RDKS 941
Cdd:COG1123 264 RNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLglLRPT----SGSILFDGKDltklsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 FPRSIGY-CQQQDLHL-KTATVRESLRFSayLRQPAEVSIEEKNRYVEEVIkilemekyaDAVvgvageGLNVE------ 1013
Cdd:COG1123 340 LRRRVQMvFQDPYSSLnPRMTVGDIIAEP--LRLHGLLSRAERRERVAELL---------ERV------GLPPDladryp 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1014 ------QRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSaiLMQEF-DRLLFMQ 1085
Cdd:COG1123 403 helsggQRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLA--VVRYIaDRVAVMY 479
|
..
gi 398365429 1086 RG 1087
Cdd:COG1123 480 DG 481
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
888-1068 |
7.22e-16 |
|
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: 78.22 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIP----RDKSFP---RSIGYCQQQDLHLKTAT 960
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGQDvsdlRGRAIPylrRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLrqpAEVSIEEKNRYVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSG 1040
Cdd:cd03292 95 VYENVAFALEV---TGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILI-ADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 398365429 1041 LDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
888-1081 |
8.82e-16 |
|
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: 79.74 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNG--IPRD-KSFPRSIGYCQQQ-----DLhl 956
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLT-----TLLRptsGTARVAGydVVREpRKVRRSIGIVPQYasvdeDL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 ktaTVRESLRFSAYLRqpaEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLvFLDE 1036
Cdd:TIGR01188 82 ---TGRENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLANHGQAILCTIHQpsailMQEFDRL 1081
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTHY-----MEEADKL 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
885-1094 |
3.36e-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: 76.84 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMGVIT-GDILVNGIPRDK--SFPRSIGYCQQQdLHL--- 956
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLiDGTDINKLKGKAlrQLRRQIGMIFQQ-FNLier 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 -------------KTATVRESLRFsaylrqpaeVSIEEKNRyveeVIKILE---MEKYADAVVGVAGEGlnveQRKRLTI 1020
Cdd:cd03256 93 lsvlenvlsgrlgRRSTWRSLFGL---------FPKEEKQR----ALAALErvgLLDKAYQRADQLSGG----QQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1021 GVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSaILMQEFDRLLFMqRGGKTVYFG 1094
Cdd:cd03256 156 ARALMQQPKLIL-ADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVD-LAREYADRIVGL-KDGRIVFDG 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
895-1087 |
3.60e-15 |
|
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: 76.09 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNGI------PRDKSfpRSIGYCqQQDLHLKTATVRESL 965
Cdd:cd03245 27 IRAGEKVAIIGRVGSGKSTLL-----KLLAGLYKptsGSVLLDGTdirqldPADLR--RNIGYV-PQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 966 RFSAylrqpAEVSIEEknryVEEVIKILEMEKYA-------DAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLvFLDEPT 1038
Cdd:cd03245 99 TLGA-----PLADDER----ILRAAELAGVTDFVnkhpnglDLQIGERGRGLSGGQRQAVALARALLNDPPIL-LLDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTiHQPSaiLMQEFDRLLFMQRG 1087
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDKTLIIIT-HRPS--LLDLVDRIIVMDSG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
884-1098 |
3.74e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.84 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNGIPRDKSFPRSIGYcqqqdlhL---- 956
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILApdsGEVLWDGEPLDPEDRRRIGY-------Lpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 ---KTATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAvvgvageglNVE------QRKrltigVELTA- 1026
Cdd:COG4152 81 glyPKMKVGEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANK---------KVEelskgnQQK-----VQLIAa 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 1027 ---KPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSaiLMQEF-DRLLFMQRgGKTVYFGDLGE 1098
Cdd:COG4152 144 llhDPELLI-LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQME--LVEELcDRIVIINK-GRKVLSGSVDE 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
151-392 |
3.83e-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: 75.36 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 151 NIPYKILKSGLRKfqrsketntfQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKIsysgySGDD 230
Cdd:cd03232 8 NLNYTVPVKGGKR----------QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILI-----NGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 231 IKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLktpqnrikgvdresyanhlaevamatyglshtrntkvgndivRGVS 310
Cdd:cd03232 73 LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALL------------------------------------------RGLS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 311 GGERKRVSIA-EVSicgSK----FqcWDNATRGLDSATALEFIRALKTQADiSNTSATVAIYQCSQDAYDLFNKVCVLDD 385
Cdd:cd03232 111 VEQRKRLTIGvELA---AKpsilF--LDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKFDRLLLLKR 184
|
....*...
gi 398365429 386 GYQ-IYYG 392
Cdd:cd03232 185 GGKtVYFG 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
881-1087 |
4.34e-15 |
|
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: 75.58 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA-ErvtMGVITGDILVNGiprdksfprSIGYCQQQDLhLKTA 959
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgE---LEKLSGSVSVPG---------SIAYVSQEPW-IQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPaevsieeknRYvEEVIKI------LEMEKYADA-VVGVAGEGLNVEQRKRLTIGVELTAKPKlLV 1032
Cdd:cd03250 81 TIRENILFGKPFDEE---------RY-EKVIKAcalepdLEILPDGDLtEIGEKGINLSGGQKQRISLARAVYSDAD-IY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1033 FLDEPTSGLDSQTAWSICQ--LMKKLANHGQAILCTiHQPSAILmqEFDRLLFMQRG 1087
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVT-HQLQLLP--HADQIVVLDNG 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
887-1081 |
5.60e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVIT---GDILVNGIP---RDKSFPRSIGYCQQQDLHLKTAT 960
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTI-----ARMILGMTSpdaGKITVLGVPvpaRARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLR-FSAYLRQpaevsieeKNRYVEEVI-KILE---MEKYADAVVGVAGEGLnveqRKRLTIGVELTAKPKLLVfLD 1035
Cdd:PRK13536 131 VRENLLvFGRYFGM--------STREIEAVIpSLLEfarLESKADARVSDLSGGM----KRRLTLARALINDPQLLI-LD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLANHGQAILCTIHqpsaiLMQEFDRL 1081
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEEAERL 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
885-1087 |
7.94e-15 |
|
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: 75.29 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGV-ITGDILVNG------IPRDKSFPRSIGYCQQQDLH 955
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlNDLIPGApDEGEVLLDGkdiydlDVDVLELRRRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKtATVRESLRFSAYLRQpaEVSIEEKNRYVEEVIKILEMEKYADAvvGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLD 1035
Cdd:cd03260 93 FP-GSIYDNVAYGLRLHG--IKLKEELDERVEEALRKAALWDEVKD--RLHALGLSGGQQQRLCLARALANEPEVLL-LD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLANHGQAILCT--IHQPSAILmqefDRLLFMQRG 1087
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAARVA----DRTAFLLNG 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
888-1056 |
9.78e-15 |
|
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: 75.31 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGipRD---------KSFPRSIGYCQQQDLHL 956
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINglERPT----SGSVLVDG--TDltllsgkelRKARRRIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 KTATVRESLrfsAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLvFLDE 1036
Cdd:cd03258 95 SSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGG----QKQRVGIARALANNPKVL-LCDE 166
|
170 180
....*....|....*....|
gi 398365429 1037 PTSGLDSQTAWSICQLMKKL 1056
Cdd:cd03258 167 ATSALDPETTQSILALLRDI 186
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
885-1087 |
1.07e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.09 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLD--CLAERVTmgviTGDILVNGIP----RDKSFP---RSIGYCqQQDLH 955
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKllYGEERPT----SGQVLVNGQDlsrlKRREIPylrRRIGVV-FQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 L-KTATVRESLRFsaylrqPAEV---SIEEKNRYVEEVIKILEMEKYADAVVGV--AGEglnveqRKRLTIGVELTAKPK 1029
Cdd:COG2884 90 LlPDRTVYENVAL------PLRVtgkSRKEIRRRVREVLDLVGLSDKAKALPHElsGGE------QQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1030 LLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSaiLMQEFD-RLLFMQRG 1087
Cdd:COG2884 158 LLL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
895-1087 |
1.97e-14 |
|
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: 79.29 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNG---IPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYL 971
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGksiLTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 972 RQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLlVFLDEPTSGLDSQTAWSICQ 1051
Cdd:TIGR01257 2040 RG---VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPPL-VLLDEPTTGMDPQARRMLWN 2111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365429 1052 LMKKLANHGQAILCTIHQpsailMQEFD----RLLFMQRG 1087
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHS-----MEECEalctRLAIMVKG 2146
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
887-1087 |
2.53e-14 |
|
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: 73.44 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVI-TGDILVNGIPRDKsfpRSIGYCQQQDLHLKTATVRE 963
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPTSGRIyIGGRDVTDLPPKD---RDIAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLRFSAYLRQPAEVSIEEKnryVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEPTSGLDS 1043
Cdd:cd03301 92 NIAFGLKLRKVPKDEIDER---VREVAELLQIEHLLDRKPKQLSGG----QRQRVALGRAIVREPKVFL-MDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365429 1044 QTAWSICQLMKKL-ANHGQAILCTIH-QPSAILMQefDRLLFMQRG 1087
Cdd:cd03301 164 KLRVQMRAELKRLqQRLGTTTIYVTHdQVEAMTMA--DRIAVMNDG 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
886-1068 |
3.00e-14 |
|
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: 72.84 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDKS------FPRSIGYC-QQQDLH 955
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN-----GLLrpqSGAVLIDGEPLDYSrkglleRRQRVGLVfQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRFSaylrqPAEV--SIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVf 1033
Cdd:TIGR01166 81 LFAADVDQDVAFG-----PLNLglSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDVLL- 150
|
170 180 190
....*....|....*....|....*....|....*
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
872-1084 |
4.07e-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: 73.27 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIPRDKSfPRSIGYC 949
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAglERPT----SGEVLVDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 950 QQQDLHLKTATVRESLRFSAYLRqpaEVSIEEKNRYVEEVIKILEMEKYADA----VVGvaGeglnveQRKRLTIGVELT 1025
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLSGFENAyphqLSG--G------MRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1026 AKPKLLvFLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPS-AILMQefDRLLFM 1084
Cdd:cd03293 148 VDPDVL-LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDeAVFLA--DRVVVL 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
885-1073 |
4.40e-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: 73.42 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVtMGVITGDILVNGIP-RD---KSFPRSIGYCQQqDLHLKTAT 960
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RF-YDVSSGSILIDGQDiREvtlDSLRRAIGVVPQ-DTVLFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRfsaYLRQPA-EVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLvFLDEPTS 1039
Cdd:cd03253 91 IGYNIR---YGRPDAtDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL-LLDEATS 166
|
170 180 190
....*....|....*....|....*....|....
gi 398365429 1040 GLDSQTAWSICQLMKKLANHGQAILCTiHQPSAI 1073
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTI 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
872-1087 |
5.22e-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: 73.59 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIPRDKSFPRsIGYC 949
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAglEKPT----SGEVLVDGKPVTGPGPD-RGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 950 QQQDLHLKTATVRESLRFSayLRQpAEVSIEEKNRYVEEVIKILEMEKYADAVV-----GvageglnveQRKRLTIGVEL 1024
Cdd:COG1116 86 FQEPALLPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFEDAYPhqlsgG---------MRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1025 TAKPKLLvFLDEPTSGLDSQTAWSI-CQLMKKLANHGQAILCTIHQPS-AILMQefDRLLFMQRG 1087
Cdd:COG1116 154 ANDPEVL-LMDEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDVDeAVFLA--DRVVVLSAR 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
878-1069 |
1.01e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 878 VQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERV--TMGVITGDILVNGIPRDKSFPRSIGycqqqdlh 955
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLIDAIG-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 lktatvreslrfsaylrqpaevsieeKNRYVEEVIKILEMEKYADAVVGVA--GEgLNVEQRKRLTIGVELTAKPKLLVf 1033
Cdd:COG2401 108 --------------------------RKGDFKDAVELLNAVGLSDAVLWLRrfKE-LSTGQKFRFRLALLLAERPKLLV- 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLA-NHG-QAILCTIHQ 1069
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLArRAGiTLVVATHHY 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
887-1045 |
1.38e-13 |
|
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: 72.19 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDcLAERVtMGVITGDILVNGIP-RD---KSFPRSIGYCqQQDLHLKTATVR 962
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVS-LLERF-YDPTSGEILLDGVDiRDlnlRWLRSQIGLV-SQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAYLRQPAEVSIEEKNRYVEEVIKILeMEKYaDAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLD 1042
Cdd:cd03249 95 ENIRYGKPDATDEEVEEAAKKANIHDFIMSL-PDGY-DTLVGERGSQLSGGQKQRIAIARALLRNPKILL-LDEATSALD 171
|
...
