|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
90-1478 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1775.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 90 PEFRARDWAKAFYNARYNADENCPPRVAGVAFKDLNVSGYGSPVDYQMSVGNALLKLPTQIYQFLGGKK--RKINILQGL 167
Cdd:TIGR00956 1 EEFNAKAWVKNFRKLIDSDPIYYKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRdtKTFDILKPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 168 DGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVDPAAYINYHGITPKQMSTDFRGEAIYTAEVDAHYPQLSVGDTLY 247
Cdd:TIGR00956 81 DGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 248 FASLARAPRHLPGGISSQEYATHLRDVIMAMFGIGHTINTRVGNDFVRGVSGGERKRVTIAEAALSYAPLQCWDNSTRGL 327
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 328 DSANAVEFCRTLRTQSDVFGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAKAYFERLGFLCPESQTTADFLT 407
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 408 SMSSPTERIIRPGFESLAPRTSEEFAKHWKESNERQSLLRQIDQYANEHPfDGDDLDRFAQSRKTEKSKNQRQKSPYTLS 487
Cdd:TIGR00956 321 SLTSPAERQIKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRCS-ESDTKEAYRESHVAKQSKRTRPSSPYTVS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 488 YWGQIRLCMWRELQRLKNDPSVTIVMLINNFFEALIISSIFYNLSGNTSSFFSRGAILFMMVLLNAFSSMLEILSLYAKR 567
Cdd:TIGR00956 400 FSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIASMYEAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 568 TIVEKHNRYALYHPSAEAISSMIMDMPYKIVNSILMNLTLYFMANLRREPGPFFFNYLISFMMVMSMSMFFRLFASLTKT 647
Cdd:TIGR00956 480 PIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 648 IQQALAPSSIILMALVLYTGFAIPVSYMRGWASWIRYLNPVAYGFEAIMVNEFHGRTFPCASFVPSGVGYENISKDEHIC 727
Cdd:TIGR00956 560 LSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYDNLGVTNKVC 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 728 SVVGSIPGSDLVDGTAFVKSTYGYENSHRWRNFGIILALTVFLALCQLIATELVASERSKGEVLVFRRGSSQKARTKQCQ 807
Cdd:TIGR00956 640 TVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKKAGET 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 808 HD------EERTQAPVIQNEKHSEGPDSTIGVEKQT--SIFHWENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSG 879
Cdd:TIGR00956 720 SAsnkndiEAGEVLGSTDLTDESDDVNDEKDMEKESgeDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASG 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 880 AGKTTLLDVLANRTTVGVV-GGDMLVDGRPRDSSFQRKTGYVQQQDLHLHTSTVREALEFSALLRQPPQYTREEKLDYVE 958
Cdd:TIGR00956 800 AGKTTLLNVLAERVTTGVItGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVE 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 959 KVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTI 1038
Cdd:TIGR00956 880 EVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTI 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1039 HQPSAMLFQRFDRLLLLAKGGKTVYFGDIGRESRILMDYFTRNGGPALPPGSNPAEHMLEVIGAAPGAKSEIDWPAVWRN 1118
Cdd:TIGR00956 960 HQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRN 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1119 SPEYQNVRHELSNlraLANQPSPISDTNEKSSYAEFAAPFATQFMQVGLRVFQQYWRTPAYIYSKVLLTIGCSLFIGFSF 1198
Cdd:TIGR00956 1040 SSEYQAVKNELDR---LEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTF 1116
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1199 FKADNTAQGLQNQMFGVFVFLFVVIQLIIQIIPSFVTQRTLYEARERQSKTYSWQAFVVTNILVELAWNSIMAIFCFLVW 1278
Cdd:TIGR00956 1117 FKVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIW 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1279 FYPVGLFHNAEYTDTLHSRSTLAFLFIWVTFLFASSLAHMLIAGIESEEIASSLSNILAIMMYAFCGILAGPGALPGFWI 1358
Cdd:TIGR00956 1197 YYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWI 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1359 FMYRVNPFTYLVSGLLSTSLGEAPMYCAENEFLSFSTPANLTCGEYMQGYISTNGGYLLNSEAQGgeGCHFCATGNTTQF 1438
Cdd:TIGR00956 1277 FMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAGGYLLNPNATD--SCSFCQYSYTNDF 1354
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|
gi 1799732068 1439 LQNVHIDFSTRWRDFGLMWVYVAFNIVAAISLYWLSRVPK 1478
Cdd:TIGR00956 1355 LEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
157-1380 |
6.73e-128 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 433.50 E-value: 6.73e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 157 KKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPA----AYINYHG-----ITPKQMSTdfrgea 227
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAG-----KLDPSlkvsGEITYNGyrlneFVPRKTSA------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 228 iYTAEVDAHYPQLSVGDTLYFAS--------------LARapRHLPGGISSQE------YATHLR--------DVIMAMF 279
Cdd:PLN03140 243 -YISQNDVHVGVMTVKETLDFSArcqgvgtrydllseLAR--REKDAGIFPEAevdlfmKATAMEgvksslitDYTLKIL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 280 GIGHTINTRVGNDFVRGVSGGERKRVTIAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQAPQ 359
Cdd:PLN03140 320 GLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAP 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 360 AAYNLFDKVIVLYEGHQIYFGAAHDAKAYFERLGFLCPESQTTADFLTSMSSPTERIIRPGFESLAPR--TSEEFAKHWK 437
Cdd:PLN03140 400 ETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRyiSVSEFAERFK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 438 ESNERQSLLRQIDQyanehPFDgddldrfaqsrKTEKSKNQRQKSPYTLSYWGQIRLCMWRELQRLKNDPSVTIVMLINN 517
Cdd:PLN03140 480 SFHVGMQLENELSV-----PFD-----------KSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 518 FFEALIISSIFYNLSGNTSS----FFSRGAILFMMVLlNAFSSMLEiLSLYAKRTIVEKHNRYALYHPS-AEAISSMIMD 592
Cdd:PLN03140 544 IIVAAIASTVFLRTEMHTRNeedgALYIGALLFSMII-NMFNGFAE-LALMIQRLPVFYKQRDLLFHPPwTFTLPTFLLG 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 593 MPYKIVNSILMNLTLYFMANLRREPGPFFFNYLISFMMVMSMSMFFRLFASLTKTIQQALAPSSIILMALVLYTGFAIPV 672
Cdd:PLN03140 622 IPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPK 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 673 SYMRGWASWIRYLNPVAYGFEAIMVNEFhgrtfpcasFVPSgvgYENISKDEHICSVvgsipgsdlvdGTAFVKSTYGYE 752
Cdd:PLN03140 702 GEIPNWWEWAYWVSPLSYGFNALAVNEM---------FAPR---WMNKMASDNSTRL-----------GTAVLNIFDVFT 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 753 NSH-RWRNFGIILALTVF------LALC--------QLIATELVASERSKGEVLVFRRGSSQKA-RTKQCQHDEERTQAP 816
Cdd:PLN03140 759 DKNwYWIGVGALLGFTILfnvlftLALTylnplgkkQAIISEETAEEMEGEEDSIPRSLSSADGnNTREVAIQRMSNPEG 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 817 VIQNEKHSEGPDSTIGVEKQTSI------FHWENVCYDVKIKSETR---------RILDHVDGWIKPGTLTALMGSSGAG 881
Cdd:PLN03140 839 LSKNRDSSLEAANGVAPKRGMVLpftplaMSFDDVNYFVDMPAEMKeqgvtedrlQLLREVTGAFRPGVLTALMGVSGAG 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 882 KTTLLDVLANRTTVGVVGGDMLVDGRP-RDSSFQRKTGYVQQQDLHLHTSTVREALEFSALLRQPPQYTREEKLDYVEKV 960
Cdd:PLN03140 919 KTTLMDVLAGRKTGGYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEV 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 961 LDLLNMRDYADAIVGIPG-EGLNVEQRKRLTIGVELAARPKLLlFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PLN03140 999 MELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1040 QPSAMLFQRFDRLLLLAKGGKTVYFGDIGRESRILMDYFTR-NGGPALPPGSNPAEHMLEVIGAAPGAKSEIDWPAVWRN 1118
Cdd:PLN03140 1078 QPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAiPGVPKIKEKYNPATWMLEVSSLAAEVKLGIDFAEHYKS 1157
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1119 SPEYQNVRhelSNLRALANQPSPISDTNekssyaefaapFATQFMQVGLRVFQQ--------YWRTPAYIYSKVLLTIGC 1190
Cdd:PLN03140 1158 SSLYQRNK---ALVKELSTPPPGASDLY-----------FATQYSQSTWGQFKSclwkqwwtYWRSPDYNLVRFFFTLAA 1223
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1191 SLFIGFSFF----KADNTAQGLQNQMFGVFVFLFVVIQLIIQIIPSFVTQRTLYeARERQSKTYSWQAFVVTNILVELAW 1266
Cdd:PLN03140 1224 ALMVGTIFWkvgtKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVF-YRERAAGMYSALPYAIAQVVCEIPY 1302
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1267 NSIMAIFCFLVWFYPVGLfhnaEYTdtlhSRSTLAFLFI-WVTFLFASSLAHMLIAGIESEEIASslsnILAIMMYA--- 1342
Cdd:PLN03140 1303 VLIQTTYYTLIVYAMVAF----EWT----AAKFFWFYFIsFFSFLYFTYYGMMTVSLTPNQQVAA----IFAAAFYGlfn 1370
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 1799732068 1343 -FCGILAGPGALPGFWIFMYRVNPFTYLVSGLLSTSLGE 1380
Cdd:PLN03140 1371 lFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGD 1409