gi 398365429 1043 SQT 1045
Cdd:cd03249 172 AES 174
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
888-1098 |
2.00e-13 |
|
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: 71.60 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNG-----IPRDKsfpRSIGY-CQQQDL--HL 956
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIkpdSGKILLNGkditnLPPEK---RDISYvPQNYALfpHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 ktaTVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILE-MEKYADAVVGvaGEglnveqRKRLTIGVELTAKPKLLvFLD 1035
Cdd:cd03299 87 ---TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHlLNRKPETLSG--GE------QQRVAIARALVVNPKIL-LLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAILMQEfDRLLFMqRGGKTVYFGDLGE 1098
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALA-DKVAIM-LNGKLIQVGKPEE 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
884-1068 |
2.33e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.42 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNG-----IPRDKSFPRSIGYCQQQDLH 955
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTF-----YMIVGLVkpdSGKILLDGqditkLPMHKRARLGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRfsAYLRQpAEVSIEEKNRYVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTIGVELTAKPKLLvFLD 1035
Cdd:cd03218 87 FRKLTVEENIL--AVLEI-RGLSKKEREEKLEELLEEFHITHLRKSK----ASSLSGGERRRVEIARALATNPKFL-LLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
881-1068 |
2.58e-13 |
|
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: 71.21 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNG-IP--RDKSFPRSIGYCQQQ-- 952
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-----GLLQptsGEVRVAGlVPwkRRKKFLRRIGVVFGQkt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 ----DLhlktaTVRESLRFsayLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELTAKP 1028
Cdd:cd03267 105 qlwwDL-----PVIDSFYL---LAAIYDLPPARFKKRLDELSELLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365429 1029 KLLvFLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIH 1068
Cdd:cd03267 173 EIL-FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSH 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
901-1044 |
2.88e-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: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 901 TALMGASGAGKTTLLDCLA--ERVTMGVIT--GDILVNG-----IPRDKsfpRSIGYCQQQDL---HLktaTVRESLRFs 968
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAglERPDSGRIRlgGEVLQDSargifLPPHR---RRIGYVFQEARlfpHL---SVRGNLLY- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 969 AYLRQPAEVSIEEknryVEEVIKILE----MEKYADAVVGvaGEglnveqRKRLTIGVELTAKPKLLVfLDEPTSGLDSQ 1044
Cdd:COG4148 101 GRKRAPRAERRIS----FDEVVELLGighlLDRRPATLSG--GE------RQRVAIGRALLSSPRLLL-MDEPLAALDLA 167
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
884-1068 |
3.31e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMgvITGDILVNGIP----RDKSFPRSIGYCQQQDLHLKTA 959
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDKPismlSSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVREslrFSAYLRQP-----AEVSIEEKNRyVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELtAKPKLLVFL 1034
Cdd:PRK11231 92 TVRE---LVAYGRSPwlslwGRLSAEDNAR-VNQAMEQTRINHLADRRL----TDLSGGQRQRAFLAMVL-AQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 398365429 1035 DEPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
872-1087 |
3.39e-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: 69.17 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYevQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDK----SFPR 944
Cdd:cd03246 4 ENVSF--RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL-----GLLrptSGRVRLDGADISQwdpnELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 945 SIGYCQQQDLhLKTATVRESlrfsaylrqpaevsieeknryveevikILEmekyadavvgvAGeglnveQRKRLTIGVEL 1024
Cdd:cd03246 77 HVGYLPQDDE-LFSGSIAEN---------------------------ILS-----------GG------QRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1025 TAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:cd03246 112 YGNPRILV-LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL--ASADRILVLEDG 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
886-1087 |
3.48e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 70.83 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGI------PRDksfpRSIGYCQQQDLHLK 957
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPD----SGTILFGGEdatdvpVQE----RNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAYLR----QPAEVSIEEKnryVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTIGVELTAKPKLLVf 1033
Cdd:cd03296 88 HMTVFDNVAFGLRVKprseRPPEAEIRAK---VHELLKLVQLDWLADRY----PAQLSGGQRQRVALARALAVEPKVLL- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLAN--HGQAILCTIHQPSAilMQEFDRLLFMQRG 1087
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEA--LEVADRVVVMNKG 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
895-1087 |
4.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLDCLaervtMGVI--TGDILVNGIP-RDKSFPRsigYCQQ-----QDLHLKTATVRESLR 966
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNAL-----LGFLpyQGSLKINGIElRELDPES---WRKHlswvgQNPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 967 FSAYLRQPAEVSIEEKNRYVEEVIKilEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTA 1046
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLP--LLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL-LDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365429 1047 WSICQLMKKlANHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:PRK11174 522 QLVMQALNA-ASRRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
886-1042 |
7.72e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.64 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGIPRDKsfpRSIGYC-QQQDL--HLkta 959
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAglEDPTSGEILiGGRDVTDLPPKD---RNIAMVfQSYALypHM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSayLRQpAEVSIEEKNRYVEEVIKILEMEKYAD----AVVGvaGeglnveQRKRLTIGVELTAKPKllVFL- 1034
Cdd:COG3839 91 TVYENIAFP--LKL-RKVPKAEIDRRVREAAELLGLEDLLDrkpkQLSG--G------QRQRVALGRALVREPK--VFLl 157
|
....*...
gi 398365429 1035 DEPTSGLD 1042
Cdd:COG3839 158 DEPLSNLD 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
872-1070 |
8.87e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVqikaETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMG-----VITGDILVNG-----IPRDKS 941
Cdd:COG0396 4 KNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLA-----KVLMGhpkyeVTSGSILLDGedileLSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 FPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEM-EKYADavvgvagEGLNVE----QRK 1016
Cdd:COG0396 75 ARAGIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLD-------RYVNEGfsggEKK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1017 RLTIgveLTA---KPKLLVfLDEPTSGLDsqtAWS---ICQLMKKLANHGQAILCTIHQP 1070
Cdd:COG0396 148 RNEI---LQMlllEPKLAI-LDETDSGLD---IDAlriVAEGVNKLRSPDRGILIITHYQ 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
888-1068 |
9.16e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLdcLAERVTMGVITGDILVNG--IPRDKS----FPRSIGYC-QQQDLHLKTAT 960
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLF--LHFNGILKPTSGEVLIKGepIKYDKKslleVRKTVGIVfQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSaylrqPAEV--SIEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPT 1038
Cdd:PRK13639 96 VEEDVAFG-----PLNLglSKEEVEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIAGILAMKPEIIV-LDEPT 165
|
170 180 190
....*....|....*....|....*....|
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
885-1068 |
1.23e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATV 961
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 RESLRFSAYLRQpaEVSIEEKNRYVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTIGVELTAKPKlLVFLDEPTSGL 1041
Cdd:PRK10895 96 YDNLMAVLQIRD--DLSAEQREDRANELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPK-FILLDEPFAGV 168
|
170 180
....*....|....*....|....*..
gi 398365429 1042 DSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
868-1098 |
1.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 868 IFHWRNLCYEVqikAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDKS--- 941
Cdd:PRK13636 5 ILKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN-----GILkpsSGRILFDGKPIDYSrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 ---FPRSIGYC-QQQDLHLKTATVRESLRFSAYLRQPAEvsiEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKR 1017
Cdd:PRK13636 77 lmkLRESVGMVfQDPDNQLFSASVYQDVSFGAVNLKLPE---DEVRKRVDNALKRTGIEHLKDK----PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1018 LTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANH-GQAILCTIHQPSAILMQeFDRLLFMQRgGKTVYFGDL 1096
Cdd:PRK13636 150 VAIAGVLVMEPKVLV-LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLY-CDNVFVMKE-GRVILQGNP 226
|
..
gi 398365429 1097 GE 1098
Cdd:PRK13636 227 KE 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
886-1042 |
2.73e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.13 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGIPRDKsfpRSIGYCQQQDL---HLkta 959
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPDSGRILlDGRDVTGLPPEK---RNVGMVFQDYAlfpHL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSayLRQpAEVSIEEKNRYVEEVIKILEMEKYADAVV----GvageglnvEQRKRltigVELtA-----KPKL 1030
Cdd:COG3842 93 TVAENVAFG--LRM-RGVPKAEIRARVAELLELVGLEGLADRYPhqlsG--------GQQQR----VAL-AralapEPRV 156
|
170
....*....|..
gi 398365429 1031 LvFLDEPTSGLD 1042
Cdd:COG3842 157 L-LLDEPLSALD 167
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
885-1087 |
2.94e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDC--LAERVTMGVIT-GDILVNGiprdksfPRSIGycQQQDLhlktatV 961
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDT-------ARSLS--QQKGL------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 REslrfsayLRQPAEVSIEEKNRY-----VEEVIK---ILEMEKYADAV---------VGVAGEG------LNVEQRKRL 1018
Cdd:PRK11264 81 RQ-------LRQHVGFVFQNFNLFphrtvLENIIEgpvIVKGEPKEEATararellakVGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1019 TIGVELTAKPKLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSaILMQEFDRLLFMQRG 1087
Cdd:PRK11264 154 AIARALAMRPEVILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS-FARDVADRAIFMDQG 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
872-1111 |
3.28e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVqikaETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGiprdksfprsigycqq 951
Cdd:cd03217 4 KDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 952 QDlhLKTATVRESLRFSAYL--RQPAE---VSIEEKNRYVeevikilemekyadavvgvaGEGLNVEQRKRLTIGVELTA 1026
Cdd:cd03217 64 ED--ITDLPPEERARLGIFLafQYPPEipgVKNADFLRYV--------------------NEGFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1027 KPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRgGKTVYFGDlgegcKTMIDY 1106
Cdd:cd03217 122 EPDLAI-LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYD-GRIVKSGD-----KELALE 194
|
....*
gi 398365429 1107 FESHG 1111
Cdd:cd03217 195 IEKKG 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
887-1091 |
4.28e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAErvtMGVIT-GDILVNGIP-RD-KSFPRSI----GYCQQQDLHLKTA 959
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINK---LEEITsGDLIVDGLKvNDpKVDERLIrqeaGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAylRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVFlDEPTS 1039
Cdd:PRK09493 93 TALENVMFGP--LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGG----QQQRVAIARALAVKPKLMLF-DEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1040 GLDSQTAWSICQLMKKLANHGQAILCTIHQpSAILMQEFDRLLFMQRGGKTV 1091
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHE-IGFAEKVASRLIFIDKGRIAE 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
175-356 |
5.62e-12 |
|
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: 66.73 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 175 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTV 254
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILA----GLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 255 FETLVTVARLKTPQnrikgVDRESYANHLAEVamatyGLSHTRNTKVGNdivrgVSGGERKRVSIAEVSICGSKfqCW-- 332
Cdd:COG4133 93 RENLRFWAALYGLR-----ADREAIDEALEAV-----GLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAP--LWll 155
|
170 180
....*....|....*....|....
gi 398365429 333 DNATRGLDSATALEFIRALKTQAD 356
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLA 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
183-343 |
6.09e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 66.76 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSIS---SNTHGFdlgadtkISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLV 259
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTgelRPTSGT-------AYINGYSIRTDRKAARQSLGYCPQFDALFDELTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 260 TVARLKtpqnrikGVdRESYANHLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIAeVSICG-SKFQCWDNATRG 338
Cdd:cd03263 98 FYARLK-------GL-PKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLA-IALIGgPSVLLLDEPTSG 163
|
....*
gi 398365429 339 LDSAT 343
Cdd:cd03263 164 LDPAS 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
872-1068 |
8.83e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.19 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLC--YEVQIKAE------------TRRILNNVDGW---VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDI 931
Cdd:COG4586 5 ENLSktYRVYEKEPglkgalkglfrrEYREVEAVDDIsftIEPGEIVGFIGPNGAGKSTTIKMLT-----GILVptsGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 932 LVNG-IP--RDKSFPRSIG--YCQ-QQ---DLhlktaTVRESLRfsaYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAV 1002
Cdd:COG4586 80 RVLGyVPfkRRKEFARRIGvvFGQrSQlwwDL-----PAIDSFR---LLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1003 V-----GvageglnveQRKRltigVELTA----KPKLLvFLDEPTSGLD--SQTAwsICQLMKKL-ANHGQAILCTIH 1068
Cdd:COG4586 152 VrqlslG---------QRMR----CELAAallhRPKIL-FLDEPTIGLDvvSKEA--IREFLKEYnRERGTTILLTSH 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
887-1094 |
1.03e-11 |
|
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: 65.98 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVTMgVITGDILVNGIP---------RdksfpRSIGYCqQQDLHLK 957
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVE-LSSGSILIDGVDiskiglhdlR-----SRISII-PQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLR-FSAYlrqpaevSIEEKNRYVEEV-IK--ILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVf 1033
Cdd:cd03244 91 SGTIRSNLDpFGEY-------SDEELWQALERVgLKefVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1034 LDEPTSGLDSQTAWSICQ-LMKKLANHgqAILCTIHQPSAILmqEFDRLLFMQRgGKTVYFG 1094
Cdd:cd03244 163 LDEATASVDPETDALIQKtIREAFKDC--TVLTIAHRLDTII--DSDRILVLDK-GRVVEFD 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
872-1094 |
1.14e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 66.68 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQikaeTRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDkSFPRsigy 948
Cdd:COG4559 5 ENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-----GELTpssGEVRLNGRPLA-AWSP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 949 cqqQDLhlktATVRESLRFSAYL-------------RQPAEVSIEEKNRYVEEVIKILEMEKYAD----AVVGvaGEgln 1011
Cdd:COG4559 71 ---WEL----ARRRAVLPQHSSLafpftveevvalgRAPHGSSAAQDRQIVREALALVGLAHLAGrsyqTLSG--GE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1012 vEQRkrltigVEL-----------TAKPKLLvFLDEPTSGLD----SQTAwsicQLMKKLANHGQAILCTIHQPSaiLMQ 1076
Cdd:COG4559 139 -QQR------VQLarvlaqlwepvDGGPRWL-FLDEPTSALDlahqHAVL----RLARQLARRGGGVVAVLHDLN--LAA 204
|
250
....*....|....*....
gi 398365429 1077 EF-DRLLFMQRgGKTVYFG 1094
Cdd:COG4559 205 QYaDRILLLHQ-GRLVAQG 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
886-1068 |
1.38e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNGIPRDKSFPRSIGYcqqqdlhlKTATVR 962
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLTptaGTVLVAGDDVEALSARAASR--------RVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 E--SLRFSAYLRQPAEV-----------SIEEKNRYVEEVIKILEMEKYAD-AVVGVAGeglnvEQRKRLTIGVELT-AK 1027
Cdd:PRK09536 84 QdtSLSFEFDVRQVVEMgrtphrsrfdtWTETDRAAVERAMERTGVAQFADrPVTSLSG-----GERQRVLLARALAqAT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365429 1028 PKLLvfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK09536 159 PVLL--LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
885-1070 |
2.34e-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: 64.69 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDKSFP---RSIGYCQQQDlHLKT 958
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA-----GLLrpdSGEVRWNGTPLAEQRDephENILYLGHLP-GLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 A-TVRESLRFSAYLRQPAEVSIEEKnryVEEVikilEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEP 1037
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDA---LAAV----GLTGFEDLPAAQLSAG----QQRRLALARLWLSRRPLWI-LDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365429 1038 TSGLDSQtawSICQLMKKLANH---GQAILCTIHQP 1070
Cdd:TIGR01189 155 TTALDKA---GVALLAGLLRAHlarGGIVLLTTHQD 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
886-1069 |
2.43e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 65.34 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGIPRDKsfpRSIGYC-QQQDL--HLkta 959
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfETPTSGEILlDGKDITNLPPHK---RPVNTVfQNYALfpHL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPAEVSIEEKnryVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTS 1039
Cdd:cd03300 88 TVFENIAFGLRLKKLPKAEIKER---VAEALDLVQLEGYANRKP----SQLSGGQQQRVAIARALVNEPKVLL-LDEPLG 159
|
170 180 190
....*....|....*....|....*....|
gi 398365429 1040 GLDsqtawsicqlmKKLANHGQAILCTIHQ 1069
Cdd:cd03300 160 ALD-----------LKLRKDMQLELKRLQK 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
886-1064 |
2.68e-11 |
|
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: 65.39 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGDILVNG--IPRDKSFPRS---IGYCQQ-----Q 952
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI-----SGLLpprSGSIRFDGedITGLPPHRIArlgIGYVPEgrrifP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 DLhlktaTVRESLRFSAYLRQPAEvSIEEKnryVEEVikiLEM-----EKYADAvvgvAGE---GlnveQRKRLTIGVEL 1024
Cdd:COG0410 92 SL-----TVEENLLLGAYARRDRA-EVRAD---LERV---YELfprlkERRRQR----AGTlsgG----EQQMLAIGRAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398365429 1025 TAKPKLLVfLDEPTSGLdsqtAWSICQLM----KKLANHGQAIL 1064
Cdd:COG0410 152 MSRPKLLL-LDEPSLGL----APLIVEEIfeiiRRLNREGVTIL 190
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
887-1087 |
2.89e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAERVtmgviTGDILVNGIP----RDKSFPRSIGYCQQQDLhLKTA 959
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPT-----GGQVLLDGVPlvqyDHHYLHRQVALVGQEPV-LFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPAEVSIEEKNRYVEEVikILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTS 1039
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDF--IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365429 1040 GLDSQTAWSICQLMKKlanHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:TIGR00958 647 ALDAECEQLLQESRSR---ASRTVLLIAHRLSTV--ERADQILVLKKG 689
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
885-1070 |
3.18e-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: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAErvTMGVITGDILVNGIPRDK---SFPRSIGYCQQQDlHLKTA-T 960
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG--LSPPLAGRVLLNGGPLDFqrdSIARGLLYLGHAP-GIKTTlS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLRQPAEVsieeknryvEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEPTSG 1040
Cdd:cd03231 90 VLENLRFWHADHSDEQV---------EEALARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LDEPTTA 155
|
170 180 190
....*....|....*....|....*....|...
gi 398365429 1041 LDSQtawSICQLMKKLANH---GQAILCTIHQP 1070
Cdd:cd03231 156 LDKA---GVARFAEAMAGHcarGGMVVLTTHQD 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
888-1064 |
3.80e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKSFPR-------SIGYcqqQDLHL- 956
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVYQpdsGEILLDGEPVRFRSPRdaqaagiAIIH---QELNLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 KTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLLVfLDE 1036
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSRDARVLI-LDE 166
|
170 180
....*....|....*....|....*...
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLANHGQAIL 1064
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
887-1056 |
7.52e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMG-VITGDILVNGIPRDKsfpRSIGYC-QQQDL--HLktaT 960
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGdLFIGEKRMNDVPPAE---RGVGMVfQSYALypHL---S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYLrqpAEVSIEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKPKllVFL-DEPTS 1039
Cdd:PRK11000 92 VAENMSFGLKL---AGAKKEEINQRVNQVAEVLQLAHLLDR----KPKALSGGQRQRVAIGRTLVAEPS--VFLlDEPLS 162
|
170 180
....*....|....*....|.
gi 398365429 1040 GLDS----QTAWSICQLMKKL 1056
Cdd:PRK11000 163 NLDAalrvQMRIEISRLHKRL 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
863-1068 |
7.82e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 863 SKSEAIFHWRNLCYEVqikaETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGIP----R 938
Cdd:PRK10575 6 NHSDTTFALRNVSFRV----PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPleswS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 939 DKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPA--EVSIEEKNRyVEEVIKILEMEKYADAVVgvagEGLNVEQRK 1016
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGAlgRFGAADREK-VEEAISLVGLKPLAHRLV----DSLSGGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1017 RLTIGVeLTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIH 1068
Cdd:PRK10575 155 RAWIAM-LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLH 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
886-1068 |
9.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAE--RVTMGVI-TGDILVNGIPRDKSFP---RSIGYC-QQQDLHLKT 958
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVtVGDIVVSSTSKQKEIKpvrKKVGVVfQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAylrQPAEVSIEEKNRYVEEVIKILEMEK--YADAVVGVAGeglnvEQRKRLTIGVELTAKPKLLVfLDE 1036
Cdd:PRK13643 100 ETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADefWEKSPFELSG-----GQMRRVAIAGILAMEPEVLV-LDE 170
|
170 180 190
....*....|....*....|....*....|..
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
159-361 |
1.16e-10 |
|
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: 62.89 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 159 SGLRKfQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthgfdlGADTkiSYSGYS---GDDIKK-- 233
Cdd:cd03255 4 KNLSK-TYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG--------GLDR--PTSGEVrvdGTDISKls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 234 -----HFRGEVV------YNAeadvhLPHLTVFETLVTVARLKtpqnRIKGVDRESYANHLAEVAmatyGLSHTRNTKVG 302
Cdd:cd03255 73 ekelaAFRRRHIgfvfqsFNL-----LPDLTALENVELPLLLA----GVPKKERRERAEELLERV----GLGDRLNHYPS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 303 NdivrgVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTS 361
Cdd:cd03255 140 E-----LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTT 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
886-1091 |
1.62e-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: 61.29 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDksfprsigycqqqdlhlkTATVR 962
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYKpdsGEILVDGKEVS------------------FASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRfsaylrqpaevsieeknryveevikilemekyadavvgvAGEG----LNVEQRKRLTIGVELTAKPKLLVfLDEPT 1038
Cdd:cd03216 71 DARR---------------------------------------AGIAmvyqLSVGERQMVEIARALARNARLLI-LDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlmQEF-DRLLFMqRGGKTV 1091
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEV--FEIaDRVTVL-RDGRVV 161
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
887-1087 |
3.32e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIP----RDKSFPRSIGYCQQQdLHLKTATVR 962
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQGEILLNGQPiadySEAALRQAISVVSQR-VHLFSATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAylrqpAEVSIEEKNRYVEEV--IKILEMEKYADAVVGVAGEGLNVEQRKRLTIG-VELTAKPKLLvfLDEPTS 1039
Cdd:PRK11160 432 DNLLLAA-----PNASDEALIEVLQQVglEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIArALLHDAPLLL--LDEPTE 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365429 1040 GLDSQTAWSICQLMKKLANHGQAILCTiHQpsAILMQEFDRLLFMQRG 1087
Cdd:PRK11160 505 GLDAETERQILELLAEHAQNKTVLMIT-HR--LTGLEQFDRICVMDNG 549
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
885-1087 |
3.83e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.41 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNG--IPRDKSFPRS--IG--YcqqQDLH 955
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-----GSLppdSGSILIDGkdVTKLPEYKRAkyIGrvF---QDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTA---TVRESLRFsAYLR------QPAeVSIEEKNRYVEEvIKILEM--EKYADAVVGVAGEGlnveQRKRLTIGVEL 1024
Cdd:COG1101 91 MGTApsmTIEENLAL-AYRRgkrrglRRG-LTKKRRELFREL-LATLGLglENRLDTKVGLLSGG----QRQALSLLMAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1025 TAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQaiLCTI---HQpsailMQ---EF-DRLLFMQRG 1087
Cdd:COG1101 164 LTKPKLLL-LDEHTAALDPKTAALVLELTEKIVEENN--LTTLmvtHN-----MEqalDYgNRLIMMHEG 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
885-1087 |
6.43e-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: 60.95 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERVTMgVITGDILVNGIPrdksfprsIGYCQQQDLHLKTATV-RE 963
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-ENFYQ-PQGGQVLLDGKP--------ISQYEHKYLHSKVSLVgQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLRFSAYLRQP-----AEVSIEeknRYVEEVIK------ILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLV 1032
Cdd:cd03248 97 PVLFARSLQDNiayglQSCSFE---CVKEAAQKahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1033 fLDEPTSGLDSQTAWSICQLMKKlANHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:cd03248 174 -LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV--ERADQILVLDGG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
881-1056 |
9.29e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP---------RDKSfpRSIGYC 949
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINllERPT----SGSVLVDGVDltalserelRAAR--RKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 950 QQQDLHLKTATVRESLRFSayLRQpAEVSIEEKNRYVEEVIKILEMEKYADAV-----------VGVAgeglnveqRKrl 1018
Cdd:COG1135 88 FQHFNLLSSRTVAENVALP--LEI-AGVPKAEIRKRVAELLELVGLSDKADAYpsqlsggqkqrVGIA--------RA-- 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365429 1019 tigveLTAKPKLLvFLDEPTSGLDSQTAWSICQLMKKL 1056
Cdd:COG1135 155 -----LANNPKVL-LCDEATSALDPETTRSILDLLKDI 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
872-1098 |
1.24e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYevqIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNGIPRDKS----FPR 944
Cdd:PRK13652 7 RDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLF-----RHFNGILKptsGSVLIRGEPITKEnireVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 945 SIGYC-QQQDLHLKTATVRESLRFSaylrqPAEVSIEE---KNRyVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTI 1020
Cdd:PRK13652 79 FVGLVfQNPDDQIFSPTVEQDIAFG-----PINLGLDEetvAHR-VSSALHMLGLEELRDRV----PHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1021 GVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSaiLMQEFDRLLFMQRGGKTVYFGDLGE 1098
Cdd:PRK13652 149 AGVIAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLD--LVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
175-356 |
1.48e-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: 59.47 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 175 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIS---SNTHGfdlgadtKISYSGYSGDDIKKHFrGEVVYNAEADVHLPh 251
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllKPTSG-------SIRVFGKPLEKERKRI-GYVPQRRSIDRDFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 252 LTVFEtLVTVARL--KTPQNRIKGVDREsyanhLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIAEVSICGSKF 329
Cdd:cd03235 85 ISVRD-VVLMGLYghKGLFRRLSKADKA-----KVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDL 153
|
170 180
....*....|....*....|....*..
gi 398365429 330 QCWDNATRGLDSATALEFIRALKTQAD 356
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRR 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
884-1087 |
1.82e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.29 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERV---TMGVITGD-ILVNGIPRdKSFPRSIGYCQQQDLhLKTA 959
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVfdpQSGRILIDgTDIRTVTR-ASLRRNIAVVFQDAG-LFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRF------SAYLRQPAEVS-----IEEK-NRYveevikilemekyaDAVVGVAGEGLNVEQRKRLTIGVELTAK 1027
Cdd:PRK13657 424 SIEDNIRVgrpdatDEEMRAAAERAqahdfIERKpDGY--------------DTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1028 PKLLVfLDEPTSGLDSQTAWSICQLMKKLAnHGQAILCTIHQPSAIlmQEFDRLLFMQRG 1087
Cdd:PRK13657 490 PPILI-LDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTV--RNADRILVFDNG 545
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
886-1069 |
2.07e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVITGD--------ILVNGIPRDKSFPRSI-------GYCQ 950
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-----GLITGDksagshieLLGRTVQREGRLARDIrksrantGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 951 QQDLHLKTATVRESLRFSAYLRQP------AEVSIEEKNRYVEEVIKIlEMEKYADAVVGVAGEGlnveQRKRLTIGVEL 1024
Cdd:PRK09984 93 QQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRV-GMVHFAHQRVSTLSGG----QQQRVAIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365429 1025 TAKPKlLVFLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQ 1069
Cdd:PRK09984 168 MQQAK-VILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQ 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
887-1087 |
2.24e-09 |
|
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: 58.48 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLdclaervtmGVITGD-------ILVNGIP---RDKSFPRSIGYCQQQdLHL 956
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLL---------QLLTGDlkpqqgeITLDGVPvsdLEKALSSLISVLNQR-PYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 KTATVRESL--RFSaylrqpaevsieeknryveevikilemekyadavvgvAGEglnveqRKRLTIG-VELTAKPklLVF 1033
Cdd:cd03247 87 FDTTLRNNLgrRFS-------------------------------------GGE------RQRLALArILLQDAP--IVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1034 LDEPTSGLDSQTAWSICQLMKKLANhGQAILCTIHQPSAilMQEFDRLLFMQRG 1087
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
183-386 |
2.66e-09 |
|
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: 58.63 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISsnthGFdLGADT-KISYSGYS-GDDIKKHFRGEVVY---NaeADVHLPHLTVFET 257
Cdd:cd03225 24 IKKGEFVLIVGPNGSGKSTLLRLLN----GL-LGPTSgEVLVDGKDlTKLSLKELRRKVGLvfqN--PDDQFFGPTVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 258 LVTvarlkTPQNRikGVDRESyANHLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIAEVSICGSKFQCWDNATR 337
Cdd:cd03225 97 VAF-----GLENL--GLPEEE-IEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365429 338 GLDSATALEFIRALKtqaDISNTSATVAIyqCSQD---AYDLFNKVCVLDDG 386
Cdd:cd03225 164 GLDPAGRRELLELLK---KLKAEGKTIII--VTHDldlLLELADRVIVLEDG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
897-1105 |
4.56e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 897 PGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDKSfPRSIGYCQQQ--------DLHLKTATVRESL 965
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS-----GLLrpqKGAVLWQGKPLDYS-KRGLLALRQQvatvfqdpEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 966 RFSayLRQPAeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQT 1045
Cdd:PRK13638 100 AFS--LRNLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG----QKKRVAIAGALVLQARYLL-LDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1046 AWSICQLMKKLANHGQAILCTIHQPSaiLMQEFDRLLFMQRGGKTVYFGDLGE--GCKTMID 1105
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDID--LIYEISDAVYVLRQGQILTHGAPGEvfACTEAME 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
885-1070 |
5.63e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRDKSFPR-SIGYCQQQDLhLKTA- 959
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLL-----RLIAGLLppaAGTIKLDGGDIDDPDVAeACHYLGHRNA-MKPAl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQPAEVSIEEknryveevikilemekyADAVVGVAGEG------LNVEQRKRLTIGveltakpKLLVF 1033
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAA-----------------ALEAVGLAPLAhlpfgyLSAGQKRRVALA-------RLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365429 1034 ------LDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQP 1070
Cdd:PRK13539 145 nrpiwiLDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
898-1068 |
8.73e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 898 GTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGI---PRDKSFPRS-IGYC-QQQDLHLKTATVRESLRFSA 969
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLLHLN-----GIYLpqrGRVKVMGRevnAENEKWVRSkVGLVfQDPDDQVFSSTVWDDVAFGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 970 ylrQPAEVSIEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSI 1049
Cdd:PRK13647 106 ---VNMGLDKDEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV-LDEPMAYLDPRGQETL 177
|
170
....*....|....*....