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
838-1065 |
1.24e-105 |
|
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: 333.44 E-value: 1.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 838 SIFHWENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGRPRDSSFQRKT 917
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 918 GYVQQQDLHLHTSTVREALEFSALLRqppqytreekldyvekvldllnmrdyadaivgipgeGLNVEQRKRLTIGVELAA 997
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 998 RPkLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKGGKTVYFG 1065
Cdd:cd03232 126 KP-SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
852-1374 |
1.16e-79 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 276.16 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 852 KSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGV-VGGDMLVDGRPRDSSFQRK-TGYVQQQDLHLHT 929
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAiSAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPG--EGLNVEQRKRLTIGVELAARPKLLlFLDE 1007
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLL-FCDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKgGKTVYFGDIGResriLMDYFTRNGGPaLP 1087
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE-GRVAYLGSPDQ----AVPFFSDLGHP-CP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1088 PGSNPAEHMLEVIGAAPG--AKSEIDWPAVWRN--SPEYQNVRHELSNLRALANQPSPISDTNEKSSyaEFAAPFATQFM 1163
Cdd:TIGR00955 267 ENYNPADFYVQVLAVIPGseNESRERIEKICDSfaVSDIGRDMLVNTNLWSGKAGGLVKDSENMEGI--GYNASWWTQFY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1164 QVGLRVFQQYWRTPAYIYSKVLLTIGCSLFIGFSFFKADNTAQGLQN-QMFGVFVFLFVVIQLIIQIIPSFVTQRTLYeA 1242
Cdd:TIGR00955 345 ALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNiNGALFLFLTNMTFQNVFPVINVFTAELPVF-L 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1243 RERQSKTYSWQAFVVTNILVELAWnSIMAIFCFLVWFYP-VGLFHNAEYtdtlhsrsTLAFLFIWV-TFLFASSLAHMLI 1320
Cdd:TIGR00955 424 RETRSGLYRVSAYFLAKTIAELPL-FIILPALFTSITYWmIGLRSGATH--------FLTFLFLVTlVANVATSFGYLIS 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 1321 AGIESEEIASSLSNILAIMMYAFCGILAGPGALPGFWIFMYRVNPFTYLVSGLL 1374
Cdd:TIGR00955 495 CAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLL 548
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
149-380 |
1.75e-67 |
|
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: 225.99 E-value: 1.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 149 QIYQFLGGKKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFqVDPAAYINYHGITPKQMSTDFRGEAI 228
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 229 YTAEVDAHYPQLSVGDTLYFASLARaprhlpggissqeyathlrdvimamfgightintrvGNDFVRGVSGGERKRVTIA 308
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799732068 309 EAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
838-1065 |
1.95e-64 |
|
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: 217.03 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 838 SIFHWENVCYDVKIKSET--RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGRPRD-SSFQ 914
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDkRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 915 RKTGYVQQQDLHLHTSTVREALEFSALLRqppqytreekldyvekvldllnmrdyadaivGIPGEglnveQRKRLTIGVE 994
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------GLSGG-----ERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 995 LAARPkLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKgGKTVYFG 1065
Cdd:cd03213 126 LVSNP-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
152-777 |
8.41e-56 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 206.05 E-value: 8.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 152 QFLGGKKRKInILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG-ETHGFQVDPAAYINYHGITPKQMstdfRGEAIYT 230
Cdd:TIGR00955 30 CFCRERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSGSVLLNGMPIDAKEM----RAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 231 AEVDAHYPQLSVGDTLYFASLARAPRHLPggisSQEYATHLRDVIMAMfGIGHTINTRVGN-DFVRGVSGGERKRVTIAE 309
Cdd:TIGR00955 105 QQDDLFIPTLTVREHLMFQAHLRMPRRVT----KKEKRERVDEVLQAL-GLRKCANTRIGVpGRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 310 AALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAKAYF 389
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 390 ERLGFLCPESQTTADFLTSMSSpteriIRPGFESlAPRtsEEFAKHWkESNERQSLLRQIDQYANEHPFDGDDLDRFAQS 469
Cdd:TIGR00955 259 SDLGHPCPENYNPADFYVQVLA-----VIPGSEN-ESR--ERIEKIC-DSFAVSDIGRDMLVNTNLWSGKAGGLVKDSEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 470 RKteksknqrqKSPYTLSYWGQIRLCMWRELQRLKNDPSVTIVMLINNFFEALIISSIFYNLSGNTSSFFSRGAILFMMV 549
Cdd:TIGR00955 330 ME---------GIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 550 LLNAFSSMLEILSLY-AKRTIVEKHNRYALYHPSAEAISSMIMDMPYKIVNSILMNLTLYFMANLRREPGPFFFNYLISF 628
Cdd:TIGR00955 401 TNMTFQNVFPVINVFtAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 629 MMVMSMSMFFRLFASLTKTIQQALAPSSIILMALVLYTGF-----AIPVSYMrgwasWIRYLNPVAYGFEAIMVNEFHGR 703
Cdd:TIGR00955 481 LVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFfinsdSIPVYFK-----WLSYLSWFRYGNEGLLINQWSDV 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 704 TfPCASFVpsgvgyeniskdehiCSVVGSIPGSDLVdgtafVKSTYGYENSHRWRNFGIILALTVFLALCQLIA 777
Cdd:TIGR00955 556 D-NIECTS---------------ANTTGPCPSSGEV-----ILETLSFRNADLYLDLIGLVILIFFFRLLAYFA 608
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
842-1065 |
1.83e-51 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 181.32 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 842 WENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRT-TVGVVGGDMLVDGRPRD-SSFQRKTGY 919
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeGGGTTSGQILFNGQPRKpDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 VQQQDLHLHTSTVREALEFSALLRQPPQYTREEKldyvEKVLDLLNMRDYADAIVGIPG-EGLNVEQRKRLTIGVELAAR 998
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 999 PKLLlFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKGGKtVYFG 1065
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
163-702 |
9.61e-50 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 188.94 E-value: 9.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVDPAAYINYHGITPKQMS-TDFrgeaiyTAEVDAHYPQLS 241
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKrTGF------VTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTLYFASLARAPRHLpggisSQEYATHLRDVIMAMFGIGHTINTRVGNDFVRGVSGGERKRVTIAEAALSYAPLQCWD 321
Cdd:PLN03211 157 VRETLVFCSLLRLPKSL-----TKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 322 NSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAKAYFERLGFLCPESQT 401
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 402 TADFLTSMSSpteriirpGFESLAPRTSEEfakhwkESNERQSLLRQIDQYANEHPFDGDDLDRFAQSRK----TEKSKN 477
Cdd:PLN03211 311 PADFLLDLAN--------GVCQTDGVSERE------KPNVKQSLVASYNTLLAPKVKAAIEMSHFPQANArfvgSASTKE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 478 QRQKSPYTLSYW-GQIRLCMWRELQRLKNDPSVTIVMLinnffeALIISSIFYNLSGNTSSFFS----RGAILFMMVLLN 552
Cdd:PLN03211 377 HRSSDRISISTWfNQFSILLQRSLKERKHESFNTLRVF------QVIAAALLAGLMWWHSDFRDvqdrLGLLFFISIFWG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 553 AFSSMLEILSLYAKRTIVEKHNRYALYHPSAEAISSMIMDMPYK-IVNSILMNLTlYFMANLRREPGPFFFNYLISFMMV 631
Cdd:PLN03211 451 VFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMElILPTIFLTVT-YWMAGLKPELGAFLLTLLVLLGYV 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 632 MSMSMFFRLFASLTKTIQQALAPSSIILMALVLYTGFAipVSYMRGWASWIRYLNPVAYGFEaIMVNEFHG 702
Cdd:PLN03211 530 LVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFY--VHKLPSCMAWIKYISTTFYSYR-LLINVQYG 597
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
495-698 |
1.32e-41 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 152.04 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 495 CMWRELQRLKNDPSVTIVMLINNFFEALIISSIFYNLsGNTSSFFSRGAILFMMVLLNAFSSMLEILSLYAK-RTIVEKH 573
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL-GNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKeRGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 574 NRYALYHPSAEAISSMIMDMPYKIVNSILMNLTLYFMANLRREPGPFFFNYLISFMMVMSMSMFFRLFASLTKTIQQALA 653