gi 398365429 1050 CQLMKKLANHGQAILCTIH 1068
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATH 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
873-1087 |
9.36e-09 |
|
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: 57.04 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 873 NLCyeVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIPRDK----SFPRSIGy 948
Cdd:cd03369 11 NLS--VRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE--AEEGKIEIDGIDISTipleDLRSSLT- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 949 CQQQDLHLKTATVRESLrfsaylrqpaevsiEEKNRYVEEVIkilemekYADAVVGVAGEGLNVEQRKRLTIGVELTAKP 1028
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL--------------DPFDEYSDEEI-------YGALRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1029 KLLVfLDEPTSGLDSQTAWSICQLMKKLANhGQAILCTIHQPSAILmqEFDRLLFMQRG 1087
Cdd:cd03369 145 RVLV-LDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTII--DYDKILVMDAG 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
887-1087 |
1.12e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMGVITgdilVNG----IPRDKSfprsiGYCQQQDLH-LKTA 959
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPSEGSIV----VNGqtinLVRDKD-----GQLKVADKNqLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAY------------LRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAK 1027
Cdd:PRK10619 91 RTRLTMVFQHFnlwshmtvlenvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1028 PKLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQpsailmQEFDR-----LLFMQRG 1087
Cdd:PRK10619 171 PEVLLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE------MGFARhvsshVIFLHQG 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
887-1087 |
1.31e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGV---ITGDILVNGIP--------RDKSFPRSIGYCQQQDLH 955
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILA-----GLddgSSGEVSLVGQPlhqmdeeaRAKLRAKHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRFSAYLRqpAEVSIEEKNRYVeEVIKILEMEKYADAVVGVAGEGlnvEQrKRLTIGVELTAKPKLLvFLD 1035
Cdd:PRK10584 100 IPTLNALENVELPALLR--GESSRQSRNGAK-ALLEQLGLGKRLDHLPAQLSGG---EQ-QRVALARAFNGRPDVL-FAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLaNHGQA---ILCTiHQPSaiLMQEFDRLLFMQRG 1087
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSL-NREHGttlILVT-HDLQ--LAARCDRRLRLVNG 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
900-1087 |
1.82e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 900 LTALMGASGAGKTTLLDCLAErvTMGVITGDILVNGIPRDKSFP---RSIGYCQQQDLHLKTATVRESLRFSAYL--RQP 974
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTG--LLPPTSGTVLVGGKDIETNLDavrQSLGMCPQHNILFHHLTVAEHILFYAQLkgRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 975 AEVSIEEKNRYVEEVIKILEMEKYADAVVGVageglnveQRKrLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMK 1054
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM--------QRK-LSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|...
gi 398365429 1055 KLANHGQAILCTIHQPSAILMQefDRLLFMQRG 1087
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
885-1045 |
1.91e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 59.06 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLL-------DclaervtmgVITGDILVNGIP-RD---KSFPRSIGYCQQqD 953
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyD---------VTSGRILIDGQDiRDvtqASLRAAIGIVPQ-D 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 954 LHLKTATVRESLrfsAYLRqpAEVSIEEknryVEEVIK-------ILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTA 1026
Cdd:COG5265 441 TVLFNDTIAYNI---AYGR--PDASEEE----VEAAARaaqihdfIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLK 511
|
170
....*....|....*....
gi 398365429 1027 KPKLLVFlDEPTSGLDSQT 1045
Cdd:COG5265 512 NPPILIF-DEATSALDSRT 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
886-1094 |
2.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTM---GVITGDILVNGIPRDK----SFPRSIGYCQQQDLHLKT 958
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypeARVSGEVYLDGQDIFKmdviELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEgLNVEQRKRLTIGVELTAKPKLLVfLDEPT 1038
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLL-ADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFmqrGGKTVYFG 1094
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLY---KGQIVEWG 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
872-1068 |
2.50e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 872 RNLCYEVQikaeTRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIPRDkSFPRsigycqq 951
Cdd:PRK13548 6 RNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS--PDSGEVRLNGRPLA-DWSP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 952 QDLHLKTA------------TVRESLRFSAYlrqPAEVSIEEKNRYVEEVIKILEMEKYAD----AVVGvaGEglnvEQR 1015
Cdd:PRK13548 72 AELARRRAvlpqhsslsfpfTVEEVVAMGRA---PHGLSRAEDDALVAAALAQVDLAHLAGrdypQLSG--GE----QQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1016 krltigVEL----------TAKPKLLvFLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIH 1068
Cdd:PRK13548 143 ------VQLarvlaqlwepDGPPRWL-LLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
885-1070 |
3.18e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRDK---SFprsigycqQQDL---- 954
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLL-----RILAGLArpdAGEVLWQGEPIRRqrdEY--------HQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 955 HL---KTA-TVRESLRFSAYLRQPAEvsieeknryVEEVIKILE---MEKYADAVVGV--AGeglnveQRKRLTIGVELT 1025
Cdd:PRK13538 81 HQpgiKTElTALENLRFYQRLHGPGD---------DEALWEALAqvgLAGFEDVPVRQlsAG------QQRRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365429 1026 AKPKLLVfLDEPTSGLDSQ-TAWSICQLMKKLANHGQAILcTIHQP 1070
Cdd:PRK13538 146 TRAPLWI-LDEPFTAIDKQgVARLEALLAQHAEQGGMVIL-TTHQD 189
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
875-937 |
3.24e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 3.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 875 CYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV------ITGDILVNGIP 937
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEP 72
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
885-1068 |
3.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAERVTMGVITGDILVNGIPRDK---SFPRSIGYC-QQQDLHLK 957
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTimqLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVfQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFSAylrQPAEVSIEEKNRYVEEVIkilemekyadAVVGVAGE-------GLNVEQRKRLTIGVELTAKPKL 1030
Cdd:PRK13649 100 EETVLKDVAFGP---QNFGVSQEEAEALAREKL----------ALVGISESlfeknpfELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365429 1031 LVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK13649 167 LV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
167-386 |
3.44e-08 |
|
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: 54.17 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 167 SKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSnthgfdlgadtkisysgysgddIKKHFRGEVVYNAEAD 246
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG----------------------LLKPTSGEILIDGKDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 247 VHLPHLTVFETLVTVARLktpqnrikgvdresyanhlaevamatyglshtrntkvgndivrgvSGGERKRVSIAEVSICG 326
Cdd:cd00267 64 AKLPLEELRRRIGYVPQL---------------------------------------------SGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 327 SKFQCWDNATRGLDSATALEFIRALKTQADisnTSATVAIyqCSQD---AYDLFNKVCVLDDG 386
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAE---EGRTVII--VTHDpelAELAADRVIVLKDG 156
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
888-1095 |
3.71e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITGDIL-VNGIPrdkSFPRSIGYCQQQDLHLKTATVRES 964
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPTAGQIMLDGVdLSHVP---PYQRPINMMFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 965 LRFSayLRQPAEVSIEEKNRyVEEVIKILEMEKYAdavvGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDsq 1044
Cdd:PRK11607 112 IAFG--LKQDKLPKAEIASR-VNEMLGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLL-LDEPMGALD-- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1045 tawsicqlmKKLANHGQ-------------AILCTIHQPSAILMQefDRLLFMQRgGKTVYFGD 1095
Cdd:PRK11607 182 ---------KKLRDRMQlevvdilervgvtCVMVTHDQEEAMTMA--GRIAIMNR-GKFVQIGE 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
183-351 |
4.03e-08 |
|
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: 57.76 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISS--NTHGFDLGADTkISYSGYSGDDIkkhfRGEVVYNAEaDVHLPHLTVFETLVt 260
Cdd:TIGR02868 358 LPPGERVAILGPSGSGKSTLLATLAGllDPLQGEVTLDG-VPVSSLDQDEV----RRRVSVCAQ-DAHLFDTTVRENLR- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 261 VARlktpqnriKGVDRESYANHLAEVAMATY--GLSHTRNTKVGNDIVRgVSGGERKRVSIAEVSICGSKFQCWDNATRG 338
Cdd:TIGR02868 431 LAR--------PDATDEELWAALERVGLADWlrALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEH 501
|
170
....*....|...
gi 398365429 339 LDSATALEFIRAL 351
Cdd:TIGR02868 502 LDAETADELLEDL 514
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
182-343 |
5.31e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 182 CLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGysGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTV 261
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIA----GLLPPAAGTIKLDG--GDIDDPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 262 ArlktpqnRIKGVDRESyanhlAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIAEVSICGSKFQCWDNATRGLDS 341
Cdd:PRK13539 98 A-------AFLGGEELD-----IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
..
gi 398365429 342 AT 343
Cdd:PRK13539 161 AA 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
186-386 |
6.19e-08 |
|
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: 54.72 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 186 GELLVVLGRPGSGCTTLLKSISSN---THGFDLGADTKIsySGYSGDDIKKHFRG-EVVYnaEADVHLPHLTVFETlVTV 261
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKEelpTSGTIRVNGQDV--SDLRGRAIPYLRRKiGVVF--QDFRLLPDRNVYEN-VAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 262 ARlktpqnRIKGVDRESYANHLAEvAMATYGLSHTRNTkvgndIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDS 341
Cdd:cd03292 102 AL------EVTGVPPREIRKRVPA-ALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365429 342 ATALEFIRALKtqaDISNTSATVAIyqcSQDAYDLFN----KVCVLDDG 386
Cdd:cd03292 170 DTTWEIMNLLK---KINKAGTTVVV---ATHAKELVDttrhRVIALERG 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
878-1043 |
6.57e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 878 VQIKAETRR-----ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIPRDKsfpRSIgycQ 950
Cdd:PRK11432 7 VVLKNITKRfgsntVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAglEKPT----EGQIFIDGEDVTH---RSI---Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 951 QQDLhlktatvreSLRFSAYLRQP--------------AEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRK 1016
Cdd:PRK11432 77 QRDI---------CMVFQSYALFPhmslgenvgyglkmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG----QQQ 143
|
170 180
....*....|....*....|....*..
gi 398365429 1017 RLTIGVELTAKPKLLVFlDEPTSGLDS 1043
Cdd:PRK11432 144 RVALARALILKPKVLLF-DEPLSNLDA 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
888-1056 |
6.87e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.35 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDC--LAERVTmgviTGDILVNGipRD---------KSFPRSIGYCQQqdlH- 955
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT----SGRVLVDG--QDltalsekelRKARRQIGMIFQ---Hf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 --LKTATVRESLRFSAYLrqpAEVSIEEKNRYVEEVIKILEMEKYADA----VVGvaGeglnveQRKRLTIGVELTAKPK 1029
Cdd:PRK11153 92 nlLSSRTVFDNVALPLEL---AGTPKAEIKARVTELLELVGLSDKADRypaqLSG--G------QKQRVAIARALASNPK 160
|
170 180
....*....|....*....|....*..
gi 398365429 1030 LLVfLDEPTSGLDSQTAWSICQLMKKL 1056
Cdd:PRK11153 161 VLL-CDEATSALDPATTRSILELLKDI 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
797-1095 |
7.63e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 56.73 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 797 EGAKQKGEILV----FPRsIVKRMKKRGVLTEKNANDPEnvGERSDLSSdrKMLQESSEEESDTYGEIGlsksEAIFHWR 872
Cdd:TIGR03269 213 EAVKASGISMVltshWPE-VIEDLSDKAIWLENGEIKEE--GTPDEVVA--VFMEGVSEVEKECEVEVG----EPIIKVR 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 873 NLC-YEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVI----------TGDILVN----GIP 937
Cdd:TIGR03269 284 NVSkRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTL-----SKIIAGVLeptsgevnvrVGDEWVDmtkpGPD 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 938 RDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSieeknryVEEVIKILEM----EKYADAVVGVAGEGLNVE 1013
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELA-------RMKAVITLKMvgfdEEKAEEILDKYPDELSEG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1014 QRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQ-LMKKLANHGQAILCTIHQPSAILMQeFDRLLFMqRGGKTVY 1092
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVI-LDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDV-CDRAALM-RDGKIVK 508
|
...
gi 398365429 1093 FGD 1095
Cdd:TIGR03269 509 IGD 511
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
171-406 |
8.20e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 171 NTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNThgfdlgadtkiSYSGYSGDdIKkhFRGEVVYNAEAD---- 246
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHP-----------AYKILEGD-IL--FKGESILDLEPEerah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 247 ----------VHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAE----VAMATYGLShtRNTkvgNDivrGVSGG 312
Cdd:CHL00131 84 lgiflafqypIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEklklVGMDPSFLS--RNV---NE---GFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 313 ERKRVSIAEVSICGSKFQCWDNATRGLDsatalefIRALKTQADISNTSAT-----VAI--YQCSQDaYDLFNKVCVLDD 385
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLD-------IDALKIIAEGINKLMTsensiILIthYQRLLD-YIKPDYVHVMQN 227
|
250 260
....*....|....*....|.
gi 398365429 386 GYQIYYGPADKAkKYFEDMGY 406
Cdd:CHL00131 228 GKIIKTGDAELA-KELEKKGY 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
168-418 |
1.04e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 168 KETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSI-------SSNTHGFDLGADTKISYSGYSGddIKKHFRGEVV 240
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDITIDTARSLSQQKG--LIRQLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 241 YNAEADVHLPHLTVFETLVTVARLktpqnrIKGVDRESyANHLAEVAMATYGLSHTRNTkvgndIVRGVSGGERKRVSIA 320
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEGPVI------VKGEPKEE-ATARARELLAKVGLAGKETS-----YPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 321 EVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAiYQCSQdAYDLFNKVCVLDDGYQIYYGPadkAKKY 400
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSF-ARDVADRAIFMDQGRIVEQGP---AKAL 231
|
250
....*....|....*...
gi 398365429 401 FEDmgyvcPSRQTTADFL 418
Cdd:PRK11264 232 FAD-----PQQPRTRQFL 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
881-1088 |
1.10e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNGIP-------RDKSFPRSIGYCQQ 951
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVglESPS----QGNVSWRGEPlaklnraQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 952 QDLHLKTA--TVRESLRfsAYLRQPAEVSIEEKNRYVEEVIKILEM-EKYADAVVGVAGEGlnveQRKRLTIGVELTAKP 1028
Cdd:PRK10419 97 DSISAVNPrkTVREIIR--EPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGG----QLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1029 KLLVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSaiLMQEF-DRLLFMQRGG 1088
Cdd:PRK10419 171 KLLI-LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLR--LVERFcQRVMVMDNGQ 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
183-386 |
1.31e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.90 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISSN---THGfdlgadtKISYSGYSGDDIKK----HFR---GeVVYnaeADVHL-PH 251
Cdd:COG2884 25 IEKGEFVFLTGPSGAGKSTLLKLLYGEerpTSG-------QVLVNGQDLSRLKRreipYLRrriG-VVF---QDFRLlPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 252 LTVFE--TLVTvarlktpqnRIKGVDRESYANHLAEVaMATYGLSHTRNTKVGNdivrgVSGGERKRVSIA-------EV 322
Cdd:COG2884 94 RTVYEnvALPL---------RVTGKSRKEIRRRVREV-LDLVGLSDKAKALPHE-----LSGGEQQRVAIAralvnrpEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 323 SICgskfqcwDNATRGLDSATALEFIRALKtqaDISNTSATVAIyqcSQDAYDLFNK----VCVLDDG 386
Cdd:COG2884 159 LLA-------DEPTGNLDPETSWEIMELLE---EINRRGTTVLI---ATHDLELVDRmpkrVLELEDG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
884-1059 |
1.47e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaERvtM-----GV-ITGDILVNGIP-RDKS--------------- 941
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NR--MndlipGArVEGEILLDGEDiYDPDvdvvelrrrvgmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 ----FPRSI-----------GYCQQQDLHlktATVRESLRfSAYLrqPAEVsieeKNRyveevikiLEMekyadavvgvA 1006
Cdd:COG1117 100 kpnpFPKSIydnvayglrlhGIKSKSELD---EIVEESLR-KAAL--WDEV----KDR--------LKK----------S 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1007 GEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANH 1059
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLL-MDEPTSALDPISTAKIEELILELKKD 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
885-1067 |
1.56e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVITGD------ILVNGIP---------RDKsfprsIGYC 949
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTI-----SKLINGLLLPDdnpnskITVDGITltaktvwdiREK-----VGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 950 -QQQDLHLKTATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKP 1028
Cdd:PRK13640 90 fQNPDNQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLADVGMLDYIDS----EPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365429 1029 KLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTI 1067
Cdd:PRK13640 163 KIII-LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
895-1068 |
1.71e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGIPRDKSFPRS-IGYC-QQQDLHLKTATVRESL----RFS 968
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNlVAYVpQSEEVDWSFPVLVEDVvmmgRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 969 --AYLRQPAEvsieEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELtAKPKLLVFLDEPTSGLDSQTA 1046
Cdd:PRK15056 108 hmGWLRRAKK----RDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLARAI-AQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|..
gi 398365429 1047 WSICQLMKKLANHGQAILCTIH 1068
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTH 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
884-1111 |
1.92e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGI------PRDKS---------FPRSI-G 947
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGEsildlePEERAhlgiflafqYPIEIpG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 948 YCQQQDLHLKTATVRESlrfsaylRQPAEVSIEEKNRYVEEVIKILEM-EKYADAVVgvaGEGLNVEQRKRLTIGVELTA 1026
Cdd:CHL00131 99 VSNADFLRLAYNSKRKF-------QGLPELDPLEFLEIINEKLKLVGMdPSFLSRNV---NEGFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1027 KPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAIlctihqpsaILMQEFDRLL---------FMQRgGKTVYFGDlg 1097
Cdd:CHL00131 169 DSELAI-LDETDSGLDIDALKIIAEGINKLMTSENSI---------ILITHYQRLLdyikpdyvhVMQN-GKIIKTGD-- 235
|
250
....*....|....
gi 398365429 1098 egcKTMIDYFESHG 1111
Cdd:CHL00131 236 ---AELAKELEKKG 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
895-1087 |
1.97e-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: 53.27 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGI------PRDKsfPRSIGYcQQQDL--HLKTAT--- 960
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIA-----GFETpqsGRVLINGVdvtaapPADR--PVSMLF-QENNLfaHLTVEQnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 --VRESLRFSAYLRQPAEVsieeknryveevikilemekyADAVVGVAG------EGLNVEQRKRLTIG-VELTAKPKLL 1031
Cdd:cd03298 93 lgLSPGLKLTAEDRQAIEV---------------------ALARVGLAGlekrlpGELSGGERQRVALArVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1032 vfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAILmQEFDRLLFMQRG 1087
Cdd:cd03298 152 --LDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNG 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
882-1087 |
2.54e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 882 AETRRiLNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT--GDILVNGIP-RDKSFP---RSIGYCQQQDLH 955
Cdd:COG4138 7 AVAGR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-----GLLPgqGEILLNGRPlSDWSAAelaRHRAYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRfsayLRQPAEVSIEEKNRYVEEVIKILEME-KYADAVVGVAGeGlnvE-QRKRLTiGVEL----TAKP- 1028
Cdd:COG4138 81 PFAMPVFQYLA----LHQPAGASSEAVEQLLAQLAEALGLEdKLSRPLTQLSG-G---EwQRVRLA-AVLLqvwpTINPe 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1029 -KLLVfLDEPTSGLD--SQTAwsICQLMKKLANHGQAILCTIHQPSAILmQEFDRLLFMQRG 1087
Cdd:COG4138 152 gQLLL-LDEPMNSLDvaQQAA--LDRLLRELCQQGITVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
878-1042 |
2.58e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 878 VQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNG------IPRDKS---------F 942
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllelSPEDRAgegifmafqY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 943 PRSI-GYCQQQDLHLKTATVREslrfsayLRQPAEVSIEEKNRYVEEVIKILEMEkyADAVVGVAGEGLNVEQRKRLTIg 1021
Cdd:PRK09580 87 PVEIpGVSNQFFLQTALNAVRS-------YRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVNVGFSGGEKKRNDI- 156
|
170 180
....*....|....*....|.
gi 398365429 1022 VELTAKPKLLVFLDEPTSGLD 1042
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
888-1075 |
2.76e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVI---TGDILVNGIPRD-----KSFPRSIGYCQQQDLHLKTA 959
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCL-----FGIYqkdSGSILFQGKEIDfksskEALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAYLRQpaEVSIEEKNRYvEEVIKIL-EMEKYADAVVGVAgeGLNVEQRKRLTIGVELTAKPKlLVFLDEPT 1038
Cdd:PRK10982 89 SVMDNMWLGRYPTK--GMFVDQDKMY-RDTKAIFdELDIDIDPRAKVA--TLSVSQMQMIEIAKAFSYNAK-IVIMDEPT 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365429 1039 SGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILM 1075
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQ 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
888-1064 |
2.87e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGVIT---GDILVNGIPRDksfPRS--------IGYCQQqdlHL 956
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKIL-----YGLYQpdsGEILIDGKPVR---IRSprdaialgIGMVHQ---HF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 957 K---TATVRESLRFSAYLRQPAEVSIEEKNRYVEEVikileMEKY-----ADAVVgvagEGLNVEQRKRltigVE----L 1024
Cdd:COG3845 90 MlvpNLTVAENIVLGLEPTKGGRLDRKAARARIREL-----SERYgldvdPDAKV----EDLSVGEQQR----VEilkaL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365429 1025 TAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAIL 1064
Cdd:COG3845 157 YRGARILI-LDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
895-1098 |
2.88e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.22 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 895 VKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKSFP--R--SIGYcQQQDL--HLktaTVRE-- 963
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIA-----GFLPpdsGRILWNGQDLTALPPaeRpvSMLF-QENNLfpHL---TVAQni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLRFSAYLRqpaeVSIEEKNRyveeVIKILEMekyadavVGVAG------EGLNVEQRKRLTIG-VELTAKPKLLvfLDE 1036
Cdd:COG3840 93 GLGLRPGLK----LTAEQRAQ----VEQALER-------VGLAGlldrlpGQLSGGQRQRVALArCLVRKRPILL--LDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLA-NHGQAILCTIHQPSAILMQeFDRLLFMQRgGKTVYFGDLGE 1098
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARI-ADRVLLVAD-GRIAADGPTAA 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
887-1069 |
3.72e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNG--IPRDK-SFPRSIGYCQQQDLHLKTAT 960
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIA-----GLLnpeKGEILFERqsIKKDLcTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFsaylrqpaEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEPTSG 1040
Cdd:PRK13540 91 LRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSG----QKRQVALLRLWMSKAKLWL-LDEPLVA 157
|
170 180 190
....*....|....*....|....*....|..
gi 398365429 1041 LDSQtawSICQLMKKLANH---GQAILCTIHQ 1069
Cdd:PRK13540 158 LDEL---SLLTIITKIQEHrakGGAVLLTSHQ 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
883-1087 |
4.23e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGIPRDKS-----------FPrsigy 948
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfETPDSGRIMlDGQDITHVPAENRhvntvfqsyalFP----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 949 cqqqdlHLktaTVRESLRFSAYLRQPAEVSIEEKnryVEEVIKILEMEKYADAVVgvagEGLNVEQRKRLTIGVELTAKP 1028
Cdd:PRK09452 100 ------HM---TVFENVAFGLRMQKTPAAEITPR---VMEALRMVQLEEFAQRKP----HQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1029 KLLVfLDEPTSGLD----SQTAWSICQLMKKLanhGQA-ILCTIHQPSAILMQefDRLLFMQRG 1087
Cdd:PRK09452 164 KVLL-LDESLSALDyklrKQMQNELKALQRKL---GITfVFVTHDQEEALTMS--DRIVVMRDG 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
172-395 |
6.09e-07 |
|
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: 53.75 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 172 TFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNT-HGFDLGAdtKISYSGYSGDDIKKHFRGEVV--YNAEADVH 248
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISG--EVLLDGRDLLELSEALRGRRIgmVFQDPMTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 249 LPHLTVFETLVTVARLKtpqnrikGVDRESyANHLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIAEVSICGSK 328
Cdd:COG1123 96 LNPVTVGDQIAEALENL-------GLSRAE-ARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 329 FQCWDNATRGLDSATALEFIRALKTQADISNTsATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPAD 395
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGT-TVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
885-1068 |
6.11e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.34 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVIT---GDILVNG-----IPRDKsfpRS---IGYCQQQ- 952
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTF-----YMIVGLVKpdsGRIFLDGedithLPMHK---RArlgIGYLPQEa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 ----DLhlktaTVRESLRfsAYLRQpAEVSIEEKNRYVEEVIKILEMEK----YADAVVGvaGEglnveqRKRLTIGVEL 1024
Cdd:COG1137 88 sifrKL-----TVEDNIL--AVLEL-RKLSKKEREERLEELLEEFGITHlrksKAYSLSG--GE------RRRVEIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398365429 1025 TAKPKLLvFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIH 1068
Cdd:COG1137 152 ATNPKFI-LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
160-320 |
7.32e-07 |
|
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: 51.75 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 160 GLRKFQRSKetntfQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIKKHFRGeV 239
Cdd:cd03259 5 GLSKTYGSV-----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA----GLERPDSGEILIDGRDVTGVPPERRN-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 240 VYNAEADVHLPHLTVFETLV---TVARLKTPQNRIKgvdresyanhlAEVAMATYGLSHTRNTKvgndiVRGVSGGERKR 316
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAfglKLRGVPKAEIRAR-----------VRELLELVGLEGLLNRY-----PHELSGGQQQR 138
|
....
gi 398365429 317 VSIA 320
Cdd:cd03259 139 VALA 142
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
866-1064 |
8.73e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 866 EAIFHWRNlcyevqIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMGV---ITGDILVNGIprdKSF 942
Cdd:PRK09700 263 ETVFEVRN------VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVdkrAGGEIRLNGK---DIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 943 PRSIGYCQQQDLHLKTATVRESLRFSAY-LRQPAEVSIEEKNRYVEEVIKIL---EMEKYADAvvgvAGEGLN-----VE 1013
Cdd:PRK09700 329 PRSPLDAVKKGMAYITESRRDNGFFPNFsIAQNMAISRSLKDGGYKGAMGLFhevDEQRTAEN----QRELLAlkchsVN 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1014 Q---------RKRLTIGVELTAKPKLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAIL 1064
Cdd:PRK09700 405 QnitelsggnQQKVLISKWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
887-1095 |
1.04e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.92 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDK---SFPRS-IGYC-QQQDLHLKT 958
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILT-----GLLkpqSGEIKIDGITISKenlKEIRKkIGIIfQNPDNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAvvgvagEGLNVE--QRKRLTIGVELTAKPKLLVFlDE 1036
Cdd:PRK13632 99 ATVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDK------EPQNLSggQKQRVAIASVLALNPEIIIF-DE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLANHGQAILCTI-HQpsailMQEF---DRLLFMQrGGKTVYFGD 1095
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISItHD-----MDEAilaDKVIVFS-EGKLIAQGK 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
891-1042 |
1.07e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 891 VDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVIT-GDILVNGI-PRDksfpRSIGYC-QQQDL--HLktaTVRE 963
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITSGEIWiGGRVVNELePAD----RDIAMVfQNYALypHM---SVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLrfsAYLRQPAEVSIEEKNRYVEEVIKILEMEKYAD----AVVGvaGeglnveQRKRLTIGVELTAKPKllVFL-DEPT 1038
Cdd:PRK11650 96 NM---AYGLKIRGMPKAEIEERVAEAARILELEPLLDrkprELSG--G------QRQRVAMGRAIVREPA--VFLfDEPL 162
|
....