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799732068 654 PSSIILMALVLYTGFAIPVSYMRGWASWIRYLNPVAYGFEAIMVN 698
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
711-802 |
3.96e-40 |
|
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: 143.37 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 711 VPSGVGYENISKDEHICSVVGSIPGSDLVDGTAFVKSTYGYENSHRWRNFGIILALTVFLALCQLIATELVASERSKGEV 790
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
90
....*....|..
gi 1799732068 791 LVFRRGSSQKAR 802
Cdd:pfam06422 81 LVFKRGKAPKLK 92
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
848-1099 |
9.72e-39 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 155.42 E-value: 9.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGRPRDSSFQRKTGYVQQQDLHL 927
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPG-EGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLI-LD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1007 EPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKgGKTVYFGDiGRESrilMDYFTRNG-GPA 1085
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGK-GSDA---MAYFESVGfSPS 306
|
250
....*....|....
gi 1799732068 1086 LPpgSNPAEHMLEV 1099
Cdd:PLN03211 307 FP--MNPADFLLDL 318
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1168-1376 |
2.05e-37 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 140.10 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1168 RVFQQYWRTPAYIYSKVLLTIGCSLFIGFSFFKADNTAQGLQNQMFGVFVFLFVVIQLIIQIIPSFVTQRTLYEaRERQS 1247
Cdd:pfam01061 4 REFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RELAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1248 KTYSWQAFVVTNILVELAWNSIMAIFCFLVWFYPVGLFHNAeytdtlhSRSTLAFLFIWVTFLFASSLAHMLIAGIESEE 1327
Cdd:pfam01061 83 PLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSA-------GRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799732068 1328 IASSLSNILAIMMYAFCGILAGPGALPGFWIFMYRVNPFTYLVSGLLST 1376
Cdd:pfam01061 156 DASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
837-1065 |
3.75e-37 |
|
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: 139.32 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 837 TSIFHWENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGV-VGGDMLVDGRPRD---SS 912
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPYKefaEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 FQRKTGYVQQQDLHLHTSTVREALEFSALLRqppqytreekldyvekvldllnmrdyADAIVgipgEGLNVEQRKRLTIG 992
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCK--------------------------GNEFV----RGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 993 VELAARPKLLLFlDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSAMLFQRFDRLLLLAkGGKTVYFG 1065
Cdd:cd03233 131 EALVSRASVLCW-DNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLY-EGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
163-380 |
1.46e-33 |
|
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: 128.44 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVDPAAYINYHGITPKQmstdFRGEAIYTAEVDAHYPQLSV 242
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRS----FRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 GDTLYFASLaraprhlpggissqeyathlrdvimamfgightintrvgndfVRGVSGGERKRVTIAEAALSYAPLQCWDN 322
Cdd:cd03213 100 RETLMFAAK------------------------------------------LRGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 323 STRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
843-1058 |
3.74e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 122.19 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKikSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVVG---GDMLVDGRPRDSS----FQR 915
Cdd:cd03225 3 KNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN-----GLLGptsGEVLVDGKDLTKLslkeLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYV-QQQDLHLHTSTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVE 994
Cdd:cd03225 76 KVGLVfQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEER---VEEALELVGLEGLRDR----SPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 995 LAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKG 1058
Cdd:cd03225 149 LAMDPDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
856-1078 |
5.30e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.78 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRP---RDSSFQRKTGYVQQQDLHLHT 929
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL-----GLLrptSGEVRVLGEDvarDPAEVRRRIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLlFLDEPT 1009
Cdd:COG1131 88 LTVRENLRFFARLYGLPRKEARER---IDELLELFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELL-ILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMlFQRFDRLLLLAKgGKTVYFGDIgRE--SRILMDYF 1078
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEA-ERLCDRVAIIDK-GRIVADGTP-DElkARLLEDVF 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
155-771 |
3.47e-29 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 127.27 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 155 GGKKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVDPAAYINyhGITPKQMStdFRGEAIYTAEVD 234
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRIS--GFPKKQET--FARISGYCEQND 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 235 AHYPQLSVGDTLYFASLARAPRHLpggisSQEYATHLRDVIMAMFGIGHTINTRVGNDFVRGVSGGERKRVTIAEAALSY 314
Cdd:PLN03140 963 IHSPQVTVRESLIYSAFLRLPKEV-----SKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 315 APLQCWDNSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQ-IYFGA----AHDAKAYF 389
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSIDIFEAFDELLLMKRGGQvIYSGPlgrnSHKIIEYF 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 390 ERLGFL--CPESQTTADFLTSMSSPTERIirpgfeslapRTSEEFAKHWKESNERQ---SLLRQIdqyaNEHPFDGDDLd 464
Cdd:PLN03140 1117 EAIPGVpkIKEKYNPATWMLEVSSLAAEV----------KLGIDFAEHYKSSSLYQrnkALVKEL----STPPPGASDL- 1181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 465 RFAqsrkteksknqrqkSPYTLSYWGQIRLCMWRELQRLKNDPSVTIVMLINNFFEALIISSIFYNLSGNTSSFFSRGAI 544
Cdd:PLN03140 1182 YFA--------------TQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMV 1247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 545 LFMM------VLLNAFSSMLEILSLyaKRTIVEKHNRYALYHPSAEAISSMIMDMPYKIVNSILMNLTLYFMANLRREPG 618
Cdd:PLN03140 1248 IGAMyaavlfVGINNCSTVQPMVAV--ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAA 1325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 619 PFFFNYLISFMMVMSMSMFFRLFASLTKTIQQALAPSSIILMALVLYTGFAIPVSYMRGWASWIRYLNPVAYGFEAIMVN 698
Cdd:PLN03140 1326 KFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVS 1405
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 699 EFHgrtfpcasfvpsgvgyenisKDEHICSVVGSIPGSDLVDgtaFVKSTYGYENSHRWRNFGIILALTVFLA 771
Cdd:PLN03140 1406 QYG--------------------DVEDTIKVPGGAPDPTIKW---YIQDHYGYDPDFMGPVAAVLVGFTVFFA 1455
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
843-1058 |
5.13e-28 |
|
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: 113.35 E-value: 5.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTvgvvGGDMLVDGRP-------RDSSF 913
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVRVDGTDisklsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 914 QRKT-GYVQQQDLHLHTSTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIG 992
Cdd:cd03255 80 RRRHiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRER---AEELLERVGLGDRLNH---YPSE-LSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 993 VELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSamLFQRFDRLLLLAKG 1058
Cdd:cd03255 153 RALANDPKIIL-ADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
856-1066 |
5.87e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDSSfQRKTGYVQQQ---DLHLHT 929
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLL-----KAILGLLpptSGTVRLFGKPPRRA-RRRIGYVPQRaevDWDFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 sTVRE--ALEFSALLRQPPQYTREEKlDYVEKVLDLLNMRDYADAIVGipgeglnvE----QRKRLTIGVELAARPKLLL 1003
Cdd:COG1121 93 -TVRDvvLMGRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIG--------ElsggQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1004 fLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLfQRFDRLLLLAKGgkTVYFGD 1066