gi 398365429 1039 SGLD 1042
Cdd:PRK11650 163 SNLD 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
885-1087 |
1.12e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLD--CLAERVTmgviTGDILVNG--IPRDKS-----FPRSIGYCQQQDLH 955
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKliCGIERPS----AGKIWFSGhdITRLKNrevpfLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKTATVRESLRFSAYLrqpAEVSIEEKNRYVEEVI-KILEMEKYADAVVGVAGeglnvEQRKRLTIGVELTAKPKLLVfL 1034
Cdd:PRK10908 91 LMDRTVYDNVAIPLII---AGASGDDIRRRVSAALdKVGLLDKAKNFPIQLSG-----GEQQRVGIARAVVNKPAVLL-A 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1035 DEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFdRLLFMQRG 1087
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSY-RMLTLSDG 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
884-1068 |
1.20e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.62 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVtMGVITGDILVNGIPRDKSFPR------SIgycQQQDLHLK 957
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RL-LPPDSGEVLVDGLDVATTPSRelakrlAI---LRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TA-TVRESLRFSAY------LRqpaevsiEEKNRYVEEVIKILEME----KYADAVVGvaGeglnveQRKRLTIGVELtA 1026
Cdd:COG4604 88 SRlTVRELVAFGRFpyskgrLT-------AEDREIIDEAIAYLDLEdladRYLDELSG--G------QRQRAFIAMVL-A 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365429 1027 KPKLLVFLDEPTSGLDSQTAWSICQLMKKLAN-HGQAILCTIH 1068
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLH 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
888-1064 |
1.21e-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: 50.51 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPRDKSFPRS-----IGYC----QQQDLH 955
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-----GLRppaSGEITLDGKPVTRRSPRDairagIAYVpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LkTATVRESLRFSAYLrqpaevSieeknryveevikilemekyadavvgvageGLNveQRKrLTIGVELTAKPKLLVfLD 1035
Cdd:cd03215 91 L-DLSVAENIALSSLL------S------------------------------GGN--QQK-VVLARWLARDPRVLI-LD 129
|
170 180
....*....|....*....|....*....
gi 398365429 1036 EPTSGLDSQTAWSICQLMKKLANHGQAIL 1064
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
886-1098 |
1.86e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCL--AERVTMGVITgdilVNGIPRDKSFPR-----SIGYCQQQDLHLKT 958
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLsgIHEPTKGTIT----INNINYNKLDHKlaaqlGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSaylRQPAE-------VSIEEKNRYVEEVIKILEMEKYADAVVGvageGLNVEQRKRLTIGVELTAKPKLL 1031
Cdd:PRK09700 95 LTVLENLYIG---RHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1032 VfLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILmQEFDRLLFMqRGGKTVYFGDLGE 1098
Cdd:PRK09700 168 I-MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR-RICDRYTVM-KDGSSVCSGMVSD 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
879-1064 |
2.26e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 879 QIKAETRRI--LNNVDGWVKPGTLTALMGASGAGKTTLLD--CLAERVTMGVITGD-ILVNGIPRDKSFPRSIGYCQQQD 953
Cdd:PRK11614 10 KVSAHYGKIqaLHEVSLHINQGEIVTLIGANGAGKTTLLGtlCGDPRATSGRIVFDgKDITDWQTAKIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 954 LHLKTATVRESLRFSAYLrqpaevsiEEKNRYVEEVIKILEM-EKYADAVVGVAGEGLNVEQrKRLTIGVELTAKPKLLV 1032
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFF--------AERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQ-QMLAIGRALMSQPRLLL 160
|
170 180 190
....*....|....*....|....*....|..
gi 398365429 1033 fLDEPTSGLDSQTAWSICQLMKKLANHGQAIL 1064
Cdd:PRK11614 161 -LDEPSLGLAPIIIQQIFDTIEQLREQGMTIF 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
884-1047 |
2.53e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 884 TRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTMGVITgdilvngIPRDKsfprSIGYCQQQDLHLKTATV 961
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgeLEPDSGEVS-------IPKGL----RIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 RESL------------RFSAYLRQPAEVSiEEKNRYVEEVIKILEMEKY-ADAVVGVAGEGLNVE--------------Q 1014
Cdd:COG0488 79 LDTVldgdaelraleaELEELEAKLAEPD-EDLERLAELQEEFEALGGWeAEARAEEILSGLGFPeedldrpvselsggW 157
|
170 180 190
....*....|....*....|....*....|....
gi 398365429 1015 RKRLTIGVELTAKPKLLvFLDEPTSGLDSQT-AW 1047
Cdd:COG0488 158 RRRVALARALLSEPDLL-LLDEPTNHLDLESiEW 190
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
885-1087 |
2.85e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGI-PRDKSFP-----RSIGYC-QQQDL 954
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN-----GLLkptSGKIIIDGVdITDKKVKlsdirKKVGLVfQYPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 955 HLKTATVRESLRFSaylrqPAE--VSIEEKNRYVEEVIKI--LEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKPKL 1030
Cdd:PRK13637 95 QLFEETIEKDIAFG-----PINlgLSEEEIENRVKRAMNIvgLDYEDYKDK----SPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1031 LVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQpsailMQEF----DRLLFMQRG 1087
Cdd:PRK13637 166 LI-LDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHS-----MEDVaklaDRIIVMNKG 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
167-320 |
3.22e-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: 49.93 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 167 SKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIKKHFRG-EVVYNAEA 245
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETPTSGEILLDGKDITNLPPHKRPvNTVFQNYA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 246 dvHLPHLTVFETLVTVARLK-TPQNRIKgvdrESYANHLAEVAMATYglshtrntkvGNDIVRGVSGGERKRVSIA 320
Cdd:cd03300 83 --LFPHLTVFENIAFGLRLKkLPKAEIK----ERVAEALDLVQLEGY----------ANRKPSQLSGGQQQRVAIA 142
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
865-1073 |
3.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 865 SEAIFHWRNLCYEVQIKAetrrILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMG----VITGDILVNG--IPR 938
Cdd:PRK14246 7 AEDVFNISRLYLYINDKA----ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskiKVDGKVLYFGkdIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 939 DKSFP--RSIGYCQQQDLHLKTATVRESLRFSayLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRK 1016
Cdd:PRK14246 83 IDAIKlrKEVGMVFQQPNPFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1017 RLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHgQAILCTIHQPSAI 1073
Cdd:PRK14246 161 RLTIARALALKPKVLL-MDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQV 215
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1268-1402 |
3.47e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 49.43 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1268 ARERPSRTF--------SWISFIFAQIFVEVPWNILAGTI----AYFIYYYPIGFYSNASAAgqlhergALFWLFSCAFy 1335
Cdd:COG0842 27 AREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLvllvALLFFGVPLRGLSLLLLL-------LVLLLFALAF- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 1336 vyvGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAV 1402
Cdd:COG0842 99 ---SGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRAL 162
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
885-1087 |
3.88e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLA--ERVTmgviTGDILVNG--IPRDKSFPRSIGYCQQQDLHLKTAT 960
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQT----SGHIRFHGtdVSRLHARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLRFSAYL----RQPAEVSIEEKnryveeVIKILEM-------EKYADAVVGvageglnvEQRKRLTIGVELTAKPK 1029
Cdd:PRK10851 91 VFDNIAFGLTVlprrERPNAAAIKAK------VTQLLEMvqlahlaDRYPAQLSG--------GQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365429 1030 LLVfLDEPTSGLDSQTAWSICQLMKKLanHGQ----AILCTIHQPSAilMQEFDRLLFMQRG 1087
Cdd:PRK10851 157 ILL-LDEPFGALDAQVRKELRRWLRQL--HEElkftSVFVTHDQEEA--MEVADRVVVMSQG 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
886-1081 |
3.97e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPRdkSFPRS---------IGYcqqQD 953
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLL-----KILSGNYqpdAGSILIDGQEM--RFASTtaalaagvaIIY---QE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 954 LHL-KTATVRESLrfsaYLRQ-PAEVSIEEKNRYVEEVIKILE---MEKYADAVVGVagegLNVEQRKRLTIGVELTAKP 1028
Cdd:PRK11288 88 LHLvPEMTVAENL----YLGQlPHKGGIVNRRLLNYEAREQLEhlgVDIDPDTPLKY----LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1029 KLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQpsailMQEFDRL 1081
Cdd:PRK11288 160 RVIAF-DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR-----MEEIFAL 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
886-1087 |
4.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVN--GIPRD-------KSFPRSIGYC-QQQ 952
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMI-----QLTNGLIiseTGQTIVGdyAIPANlkkikevKRLRKEIGLVfQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 953 DLHLKTATVRESLRFSaylrqPAEVSiEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLV 1032
Cdd:PRK13645 100 EYQLFQETIEKDIAFG-----PVNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 1033 fLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAILmQEFDRLLFMQRG 1087
Cdd:PRK13645 174 -LDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVL-RIADEVIVMHEG 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
885-1042 |
5.87e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVITGDILVngIPRDKSFprSIGYCQQQdLHLKTA---TV 961
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGLVAPDEGV--IKRNGKL--RIGYVPQK-LYLDTTlplTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 RESLRFSAYLRQpaevsieeknryvEEVIKILEMEKyADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGL 1041
Cdd:PRK09544 87 NRFLRLRPGTKK-------------EDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV-LDEPTQGV 151
|
.
gi 398365429 1042 D 1042
Cdd:PRK09544 152 D 152
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
888-1049 |
5.88e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.79 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTlldcLAERVT--MGVITGDILVNGIP-RD---KSFPRSIGYCQQQdLHLKTATV 961
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST----IANLLTrfYDIDEGEILLDGHDlRDytlASLRNQVALVSQN-VHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 RESLRFSA---YLRQpaevSIEEKNR--YVEEVIKilEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDE 1036
Cdd:PRK11176 434 ANNIAYARteqYSRE----QIEEAARmaYAMDFIN--KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI-LDE 506
|
170
....*....|...
gi 398365429 1037 PTSGLDSQTAWSI 1049
Cdd:PRK11176 507 ATSALDTESERAI 519
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
888-1069 |
5.93e-06 |
|
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: 50.59 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRS-----IGYCQQQDLHLKTATVR 962
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFSAYLRQPAE-VSIEEKNRYVEEVIKILEMEKYADA-VVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEPTSG 1040
Cdd:TIGR02633 97 ENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGG----QQQLVEIAKALNKQARLLI-LDEPSSS 171
|
170 180
....*....|....*....|....*....
gi 398365429 1041 LDSQTAWSICQLMKKLANHGQAILCTIHQ 1069
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
888-1087 |
6.39e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLldCLAERVTMGVITGDILVNGI-----PRDKSFPRSIGYC-QQQDLHLKTATV 961
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTL--ALHLNGLLRPQKGKVLVSGIdtgdfSKLQGIRKLVGIVfQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 962 RESLRFSaylrqPAEVSIE--EKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKRLTIGVELTAKPKLLVFlDEPTS 1039
Cdd:PRK13644 96 EEDLAFG-----PENLCLPpiEIRKRVDRALAEIGLEKYRHR----SPKTLSGGQGQCVALAGILTMEPECLIF-DEVTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365429 1040 GLDSQTAWSICQLMKKLANHGQAILCTIHQPSAilMQEFDRLLFMQRG 1087
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
174-395 |
6.58e-06 |
|
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: 49.31 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 174 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTH----------GFDLGadtkisysGYSGDDIKKHFrGeVVYNA 243
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfGERRG--------GEDVWELRKRI-G-LVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 244 EADVHLPHLTVFETLVT-----VARLKTPQNRikgvDREsyanhLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVS 318
Cdd:COG1119 87 LQLRFPRDETVLDVVLSgffdsIGLYREPTDE----QRE-----RARELLELLGLAHLADRPFGT-----LSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 319 IA-------EVSICgskfqcwDNATRGLDSATALEFIRALKTqadISNTSATVAIY---------QCsqdaydlFNKVCV 382
Cdd:COG1119 153 IAralvkdpELLIL-------DEPTAGLDLGARELLLALLDK---LAAEGAPTLVLvthhveeipPG-------ITHVLL 215
|
250
....*....|...
gi 398365429 383 LDDGYQIYYGPAD 395
Cdd:COG1119 216 LKDGRVVAAGPKE 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
885-1068 |
6.79e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGIP-RDKSFPRSIGYcqQQDLHLKTATVRE 963
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPvEGPGAERGVVF--QNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLRFSAYLrqpAEVSIEEKNRYVEEVIKIlemekyadavVGVAGEG------LNVEQRKRLTIGVELTAKPKLLVfLDEP 1037
Cdd:PRK11248 90 NVAFGLQL---AGVEKMQRLEIAHQMLKK----------VGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLL-LDEP 155
|
170 180 190
....*....|....*....|....*....|..