Cdd:COG1121 163 -LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVR-EYFDRVLLLNRG--LVAHGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
843-1077 |
7.11e-28 |
|
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: 113.20 E-value: 7.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVkikSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPRD----SSFQR 915
Cdd:COG1122 4 ENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-----GLLkptSGEVLVDGKDITkknlRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYV-QQQDLHLHTSTVREALEFSaLLRQppQYTREEKLDYVEKVLDLLNMRDYADAIV-----GipgeglnveQRKRL 989
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEDVAFG-PENL--GLPREEIRERVEEALELVGLEHLADRPPhelsgG---------QKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 990 TI-GVeLAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKgGKTVYFGDIg 1068
Cdd:COG1122 144 AIaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD-GRIVADGTP- 218
|
....*....
gi 1799732068 1069 REsrILMDY 1077
Cdd:COG1122 219 RE--VFSDY 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
856-1068 |
8.50e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 113.41 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVvgGDMLVDGRP---RDSSFQRKTGYVQQQD-LHLHTsT 931
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDvrkEPREARRQIGVLPDERgLYDRL-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEPTSG 1011
Cdd:COG4555 91 VRENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLL-LDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 1012 LDSQTSWSICNLMETLTKNGQAILCTIHQPS--AMLfqrFDRLLLLAKgGKTVYFGDIG 1068
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQevEAL---CDRVVILHK-GKVVAQGSLD 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
163-380 |
2.56e-25 |
|
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: 105.82 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGF-----QVdpaaYINYHGITPKQmstdFRGEAIYTAEVDAHY 237
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsgQI----LFNGQPRKPDQ----FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 238 PQLSVGDTLYFASLARAPRHLPGGISSQEYAThlrdvimamFGIGHTINTRVGNDFVRGVSGGERKRVTIAEAALSYAPL 317
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRVED---------VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 318 QCWDNSTRGLDSANAVEFCRTLRtQSDVFGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLS-QLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
859-1010 |
8.93e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.57 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGRP----RDSSFQRKTGYVQQQDLHLHTSTVRE 934
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDltddERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 935 ALEFSALLRQPpqyTREEKLDYVEKVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTS 1010
Cdd:pfam00005 79 NLRLGLLLKGL---SKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
843-1058 |
1.35e-24 |
|
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: 103.11 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKiksETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTVGVVggdmLVDGRPRDSSFQRKT-GY 919
Cdd:cd03226 3 ENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAglIKESSGSI----LLNGKPIKAKERRKSiGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 VQQQ-DLHLHTSTVREALefsaLLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGIPGEGlnveQRKRLTIGVELAAR 998
Cdd:cd03226 76 VMQDvDYQLFTDSVREEL----LLGLKELDAGNEQ---AETVLKDLDLYALKERHPLSLSGG----QKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 999 PKLLLFlDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKG 1058
Cdd:cd03226 145 KDLLIF-DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE-FLAKVCDRVLLLANG 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
843-1058 |
4.31e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.43 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRP------RD-SS 912
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-----GLDrptSGEVLIDGQDisslseRElAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 FQRKT-GYVQQQdLHLH-TSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLT 990
Cdd:COG1136 83 LRRRHiGFVFQF-FNLLpELTALENVALPLLLAGVS---RKERRERARELLERVGLGDRLDH---RPSQ-LSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 991 IGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSAMlfQRFDRLLLLAKG 1058
Cdd:COG1136 155 IARALVNRPKLIL-ADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA--ARADRVIRLRDG 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
848-1067 |
7.45e-23 |
|
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: 99.11 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDS-------SFQRKT 917
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLL-----RLIVGLLrpdSGEVLIDGEDISGlseaelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 918 GYVQQQDLhLHTS-TVREALEFsaLLRQPPQYTREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELA 996
Cdd:cd03261 80 GMLFQSGA-LFDSlTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAE-LSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 997 ARPKlLLFLDEPTSGLDSQTSWSICNLMETLTK--NGQAILCTiHQPSAmLFQRFDRLLLLAkGGKTVYFGDI 1067
Cdd:cd03261 153 LDPE-LLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVT-HDLDT-AFAIADRIAVLY-DGKIVAEGTP 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
852-1039 |
7.99e-23 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 98.35 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 852 KSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGRPRDSSF---QRKTGYVQQQDLHLH 928
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR--PTSGTAYINGYSIRTDRkaaRQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TSTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKlLLFLDEP 1008
Cdd:cd03263 89 ELTVREHLRFYARLKGLPKSEIKEE---VELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPS-VLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNgQAILCTIH 1039
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKG-RSIILTTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
856-1056 |
9.65e-23 |
|
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: 97.93 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGRP---RDSSFQRKTGYVQQQDlHLHTS-T 931
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEPirdAREDYRRRLAYLGHAD-GLKPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSALLRQPPQyTREEkldyVEKVLDLLNMRDYADaivgIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSG 1011
Cdd:COG4133 92 VRENLRFWAALYGLRA-DREA----IDEALEAVGLAGLAD----LPVRQLSAGQKRRVALARLLLSPAPLWL-LDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799732068 1012 LDSQTSWSICNLMETLTKNGQAILCTIHQPsamLFQRFDRLLLLA 1056
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLG 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
848-1058 |
1.77e-22 |
|
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: 103.68 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRR-ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRttVGVVGGDMLVDGRPRDS----SFQRKTGYVQQ 922
Cdd:COG4988 341 DVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF--LPPYSGSILINGVDLSDldpaSWRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 QDlHLHTSTVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVEL 995
Cdd:COG4988 419 NP-YLFAGTIRENLRLGR-----PDASDEE----LEAALEAAGLDEFVaalpdglDTPLGEGGRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 996 AARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:COG4988 489 LRDAPLLL-LDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLALL--AQADRILVLDDG 547
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
856-1029 |
7.44e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 96.20 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDS-------SFQRKTGYVQQQ-- 923
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLL-----KLIIGLLrpdSGEILVDGQDITGlsekelyELRRRIGMLFQGga 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 ---DLhlhtsTVREALEFSalLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIvgiPGE---GlnveQRKRltigVELA- 996
Cdd:COG1127 93 lfdSL-----TVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADKM---PSElsgG----MRKR----VALAr 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1799732068 997 ---ARPKLLlFLDEPTSGLDSQTSWSICNLMETLTK 1029
Cdd:COG1127 155 alaLDPEIL-LYDEPTAGLDPITSAVIDELIRELRD 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
868-1058 |
9.11e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 95.05 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 868 PGTLTALMGSSGAGKTTLLDVLAN--RTTVG--VVGGDMLVDGRPRD--SSFQRKTGYV-QQQDLHLHTsTVREALEFSA 940
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGtiVLNGTVLFDSRKKInlPPQQRKIGLVfQQYALFPHL-NVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 941 llrqpPQYTREEKLDYVEKVLDLLNMrdyaDAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSI 1020
Cdd:cd03297 101 -----KRKRNREDRISVDELLDLLGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLL-LDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 1021 CNLMETLTK--NGQAILCTiHQPSAMlFQRFDRLLLLAKG 1058
Cdd:cd03297 171 LPELKQIKKnlNIPVIFVT-HDLSEA-EYLADRIVVMEDG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
856-1065 |
2.29e-21 |
|
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: 94.14 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTVGVVggdmLVDGRPRDSSfQRKTGYVQQQDLHLHTSTVR 933
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILglLKPTSGSI----RVFGKPLEKE-RKRIGYVPQRRSIDRDFPIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 eALEFSALLRQP-----PQYTREEKlDYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEP 1008
Cdd:cd03235 87 -VRDVVLMGLYGhkglfRRLSKADK-AKVDEALERVGLSELADRQIG----ELSGGQQQRVLLARALVQDPDLLL-LDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKGGktVYFG 1065
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRTV--VASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
856-1066 |
2.65e-21 |
|
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: 95.11 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRP------RDSSfqRKTGYVQQQdlh 926
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLkpsSGEVLLDGRDlaslsrRELA--RRIAYVPQE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 lHTS----TVREALEFSallRQPPQ--YTREEKLDY--VEKVLDLLNMRDYADAIV-----GipgeglnveQRKRLTIGV 993
Cdd:COG1120 84 -PPApfglTVRELVALG---RYPHLglFGRPSAEDReaVEEALERTGLEHLADRPVdelsgG---------ERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 994 ELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPS-AMLFqrFDRLLLLaKGGKTVYFGD 1066
Cdd:COG1120 151 ALAQEPPLLL-LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLL-KDGRIVAQGP 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
850-1065 |
6.78e-21 |
|
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: 92.82 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 850 KIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrTTVGVVGGDMLVDG-----RPRDSsfQRKTGYVQQQD 924
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA--GLLEPDAGFATVDGfdvvkEPAEA--RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 LHLHTSTVREALEFSALLRqppQYTREEKLDYVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLLLf 1004
Cdd:cd03266 88 GLYDRLTARENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDR----RVGGFSTGMRQKVAIARALVHDPPVLL- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1005 LDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH--QPSAMLfqrFDRLLLLAKgGKTVYFG 1065
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHR-GRVVYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
848-1058 |
2.14e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.61 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRDSSF----QRKTGYVQQq 923
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDGKDIAKLPleelRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 dlhlhtstvrealefsallrqppqytreekldyvekvldllnmrdyadaivgipgegLNVEQRKRLTIGVELAARPKLLL 1003
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 1004 fLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQrFDRLLLLAKG 1058
Cdd:cd00267 104 -LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDG 156
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
850-1065 |
2.53e-20 |
|
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: 91.86 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 850 KIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRT------TVGVVGGDMLVDGRPRDSSFQRKTGYVQQQ 923
Cdd:cd03256 8 KTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NGLveptsgSVLIDGTDINKLKGKALRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 dLHL-HTSTVREALEFSALLRQPP------QYTREEKLDYVEkVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELA 996
Cdd:cd03256 87 -FNLiERLSVLENVLSGRLGRRSTwrslfgLFPKEEKQRALA-ALERVGLLDKAYQRAD----QLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 997 ARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPS-AMLFqrFDRLLLLaKGGKTVYFG 1065
Cdd:cd03256 161 QQPKLIL-ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGL-KDGRIVFDG 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
857-1058 |
2.60e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 91.04 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGR------PRdssfQRKTGYVQQQDLHLHTS 930
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD--SGEILIDGRdvtgvpPE----RRNIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVgipgEGLNVEQRKRLTIGVELAARPKLLLfLDEPTS 1010
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRAR---VRELLELVGLEGLLNRYP----HELSGGQQQRVALARALAREPSLLL-LDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1011 GLDSQTSWSICNLMETLTKNGQ--AILCTIHQPSAMLFQrfDRLLLLAKG 1058
Cdd:cd03259 160 ALDAKLREELREELKELQRELGitTIYVTHDQEEALALA--DRIAVMNEG 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
856-1065 |
3.03e-20 |
|
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: 90.72 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGtLTALMGSSGAGKTTLLDVLAnrTTVGVVGGDMLVDGRP---RDSSFQRKTGYVQQQDLHLHTSTV 932
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA--TLTPPSSGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 933 REALEFSALLRQPPQyTREEKldYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGL 1012
Cdd:cd03264 90 REFLDYIAWLKGIPS-KEVKA--RVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILI-VDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1013 DSQTSWSICNLMETLTKNGQAILCTiHQPSAMLFQrFDRLLLLAKgGKTVYFG 1065
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILST-HIVEDVESL-CNQVAVLNK-GKLVFEG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
164-324 |
6.49e-20 |
|
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: 87.70 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 164 LQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHgfqvdPAA-YINYHGIT-PKQMSTDFRGEAIYTAEVDAHYPQLS 241
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-----PTEgTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTLYFASLaraPRHLPGGISSQEyathlRDVIMAMFGIGHTINTRVGNdFVRGVSGGERKRVTIAEAALSYAPLQCWD 321
Cdd:pfam00005 76 VRENLRLGLL---LKGLSKREKDAR-----AEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
...
gi 1799732068 322 NST 324
Cdd:pfam00005 147 EPT 149
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
855-1058 |
6.93e-20 |
|
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: 88.61 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDG---RPRDSSFQRKTGYVQQQDLHLH 928
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-----GLLkpdSGEIKVLGkdiKKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TSTVREALEFSAllrqppqytreekldyvekvldllnmrdyadaivgipgeGlnveQRKRLTIGVELAARPKLLlFLDEP 1008
Cdd:cd03230 87 NLTVRENLKLSG---------------------------------------G----MKQRLALAQALLHDPELL-ILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKG 1058
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
859-1035 |
9.61e-20 |
|
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: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP--RDSSFQRktgyVQQ------QDLHL-HT 929
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT--SGSVLFDGEDitGLPPHEI----ARLgigrtfQIPRLfPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSALLRQPPQY-------TREEKLDYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLL 1002
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG----ELSYGQQRRLEIARALATDPKLL 165
|
170 180 190
....*....|....*....|....*....|...