gi 398365429 1038 TSGLDSQTAWSICQLMKKL-ANHGQAILCTIH 1068
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
157-392 |
1.27e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 157 LKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGfDLGADTKISYSGYS-------GD 229
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITG-DKSAGSHIELLGRTvqregrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 230 DIKKHfRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNR-----IKGVDRESYANHLAEVAMATYglSHTRntkvgnd 304
Cdd:PRK09984 80 DIRKS-RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswFTREQKQRALQALTRVGMVHF--AHQR------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 305 iVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKtqaDISNTSATVAIYQCSQDAYDL--FNKVCV 382
Cdd:PRK09984 150 -VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR---DINQNDGITVVVTLHQVDYALryCERIVA 225
|
250
....*....|
gi 398365429 383 LDDGYQIYYG 392
Cdd:PRK09984 226 LRQGHVFYDG 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
183-320 |
1.38e-05 |
|
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: 48.20 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISsnthGFdlgadtkisYSGYSGddiKKHFRGEVVYNAEAD--VHL----------- 249
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLIS----GF---------LRPTSG---SVLFDGEDITGLPPHeiARLgigrtfqiprl 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 250 -PHLTVFETLVTVARLKTPQN--RIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNdivrgVSGGERKRVSIA 320
Cdd:cd03219 87 fPELTVLENVMVAAQARTGSGllLARARREEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIA 155
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
849-1087 |
1.44e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.37 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 849 SSEEESDTYGEIGLSKSEAIfhwRNLCyeVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLldCLAERVTMGVIT 928
Cdd:cd03288 3 ASISGSSNSGLVGLGGEIKI---HDLC--VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 929 GDILVNGIPRDKsFP----RSIGYCQQQDLHLKTATVRESLrfsaylrQPAEVSIEEKNRYVEEVIKILEMEKY----AD 1000
Cdd:cd03288 76 GKIVIDGIDISK-LPlhtlRSRLSIILQDPILFSGSIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSlpggLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1001 AVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAwSICQLMKKLANHGQAILCTIHQPSAILmqEFDR 1080
Cdd:cd03288 148 AVVTEGGENFSVGQRQLFCLARAFVRKSSILI-MDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVSTIL--DADL 223
|
....*..
gi 398365429 1081 LLFMQRG 1087
Cdd:cd03288 224 VLVLSRG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
878-1077 |
1.77e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 878 VQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgVITGDILVNGIP----RDKSFPRSIGYCQQQD 953
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PTSGTLLFEGEDistlKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 954 LhLKTATVRESLRFSAYLR--QPAEVSIEEKNRYVEEVIKILemEKYADAVVGvaGEglnveqRKRLTIGVELTAKPKLL 1031
Cdd:PRK10247 91 T-LFGDTVYDNLIFPWQIRnqQPDPAIFLDDLERFALPDTIL--TKNIAELSG--GE------KQRISLIRNLQFMPKVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1032 VfLDEPTSGLDSQTAWSICQLMKKLA-NHGQAILCTIH--------------QPSAILMQE 1077
Cdd:PRK10247 160 L-LDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHdkdeinhadkvitlQPHAGEMQE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
881-1101 |
1.88e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.77 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVI---TGDILVNGIPrdkSFPRSIGYCQQQDLhlk 957
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GILeptSGRVEVNGRV---SALLELGAGFHPEL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 taTVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGV--AGeglnveQRKRLTIGVELTAKPKLLVfLD 1035
Cdd:COG1134 104 --TGRENIYLNGRLLG---LSRKEIDEKFDEIVEFAELGDFIDQPVKTysSG------MRARLAFAVATAVDPDILL-VD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1036 EPTSGLD------SQtawsicQLMKKLANHGQAILCTIHQPSAIlmQEF-DRLLFMQRgGKTVYFGDLGEGCK 1101
Cdd:COG1134 172 EVLAVGDaafqkkCL------ARIRELRESGRTVIFVSHSMGAV--RRLcDRAIWLEK-GRLVMDGDPEEVIA 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
881-1094 |
2.09e-05 |
|
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: 47.53 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 881 KAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGIPrdkSFPRSIGYCQQQDLhlk 957
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLL-----RLLAGIYppdSGTVTVRGRV---SSLLGLGGGFNPEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 taTVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQRKRLTIGVELTAKPKLLVfLDEP 1037
Cdd:cd03220 100 --TGRENIYLNGRLLG---LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG----MKARLAFAIATALEPDILL-IDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 1038 TSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlmQEF-DRLLFMQRgGKTVYFG 1094
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI--KRLcDRALVLEK-GKIRFDG 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
888-1095 |
4.45e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLDCL--------------------------AERVTMGVITGDILVNGIPRDKS 941
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkktkeKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 FPRSIGYCQQ-QDLHLKTATVRESLRFSAylrqpaeVSI-EEKNRYVEEVIKILEMekyadavVGVAGE-------GLNV 1012
Cdd:PRK13651 103 IRRRVGVVFQfAEYQLFEQTIEKDIIFGP-------VSMgVSKEEAKKRAAKYIEL-------VGLDESylqrspfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1013 EQRKRLTIGVELTAKPKLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILmQEFDRLLFMqRGGKTVY 1092
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVF-DEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIFF-KDGKIIK 245
|
...
gi 398365429 1093 FGD 1095
Cdd:PRK13651 246 DGD 248
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
168-398 |
5.18e-05 |
|
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: 46.21 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 168 KETNTFQILKPMDGCLNPGELLVVLGRPGSG-------CTTLLKSISSNTH--GFDLGADTkisysgysgDDIKKHFrGE 238
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGktttikmLTTLLKPTSGRATvaGHDVVREP---------REVRRRI-GI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 239 VVYNAEADvhlPHLTVFETLVTVARLktpqnriKGVDRESYANHLAEVaMATYGLshtrnTKVGNDIVRGVSGGERKRVS 318
Cdd:cd03265 78 VFQDLSVD---DELTGWENLYIHARL-------YGVPGAERRERIDEL-LDFVGL-----LEAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 319 IAEVSICGSKFQCWDNATRGLDSATAL---EFIRALKTQADISNTSATvaiyQCSQDAYDLFNKVCVLDDGYQIYYGPAD 395
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAhvwEYIEKLKEEFGMTILLTT----HYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
...
gi 398365429 396 KAK 398
Cdd:cd03265 218 ELK 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
897-1087 |
5.83e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 897 PGTLTALMGASGAGKTTLLDCLAERVTMGviTGDILVNGipRDKsfprsigycQQQDLH-LKTATVRESLRFS-AYLRQ- 973
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD--AGEVHYRM--RDG---------QLRDLYaLSEAERRRLLRTEwGFVHQh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 974 PAEVsieeknryveevikiLEMEKYADAVVG----------------VAGEGL-NVE----------------QRKRLTI 1020
Cdd:PRK11701 98 PRDG---------------LRMQVSAGGNIGerlmavgarhygdiraTAGDWLeRVEidaariddlpttfsggMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365429 1021 GVELTAKPKLlVFLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPS-AILMQefDRLLFMQRG 1087
Cdd:PRK11701 163 ARNLVTHPRL-VFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAvARLLA--HRLLVMKQG 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
886-1098 |
6.23e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 886 RILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAervtmGVIT---GDILVNGIPRDKSFP---RSIG-YCQQQDLHL-K 957
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVPpdsGTLEIGGNPCARLTPakaHQLGiYLVPQEPLLfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 958 TATVRESLRFsaylRQPAEVSIEEKnryVEEVIKILEMEKYADAVVGVagegLNVEQRKRLTIGVELTAKPKLLVfLDEP 1037
Cdd:PRK15439 100 NLSVKENILF----GLPKRQASMQK---MKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILI-LDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1038 TSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAIlMQEFDRLLFMqRGGKTVYFGDLGE 1098
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEI-RQLADRISVM-RDGTIALSGKTAD 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
176-351 |
6.29e-05 |
|
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: 47.28 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 176 LKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIK-KHFRGEVVYNAEAdvhlPHLtv 254
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLL----GFVDPTEGSIAVNGVPLADADaDSWRDQIAWVPQH----PFL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 255 FETlvTVA---RLKTPQNRIKGVDResyANHLAEVAMATYGLSHTRNTKVGNDiVRGVSGGERKRVSIAEVSICGSKFQC 331
Cdd:TIGR02857 408 FAG--TIAeniRLARPDASDAEIRE---ALERAGLDEFVAALPQGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180
....*....|....*....|
gi 398365429 332 WDNATRGLDSATALEFIRAL 351
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEAL 501
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
903-932 |
6.67e-05 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 45.44 E-value: 6.67e-05
10 20 30
....*....|....*....|....*....|....
gi 398365429 903 LMGASGAGKTTLL----DCLAERVTMGVITGDIL 932
Cdd:COG0378 18 LMGSPGSGKTTLLektiRALKDRLRIAVIEGDIY 51
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
887-1087 |
8.45e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLldclaerVTM--GVIT---GDILVNGI---PRDKSFPRSIGYCQQQDLHLKT 958
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTL-------VTHfnGLIKskyGTIQVGDIyigDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 959 ATVRESLRFSAYLRQPAEVSIEE------------KNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTA 1026
Cdd:PRK13631 114 LRRRVSMVFQFPEYQLFKDTIEKdimfgpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365429 1027 KPKLLVFlDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILmQEFDRLLFMQRG 1087
Cdd:PRK13631 194 QPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
186-392 |
9.02e-05 |
|
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: 45.56 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 186 GELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVhLPHLTVFEtlvTVARLK 265
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQ---NVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 266 TPQNRIKGVDRESYANHLAEVAMAtyGLSHTRntkvgndiVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATAL 345
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLA--GLEKRL--------PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365429 346 EFIR-ALKTQADISNTSATVAiyQCSQDAYDLFNKVCVLDDGYQIYYG 392
Cdd:cd03298 166 EMLDlVLDLHAETKMTVLMVT--HQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
866-1087 |
1.06e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.88 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 866 EAIFHWRNLCYEVQiKAETRRILNNVDGWVKPGTLTALMGASGAGKTT---LLDCLAErvtmgVITGDILVNGiprDKSF 942
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLE-----AESGQIIIDG---DLLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 943 P-------RSIGYC-QQQDLHLKTATVRESLRFSAylrQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGlnveQ 1014
Cdd:PRK13650 73 EenvwdirHKIGMVfQNPDNQFVGATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGG----Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365429 1015 RKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKL-ANHGQAILCTIHQPSAILMQefDRLLFMQRG 1087
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIII-LDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALS--DRVLVMKNG 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
885-1067 |
1.06e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNG--IPrdkSFPRSigycqqqdlHLKTA 959
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLL-----RLIGGQIapdHGEILFDGenIP---AMSRS---------RLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRF-SAYLRQPAEV------SIEEKNRYVEEVIKILEMEKYadAVVGVAGEG------LNVEQRKRLTIGVELTA 1026
Cdd:PRK11831 83 RKRMSMLFqSGALFTDMNVfdnvayPLREHTQLPAPLLHSTVMMKL--EAVGLRGAAklmpseLSGGMARRAALARAIAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365429 1027 KPKLLVFlDEPTSGLDSQTAWSICQLMKKLaNHGQAILCTI 1067
Cdd:PRK11831 161 EPDLIMF-DEPFVGQDPITMGVLVKLISEL-NSALGVTCVV 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
887-1056 |
1.11e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTT----LLDCLAERvtmgvitGDILVNGIPrdksfprsigycqqqdlhLKTATVR 962
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQP------------------LHNLNRR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLRFsaylRQPAEVSIEEKNRY------VEEVI--------KILEMEKYADAVVGVAGE-GLNVE------------QR 1015
Cdd:PRK15134 356 QLLPV----RHRIQVVFQDPNSSlnprlnVLQIIeeglrvhqPTLSAAQREQQVIAVMEEvGLDPEtrhrypaefsggQR 431
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365429 1016 KRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKL 1056
Cdd:PRK15134 432 QRIAIARALILKPSLII-LDEPTSSLDKTVQAQILALLKSL 471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
885-1078 |
1.14e-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: 47.21 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaerVTMGVITGDILVNGIPRD----KSFPRSIGYCQQQdLHLKTAT 960
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEGEIQIDGVSWNsvtlQTWRKAFGVIPQK-VFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 961 VRESLrfsaylrQP-AEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEG---LNVEQRKRLTIGVELTAKPKLLVfLDE 1036
Cdd:TIGR01271 1308 FRKNL-------DPyEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILL-LDE 1379
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365429 1037 PTSGLDSQTAWSICQLMKKLANHGQAILCTiHQPSAIL-MQEF 1078
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSE-HRVEALLeCQQF 1421
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1208-1409 |
1.15e-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: 46.23 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1208 SKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILqqYLPSFVqqrdlyeARERPSRTFSWI-------- 1279
Cdd:pfam12698 133 VLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAA--IIAVSI-------VEEKESRIKERLlvsgvspl 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 1280 SFIFAQIFvevpWNILAGTIAYFIYYYpIGFYSNASaagqLHERGALFWLFSCAFYVYVgSMGLLVISFNQVAESAANLA 1359
Cdd:pfam12698 204 QYWLGKIL----GDFLVGLLQLLIILL-LLFGIGIP----FGNLGLLLLLFLLYGLAYI-ALGYLLGSLFKNSEDAQSII 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365429 1360 SLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDV 1409
Cdd:pfam12698 274 GIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLW 323
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
175-320 |
1.63e-04 |
|
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: 44.27 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 175 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTV 254
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA----GLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 255 FETLVTVARLktpqnrikgvdrESYANHLAEVAMATYGLSHTRNTkvgndIVRGVSGGERKRVSIA 320
Cdd:TIGR01189 91 LENLHFWAAI------------HGGAQRTIEDALAAVGLTGFEDL-----PAAQLSAGQQRRLALA 139
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
888-1069 |
1.66e-04 |
|
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: 44.63 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 888 LNNVDGWVKPGTLTALMGASGAGKTTLLdcLAERVTMGVITGDIL-VNGIPRDKSFPR-------SIGYCQQQDLhLKTA 959
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHwSNKNESEPSFEAtrsrnrySVAYAAQKPW-LLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRF-SAYLRQPAEVSIEEKNryVEEVIKILemeKYADAV-VGVAGEGLNVEQRKRLTIGVELTAKPKLlVFLDEP 1037
Cdd:cd03290 94 TVEENITFgSPFNKQRYKAVTDACS--LQPDIDLL---PFGDQTeIGERGINLSGGQRQRICVARALYQNTNI-VFLDDP 167
|
170 180 190
....*....|....*....|....*....|....