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKNGQAIL 1035
Cdd:cd03219 166 L-LDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
843-1035 |
1.52e-19 |
|
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: 89.07 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTvgvvGGDMLVDGRPRDSSfQRKTGYV 920
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAglERPT----SGEVLVDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 921 QQQDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGE---GlnveQRKRLTIGVELAA 997
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVP---KAEARERAEELLELVGLSGFENA---YPHQlsgG----MRQRVALARALAV 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICN-LMETLTKNGQAIL 1035
Cdd:cd03293 149 DPDVLL-LDEPFSALDALTREQLQEeLLDIWRETGKTVL 186
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
843-1058 |
3.08e-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: 86.67 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYdvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRP----RDSSFQRKTG 918
Cdd:cd03228 4 KNVSF--SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDlrdlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 YVqQQDLHLHTSTVREALeFSAllrqppqytreekldyvekvldllnmrdyadaivGipgeglnveQRKRLTIGVELAAR 998
Cdd:cd03228 80 YV-PQDPFLFSGTIRENI-LSG----------------------------------G---------QRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 999 PKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:cd03228 115 PPILI-LDEATSALDPETEALILEALRALAKGKTVIVIA-HRLSTI--RDADRIIVLDDG 170
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
59-142 |
7.35e-19 |
|
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: 82.37 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 59 NLARKLTTKSeklHHRSPFEAREGGCLDPNSPEFRARDWAKAFYNaRYNADENCPPRVAGVAFKDLNVSGYGSPVDYQMS 138
Cdd:pfam14510 1 ELARILTRQS---SSSSSSSSPESTDPDEEDSEFDLRKWLKNLRR-LIDEDGYIKPRKLGVAFKNLTVSGVGAGADYQPT 76
|
....
gi 1799732068 139 VGNA 142
Cdd:pfam14510 77 VGNA 80
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
854-1058 |
7.41e-19 |
|
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: 92.14 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 854 ETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRP----RDSSFQRKTGYVQQqDLHLHT 929
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSITLGGVDlrdlDEDDLRRRIAVVPQ-RPHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPKLL 1002
Cdd:COG4987 423 TTLRENLRLAR-----PDATDEE----LWAALERVGLGDWLaalpdglDTWLGEGGRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:COG4987 494 L-LDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAGL--ERMDRILVLEDG 545
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
859-1039 |
8.01e-19 |
|
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: 88.99 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVG---VVGGDMLVDGRprdsSFQRKTGYVQQQ-----DLhlh 928
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRPTSGtarVAGYDVVREPR----KVRRSIGIVPQYasvdeDL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 tsTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGIPGEGlnveQRKRLTIGVELAARPKLLlFLDEP 1008
Cdd:TIGR01188 82 --TGRENLEMMGRLYGLPKDEAEER---AEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDEP 151
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
858-1058 |
1.02e-18 |
|
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: 92.20 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvgvvG------GDMLVDGRPRD----SSFQRKTGYVqQQDLHL 927
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL--------GlyeptsGRILIDGIDLRqidpASLRRQIGVV-LQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPK 1000
Cdd:COG2274 561 FSGTIRENITLGD-----PDATDEE----IIEAARLAGLHDFIealpmgyDTVVGEGGSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799732068 1001 LLLfLDEPTSGLDSQTSWSICNLMETLTKNgqailCTI----HQPSAMlfQRFDRLLLLAKG 1058
Cdd:COG2274 632 ILI-LDEATSALDAETEAIILENLRRLLKG-----RTViiiaHRLSTI--RLADRIIVLDKG 685
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
843-1027 |
1.93e-18 |
|
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: 90.73 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVC--YDVKiKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRP-------RD 910
Cdd:COG1123 264 RNLSkrYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLA-----RLLLGLLrptSGSILFDGKDltklsrrSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 911 SSFQRKTGYVQQQDLH--LHTSTVREALEFSalLRQPPQYTREEKLDYVEKVLDLLNM-RDYADAivgIPGE---Glnve 984
Cdd:COG1123 338 RELRRRVQMVFQDPYSslNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLpPDLADR---YPHElsgG---- 408
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1799732068 985 QRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETL 1027
Cdd:COG1123 409 QRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDL 450
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
848-1058 |
2.06e-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: 86.00 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVL-----ANRTTVGVVGGDM-LVDgrprDSSFQRKTGYVQ 921
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvPENGRVLVDGHDLaLAD----PAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 922 QQDLhLHTSTVREALefsALLRQPPQYtreEKLDYVEKVLD----LLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAA 997
Cdd:cd03252 83 QENV-LFNRSIRDNI---ALADPGMSM---ERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 998 RPKLLLFlDEPTSGLDSQTSWSICNLMETLTKnGQAILCTIHQPSAMlfQRFDRLLLLAKG 1058
Cdd:cd03252 156 NPRILIF-DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
843-1059 |
2.75e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 85.75 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYdvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRP-RD---SSFQRKTG 918
Cdd:cd03251 4 KNVTF--RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPR--FYDVDSGRILIDGHDvRDytlASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 YVqQQDLHLHTSTVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTI 991
Cdd:cd03251 80 LV-SQDVFLFNDTVAENIAYGR-----PGATREE----VEEAARAANAHEFImelpegyDTVIGERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 992 GVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAI-----LCTIhqpsamlfQRFDRLLLLAKGG 1059
Cdd:cd03251 150 ARALLKDPPILI-LDEATSALDTESERLVQAALERLMKNRTTFviahrLSTI--------ENADRIVVLEDGK 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
843-1058 |
3.80e-18 |
|
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: 85.63 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTvgvvGGDMLVDGRP----RDSSFQRK 916
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPW----SGEVTFDGRPvtrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 917 TGYVQQQ---DLH-LHTstVREAL-EFSALLRQPPQYTReekldyVEKVLDLlnmrdyadaiVGIPGE-----------G 980
Cdd:COG1124 81 VQMVFQDpyaSLHpRHT--VDRILaEPLRIHGLPDREER------IAELLEQ----------VGLPPSfldryphqlsgG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 981 lnveQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTK-NGQAILCTIHQPSAMlfQRF-DRLLLLAKG 1058
Cdd:COG1124 143 ----QRQRVAIARALILEPELLL-LDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVV--AHLcDRVAVMQNG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
849-1058 |
3.97e-18 |
|
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: 89.58 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 849 VKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRT-TVGVVGGDMLVDGRP-RDSSFQ---RKTGYV-QQ 922
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDlLELSEAlrgRRIGMVfQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 QDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLL 1002
Cdd:COG1123 92 PMTQLNPVTVGDQIAEALENLGLS---RAEARARVLELLEAVGLERRLDR---YPHQ-LSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSAMLfQRFDRLLLLAKG 1058
Cdd:COG1123 165 I-ADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVA-EIADRVVVMDDG 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
856-1065 |
6.20e-18 |
|
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: 83.25 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPrdssfqrktgyvqqqdlhlhtstvrea 935
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG--LLKPSSGEILLDGKD--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 936 lefsalLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIV-----GipgeglnveQRKRLTIGVELAARPKLLLfLDEPTS 1010
Cdd:cd03214 63 ------LASLSPKELARKIAYVPQALELLGLAHLADRPFnelsgG---------ERQRVLLARALAQEPPILL-LDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 1011 GLDSQTSWSICNLMETLTK-NGQAILCTIHQPS-AMLFqrFDRLLLLaKGGKTVYFG 1065
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNlAARY--ADRVILL-KDGRIVAQG 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
855-1063 |
1.35e-17 |
|
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: 83.10 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDSSFQRKTGYV-QQQDLHLHTs 930
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTI-----RMILGIIlpdSGEVLFDGKPLDIAARNRIGYLpEERGLYPKM- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSALLR-QPPQYTREEKLDYVEKvldlLNMRDYADAIVgipgEGLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:cd03269 86 KVIDQLVYLAQLKgLKKEEARRRIDEWLER----LELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLI-LDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTIHQpsaM-LFQRF-DRLLLLAKGGKTVY 1063
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQ---MeLVEELcDRVLLLNKGRAVLY 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
857-1039 |
1.44e-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: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrTTVGVVGGDMLVDG-----RPRDssFQRKTGYVQQQ---DLHLh 928
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLT--TLLKPTSGRATVAGhdvvrEPRE--VRRRIGIVFQDlsvDDEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 tsTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIVGIPGEGLnveqRKRLTIGVELAARPKLLlFLDEP 1008
Cdd:cd03265 89 --TGWENLYIHARLYGVPGAERRER---IDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTK-NGQAILCTIH 1039
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEeFGMTILLTTH 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
857-1015 |
1.70e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 83.93 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRP---------------RdsSFQrktg 918
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYrptSGRILFDGRDitglpphriarlgiaR--TFQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 yvqqqdlhlHTS-----TVREALE-----------FSALLRqPPQYTREEK--LDYVEKVLDLLNMRDYADAIVGipgeG 980
Cdd:COG0411 87 ---------NPRlfpelTVLENVLvaaharlgrglLAALLR-LPRARREEReaRERAEELLERVGLADRADEPAG----N 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1799732068 981 LNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQ 1015
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLL-LDEPAAGLNPE 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
848-1067 |
1.71e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.60 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDgW-IKPGTLTALMGSSGAGKTTLLDVLANR---TTvgvvGGDMLVDGRPRD--SSFQ--RKTGY 919
Cdd:COG1119 8 NVTVRRGGKTILDDIS-WtVKPGEHWAILGPNGAGKSTLLSLITGDlppTY----GNDVRLFGERRGgeDVWElrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 V---QQQDLHLHTsTVREALE--FSALLRQPPQYTREEKlDYVEKVLDLLNMRDYADAIVGIPGEGlnveQRKRLTIGVE 994
Cdd:COG1119 83 VspaLQLRFPRDE-TVLDVVLsgFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFGTLSQG----EQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 995 LAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNG--QAILCTiHQPSAMLfQRFDRLLLLaKGGKTVYFGDI 1067
Cdd:COG1119 157 LVKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEEIP-PGITHVLLL-KDGRVVAAGPK 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
859-1039 |
1.77e-17 |
|
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: 82.84 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVgvVGGDMLVDGRP----RDSS---FQRKTGYVQQQDLHLHTST 931
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP--TSGTIRVNGQDvsdlRGRAipyLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSALLRQ-PPQYTREEkldyVEKVLDLLNMRDYADAIvgipGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTS 1010
Cdd:cd03292 95 VYENVAFALEVTGvPPREIRKR----VPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILI-ADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1799732068 1011 GLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
858-1058 |
2.22e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.58 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRDSS------FQRKTGYV-QQQDLHLHts 930
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGLKLTDDkknineLRQKVGMVfQQFNLFPH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 tvREALEFSAL-----LRQPPQYTREEKLDYVEKVldllNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLFl 1005
Cdd:cd03262 91 --LTVLENITLapikvKGMSKAEAEERALELLEKV----GLADKADA---YPAQ-LSGGQQQRVAIARALAMNPKVMLF- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 1006 DEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQpsaMLFQR--FDRLLLLAKG 1058
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE---MGFARevADRVIFMDDG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
857-1039 |
2.26e-17 |
|
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: 81.70 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPRDSS------FQRKTGYV-QQQDLHLHT 929
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNG--LLRPQSGAVLIDGEPLDYSrkglleRRQRVGLVfQDPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSAL-LRQPPQYTREEkldyVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLLLfLDEP 1008
Cdd:TIGR01166 84 ADVDQDVAFGPLnLGLSEAEVERR----VREALTAVGASGLRER----PTHCLSGGEKKRVAIAGAVAMRPDVLL-LDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
848-1040 |
2.54e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 82.61 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLL-------DVLANRTTVGVV--GGDMLVDGRPRDSSFQRKTG 918
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPDEGEVllDGKDIYDLDVDVLELRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 YVQQQDLHLHTStVREALEFSALLRqppQYTREEKLDY-VEKVLDLLNMRDYADAIVGipGEGLNVEQRKRLTIGVELAA 997
Cdd:cd03260 85 MVFQKPNPFPGS-IYDNVAYGLRLH---GIKLKEELDErVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCT--IHQ 1040
Cdd:cd03260 159 EPEVLL-LDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
855-1063 |
4.91e-17 |
|
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: 81.49 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGrprdSSFQRKTGYVQQ-------QD 924
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTM-----KIILGLIkpdSGEITFDG----KSYQKNIEALRRigalieaPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 LHLHTsTVREALEFSALLRQppqyTREEKldyVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLf 1004
Cdd:cd03268 83 FYPNL-TARENLRLLARLLG----IRKKR---IDEVLDVVGLKDSAKKKVK----GFSLGMKQRLGIALALLGNPDLLI- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 1005 LDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLfQRFDRLLLLAKgGKTVY 1063
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQ-KVADRIGIINK-GKLIE 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
843-1016 |
5.33e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.44 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPRDSSfQRKTGY 919
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA-----GLEkptSGEVLVDGKPVTGP-GPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 VQQQDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGE---GlnveQRKRLTIGVELA 996
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVP---KAERRERARELLELVGLAGFEDA---YPHQlsgG----MRQRVAIARALA 154
|
170 180
....*....|....*....|
gi 1799732068 997 ARPKLLLfLDEPTSGLDSQT 1016
Cdd:COG1116 155 NDPEVLL-MDEPFGALDALT 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
843-1016 |
1.22e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.22 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVC--YDvkiksETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvG---VVGGDMLVDGRP-RD---SSF 913
Cdd:COG1132 343 ENVSfsYP-----GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL-----RfydPTSGRILIDGVDiRDltlESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 914 QRKTGYVqQQDLHLHTSTVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQR 986
Cdd:COG1132 413 RRQIGVV-PQDTFLFSGTIRENIRYGR-----PDATDEE----VEEAAKAAQAHEFIealpdgyDTVVGERGVNLSGGQR 482