gi 398365429 1038 TSGLDSQTAWSICQ--LMKKLANHGQAILCTIHQ 1069
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
879-926 |
1.86e-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: 44.29 E-value: 1.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398365429 879 QIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGV 926
Cdd:pfam13481 14 GLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGK 61
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
898-1056 |
1.98e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 898 GTLTALMGASGAGKTTLLDCLAErvTMGVITGDILVNG--IPR--DKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQ 973
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSR--LMTPAHGHVWLDGehIQHyaSKEVARRIGLLAQNATTPGDITVQELVARGRYPHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 974 PAevsieeKNRYVEEVIKILEMEKYADAVVGVAGEGLNV---EQRKRLTIGVELtAKPKLLVFLDEPTSGLDSQTAWSIC 1050
Cdd:PRK10253 111 PL------FTRWRKEDEEAVTKAMQATGITHLADQSVDTlsgGQRQRAWIAMVL-AQETAIMLLDEPTTWLDISHQIDLL 183
|
....*.
gi 398365429 1051 QLMKKL 1056
Cdd:PRK10253 184 ELLSEL 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
866-1044 |
1.99e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.01 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 866 EAIFHWRNLCYevQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLldclaERVTMGVI---TGDILVNGIPRDKS- 941
Cdd:PRK13635 3 EEIIRVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL-----AKLLNGLLlpeAGTITVGGMVLSEEt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 942 ---FPRSIGYC-QQQDLHLKTATVRESLRFSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAvvgvAGEGLNVEQRKR 1017
Cdd:PRK13635 76 vwdVRRQVGMVfQNPDNQFVGATVQDDVAFGLENIG---VPREEMVERVDQALRQVGMEDFLNR----EPHRLSGGQKQR 148
|
170 180
....*....|....*....|....*..
gi 398365429 1018 LTIGVELTAKPKLLVfLDEPTSGLDSQ 1044
Cdd:PRK13635 149 VAIAGVLALQPDIII-LDEATSMLDPR 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
885-1045 |
2.59e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 885 RRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAER-------VTMGVITgdilvngiprdksfprSIGYC-QQQD-LH 955
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepdsgtVKLGETV----------------KIGYFdQHQEeLD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 956 LKtATVRESLRfsaylrqpaEVSIEEKNRyveEVIKILEM----EKYADAVVGV--AGEglnveqRKRLTIGVELTAKPK 1029
Cdd:COG0488 392 PD-KTVLDELR---------DGAPGGTEQ---EVRGYLGRflfsGDDAFKPVGVlsGGE------KARLALAKLLLSPPN 452
|
170
....*....|....*.
gi 398365429 1030 LLVfLDEPTSGLDSQT 1045
Cdd:COG0488 453 VLL-LDEPTNHLDIET 467
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
887-1068 |
2.84e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLdclaeRVTMGVI---TGDILVNGiprdksfprsigycqqqdlhlKTATVRE 963
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLL-----RVLAGLLhveSGQIQIDG---------------------KTATRGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 964 SLRFSAYLRQ----PAEVSIEEKNRYVEEV--IKILEMEKYADAVVGVAG------EGLNVEQRKRLTIGvELTAKPKLL 1031
Cdd:PRK13543 80 RSRFMAYLGHlpglKADLSTLENLHFLCGLhgRRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALA-RLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365429 1032 VFLDEPTSGLDSQtawSICQLMKKLANH---GQAILCTIH 1068
Cdd:PRK13543 159 WLLDEPYANLDLE---GITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
905-1042 |
4.83e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 905 GASGAGKTTlldclaervTMGVITGdIL-------------VNgiPRDKSFPRSIGYCQQ-----QDLhlktaTVRESLR 966
Cdd:NF033858 299 GSNGCGKST---------TMKMLTG-LLpasegeawlfgqpVD--AGDIATRRRVGYMSQafslyGEL-----TVRQNLE 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 967 FSAYLRQpaeVSIEEKNRYVEEVIKILEMEKYADAVvgvaGEGLNVEQRKRLTIGVELTAKPKLLVfLDEPTSGLD 1042
Cdd:NF033858 362 LHARLFH---LPAAEIAARVAEMLERFDLADVADAL----PDSLPLGIRQRLSLAVAVIHKPELLI-LDEPTSGVD 429
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
171-322 |
8.46e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 171 NTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHgfdlgadtkiSYSGYSGDDIKKHFRGEVVYNAEADVHLP 250
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLH----------VESGQIQIDGKTATRGDRSRFMAYLGHLP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 251 HLTV-FETLVTVARLKTPQNRikgvdresYANHLAEVAMATYGLSHTRNTkvgndIVRGVSGGERKRVSIAEV 322
Cdd:PRK13543 92 GLKAdLSTLENLHFLCGLHGR--------RAKQMPGSALAIVGLAGYEDT-----LVRQLSAGQKKRLALARL 151
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
167-258 |
1.10e-03 |
|
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: 41.61 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 167 SKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIS---SNTHGfdlgadtKISYSGYSGDDIKKHFRGEVVYNA 243
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILgllKPDSG-------EIKVLGKDIKKEPEEVKRRIGYLP 79
|
90
....*....|....*
gi 398365429 244 EADVHLPHLTVFETL 258
Cdd:cd03230 80 EEPSLYENLTVRENL 94
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
612-711 |
1.37e-03 |
|
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: 42.76 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 612 LIIAVCFNIIFYFLVDFRRNGGVFFFYLLInIVAVFSMSHLFrcvGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKIL 691
Cdd:pfam12698 219 LQLLIILLLLFGIGIPFGNLGLLLLLFLLY-GLAYIALGYLL---GSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPP 294
|
90 100
....*....|....*....|
gi 398365429 692 RWSKWIWYINPLAYLFESLL 711
Cdd:pfam12698 295 SFLQWIFSIIPFFSPIDGLL 314
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
871-1045 |
1.77e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.01 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 871 WRNLCyeVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAeRVTMGViTGDILVNGIPRDKsfprsIGYcq 950
Cdd:TIGR00957 1287 FRNYC--LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESA-EGEIIIDGLNIAK-----IGL-- 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 951 qQDLHLK-TATVRESLRFSAYLRqpaeVSIEEKNRYV-EEVIKILEMEKYADAVVGV----------AGEGLNVEQRKRL 1018
Cdd:TIGR00957 1356 -HDLRFKiTIIPQDPVLFSGSLR----MNLDPFSQYSdEEVWWALELAHLKTFVSALpdkldhecaeGGENLSVGQRQLV 1430
|
170 180
....*....|....*....|....*..
gi 398365429 1019 TIGVELTAKPKLLVfLDEPTSGLDSQT 1045
Cdd:TIGR00957 1431 CLARALLRKTKILV-LDEATAAVDLET 1456
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
169-319 |
2.13e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.24 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 169 ETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLK---SISSNTHGFDLgadtkisysgYSGDDIK----KHFRGEVVY 241
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSLISPTSGTLL----------FEGEDIStlkpEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 242 NAEAdvhlPHL---TVFETLVtvarlkTP-QNRIKGVDRESYANHLAEvamatYGLSHTRNTKVGNDIvrgvSGGERKRV 317
Cdd:PRK10247 86 CAQT----PTLfgdTVYDNLI------FPwQIRNQQPDPAIFLDDLER-----FALPDTILTKNIAEL----SGGEKQRI 146
|
..
gi 398365429 318 SI 319
Cdd:PRK10247 147 SL 148
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
612-710 |
2.15e-03 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 40.95 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 612 LIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKIL 691
Cdd:COG0842 61 LLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLP 140
|
90
....*....|....*....
gi 398365429 692 RWSKWIWYINPLAYLFESL 710
Cdd:COG0842 141 GWLQAIAYLNPLTYFVEAL 159
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
887-1087 |
2.21e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.76 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 887 ILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTmgvITGDILVNGIPRDK----SFPRSIGYCQQQdLHLKTATVR 962
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN---TEGDIQIDGVSWNSvplqKWRKAFGVIPQK-VFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 963 ESLrfsaylrQPAEV-SIEEKNRYVEEVIKILEMEKYADAVVGVAGEG---LNVEQRKRLTIGVELTAKPKLLVfLDEPT 1038
Cdd:cd03289 95 KNL-------DPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILL-LDEPS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1039 SGLDSQTAwsicQLMKKLANHGQAIlCTI----HQPSAILmqEFDRLLFMQRG 1087
Cdd:cd03289 167 AHLDPITY----QVIRKTLKQAFAD-CTVilseHRIEAML--ECQRFLVIEEN 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
883-1043 |
2.94e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 883 ETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLaervtMG---VITGDILVNgiprdksfpRSIGYCQQQDLhLKTA 959
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-----LSqfeISEGRVWAE---------RSIAYVPQQAW-IMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 960 TVRESLRFSAylrqpaevsiEEKNRYVEEVIKILEMEkyADavVGVAGEGLNVEQRKRltiGVELTAKPKLLV------- 1032
Cdd:PTZ00243 736 TVRGNILFFD----------EEDAARLADAVRVSQLE--AD--LAQLGGGLETEIGEK---GVNLSGGQKARVslaravy 798
|
170
....*....|....*..
gi 398365429 1033 ------FLDEPTSGLDS 1043
Cdd:PTZ00243 799 anrdvyLLDDPLSALDA 815
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
183-346 |
3.93e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.65 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTT---LLKSISSNTHGFDLGADTKISYSGYSgddiKKHFRGEVVYNAEADVhLPHLTVFETLV 259
Cdd:PRK10895 26 VNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLLPLH----ARARRGIGYLPQEASI-FRRLSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 260 TVARLKTPQNRIKGVDResyanhlAEVAMATYGLSHTRNTkvgndIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGL 339
Cdd:PRK10895 101 AVLQIRDDLSAEQREDR-------ANELMEEFHIEHLRDS-----MGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
....*..
gi 398365429 340 DSATALE 346
Cdd:PRK10895 169 DPISVID 175
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
171-395 |
4.14e-03 |
|
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: 40.73 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 171 NTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSIssnthgfdLGadtkisysgysgddIKKHFRGEVVYNAEaDVH-L 249
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI--------IG--------------LLRPDSGEILVDGQ-DITgL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 250 PH----------------------LTVFEtlvTVA-----RLKTPQNRIKgvdresyanHLAEVAMATYGLSHTRNtKVG 302
Cdd:COG1127 73 SEkelyelrrrigmlfqggalfdsLTVFE---NVAfplreHTDLSEAEIR---------ELVLEKLELVGLPGAAD-KMP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 303 NDIvrgvSGGERKRVSIA-------EVSICgskfqcwDNATRGLDSATALEF---IRALKTQADIsnTSATVaiyqcSQD 372
Cdd:COG1127 140 SEL----SGGMRKRVALAralaldpEILLY-------DEPTAGLDPITSAVIdelIRELRDELGL--TSVVV-----THD 201
|
250 260
....*....|....*....|....*.
gi 398365429 373 ---AYDLFNKVCVLDDGYQIYYGPAD 395
Cdd:COG1127 202 ldsAFAIADRVAVLADGKIIAEGTPE 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1015-1087 |
4.34e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365429 1015 RKRLTIGVELTAKPKLLVfLDEPTSGLDSQTAWSICQLMKKLANHGQAILcTIHQPSAILMQEFDRLLFMQRG 1087
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILM-LDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
175-386 |
4.59e-03 |
|
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: 40.29 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 175 ILKPMDGCLNPGELLVVLGRPGSGCTTLLKSI------SSNTHGFDlGADTKisysGYSGDDIKKHFrGEVvynaEADVH 248
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvDSGRILID-GHDVR----DYTLASLRRQI-GLV----SQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 249 LPHLTVFETlVTVARLKTPQNRIKGVDRESYANHLAEvamatyGLSHTRNTKVGndiVRGV--SGGERKRVSIAEVSICG 326
Cdd:cd03251 87 LFNDTVAEN-IAYGRPGATREEVEEAARAANAHEFIM------ELPEGYDTVIG---ERGVklSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365429 327 SKFQCWDNATRGLDSAT------ALEFIRALKTQADISNTSATVaiyqcsQDAydlfNKVCVLDDG 386
Cdd:cd03251 157 PPILILDEATSALDTESerlvqaALERLMKNRTTFVIAHRLSTI------ENA----DRIVVLEDG 212
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
891-925 |
4.63e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 41.04 E-value: 4.63e-03
10 20 30
....*....|....*....|....*....|....*
gi 398365429 891 VDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMG 925
Cdd:COG3598 6 VPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAG 40
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
878-921 |
4.63e-03 |
|
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: 38.97 E-value: 4.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 398365429 878 VQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAER 921
Cdd:cd03221 6 LSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE 49
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
174-320 |
4.71e-03 |
|
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: 39.73 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 174 QILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISsnthGfdlgadtkisysgysgddIKKHFRGEVVYNAEADVHLPHLT 253
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA----G------------------LLKPSSGEILLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 254 VFETLVTVarlktPQnrikgvdresyanhlaevAMATYGLSHTRNtkvgndivRGV---SGGERKRVSIA 320
Cdd:cd03214 71 LARKIAYV-----PQ------------------ALELLGLAHLAD--------RPFnelSGGERQRVLLA 109
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
183-320 |
5.69e-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: 40.15 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISsnthGFDlgadtkisysgysgddikKHFRGEVVYNAEA--------------DVH 248
Cdd:cd03293 27 VEEGEFVALVGPSGCGKSTLLRIIA----GLE------------------RPTSGEVLVDGEPvtgpgpdrgyvfqqDAL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365429 249 LPHLTVFEtlvtvarlktpqN-----RIKGVDRESyANHLAEVAMATYGLSHTRNTKvgndiVRGVSGGERKRVSIA 320
Cdd:cd03293 85 LPWLTVLD------------NvalglELQGVPKAE-ARERAEELLELVGLSGFENAY-----PHQLSGGMRQRVALA 143
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
183-320 |
6.93e-03 |
|
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: 40.47 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365429 183 LNPGELLVVLGRPGSGCTTLLKSISsnthGFDLGADTKISysgysgddikkhFRGEVVYNAEADVHLP------------ 250
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIA----GLERPDSGRIR------------LGGEVLQDSARGIFLPphrrrigyvfqe 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365429 251 -----HLTVFETLV-TVARLKTPQNRIkgvdresyanHLAEVAmATYGLSH--TRNtkvgndiVRGVSGGERKRVSIA 320
Cdd:COG4148 86 arlfpHLSVRGNLLyGRKRAPRAERRI----------SFDEVV-ELLGIGHllDRR-------PATLSGGERQRVAIG 145
|
|
| |