|
170 180 190
....*....|....*....|....*....|
gi 1799732068 987 KRLTIGVELAARPKLLLfLDEPTSGLDSQT 1016
Cdd:COG1132 483 QRIAIARALLKDPPILI-LDEATSALDTET 511
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
850-1065 |
8.91e-16 |
|
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: 78.32 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 850 KIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVG---VVGGDMLVDGRP-------RDSSFQRKTGY 919
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLA-----RAILGllkPTSGSIIFDGKDllklsrrLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 V-QQQDLHLH-TSTVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAA 997
Cdd:cd03257 87 VfQDPMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNR---YPHE-LSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICNLMETL-TKNGQAILCTIHQPSAMlfQRF-DRLLLLaKGGKTVYFG 1065
Cdd:cd03257 163 NPKLLI-ADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVV--AKIaDRVAVM-YAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
843-1058 |
1.92e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.01 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCydvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLL-----DVLANRTTVGVVGGDmLVDGRPRDSSF-QRK 916
Cdd:COG2884 5 ENVS---KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLkllygEERPTSGQVLVNGQD-LSRLKRREIPYlRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 917 TGYVqQQDLHLHTS-TVREALEFsAL--LRQPPQYTREEkldyVEKVLDLLNMRDYADAivgIPGE---GlnvEQrKRLT 990
Cdd:COG2884 81 IGVV-FQDFRLLPDrTVYENVAL-PLrvTGKSRKEIRRR----VREVLDLVGLSDKAKA---LPHElsgG---EQ-QRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 991 IGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSamLFQRFD-RLLLLAKG 1058
Cdd:COG2884 148 IARALVNRPELLL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
857-1015 |
2.33e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 77.38 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTVGVV--GGDMLVDGRPRDssfqRKTGYV-QQQDLHLHTsT 931
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPDSGTIlfGGEDATDVPVQE----RNVGFVfQHYALFRHM-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSalLRQPPQYTREEKLDYVEKVLDLLNM---RDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLfLDEP 1008
Cdd:cd03296 91 VFDNVAFG--LRVKPRSERPPEAEIRAKVHELLKLvqlDWLADR---YPAQ-LSGGQRQRVALARALAVEPKVLL-LDEP 163
|
....*..
gi 1799732068 1009 TSGLDSQ 1015
Cdd:cd03296 164 FGALDAK 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
859-1040 |
2.43e-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: 77.24 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLL---DVLANRTTvgvvgGDMLVDGRPRDS-------SFQRKTGYVQQQdLHLH 928
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLERPTS-----GSVLVDGTDLTLlsgkelrKARRRIGMIFQH-FNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TS-TVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:cd03258 95 SSrTVFENVALPLEIAGVPKAEIEER---VLELLELVGLEDKADA---YPAQ-LSGGQKQRVGIARALANNPKVLL-CDE 166
|
170 180 190
....*....|....*....|....*....|....
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQ 1040
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRElGLTIVLITHE 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
854-1058 |
2.59e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 76.88 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 854 ETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRtTVGVVGGDMLVDGRP-RD---SSFQRKTGYVqQQDLHLHT 929
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MR-FYDPQKGQILIDGIDiRDisrKSLRSMIGVV-LQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSAllrqppQYTREEKldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPKLL 1002
Cdd:cd03254 91 GTIMENIRLGR------PNATDEE---VIEAAKEAGAHDFImklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:cd03254 162 I-LDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTI--KNADKILVLDDG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
856-1058 |
2.72e-15 |
|
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: 75.30 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDS------SFQRKTGYVQQQDLH 926
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLL-----RCIAGLEepdSGSILIDGEDLTDledelpPLRRRIGMVFQDFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 LHTSTVREALEFsallrqppqytreekldyvekvldllnmrdyadaivgipgeGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:cd03229 88 FPHLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVLL-LD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 1007 EPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQpsaMLF-QRF-DRLLLLAKG 1058
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHD---LDEaARLaDRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
857-1013 |
2.86e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.99 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRP--RDSSFQRKTGYVQQQDL---HLh 928
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA-----GFEtpdSGRILLDGRDvtGLPPEKRNVGMVFQDYAlfpHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 tsTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGE--GlnvEQRKRltigVELA----ARPKLL 1002
Cdd:COG3842 93 --TVAENVAFGLRMRGVPKAEIRAR---VAELLELVGLEGLADR---YPHQlsG---GQQQR----VALAralaPEPRVL 157
|
170
....*....|.
gi 1799732068 1003 LfLDEPTSGLD 1013
Cdd:COG3842 158 L-LDEPLSALD 167
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
857-1041 |
6.42e-15 |
|
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: 79.71 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPRDSSFQ---RKTGYVQQQDLHLHTS 930
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-----GLLdplQGEVTLDGVPVSSLDQdevRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSAllrqpPQYTREEKLDYVEKV--LDLL-NMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:TIGR02868 424 TVRENLRLAR-----PDATDEELWAALERVglADWLrALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL-LDE 497
|
170 180 190
....*....|....*....|....*....|....*.
gi 1799732068 1008 PTSGLDSQTSWSicnLMETL--TKNGQAILCTIHQP 1041
Cdd:TIGR02868 498 PTEHLDAETADE---LLEDLlaALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
855-1055 |
6.97e-15 |
|
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: 79.64 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRD----SSFQRKTGYVQQQDlHLHTS 930
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVPLAdadaDSWRDQIAWVPQHP-FLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALefsaLLRQPPQyTREEKLDYVEKV--LDLLN-MRDYADAIVGIPGEGLNVEQRKRLTIGVELaARPKLLLFLDE 1007
Cdd:TIGR02857 411 TIAENI----RLARPDA-SDAEIREALERAglDEFVAaLPQGLDTPIGEGGAGLSGGQAQRLALARAF-LRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMLfqRFDRLLLL 1055
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGRTVLLVT-HRLALAA--LADRIVVL 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
872-1015 |
8.49e-15 |
|
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: 77.83 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 872 TALMGSSGAGKTTLLDVLA--NRTTVG--VVGGDMLVDGRPRdsSF----QRKTGYVQQQDL---HLhtsTVREALEFSa 940
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAglERPDSGriRLGGEVLQDSARG--IFlpphRRRIGYVFQEARlfpHL---SVRGNLLYG- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 941 lLRQPPQYTREEKLDYVEKVL---DLLNMRdyADAIVGipGEglnveqRKRLTIGVELAARPKLLLfLDEPTSGLDSQ 1015
Cdd:COG4148 102 -RKRAPRAERRISFDEVVELLgigHLLDRR--PATLSG--GE------RQRVAIGRALLSSPRLLL-MDEPLAALDLA 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
858-1062 |
9.47e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRTTVgVVGGDMLVDG------RPRDSSFQRKTGYV-QQQDLHLHTS 930
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEE-ITSGDLIVDGlkvndpKVDERLIRQEAGMVfQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 tvreALEFSALlrQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPGEgLNVEQRKRLTIGVELAARPKLLLFlDEPTS 1010
Cdd:PRK09493 94 ----ALENVMF--GPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLMLF-DEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 1011 GLDSQTSWSICNLMETLTKNGQAILCTIHQpsaMLFQR--FDRLLLLAKGGKTV 1062
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHE---IGFAEkvASRLIFIDKGRIAE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
858-1066 |
1.12e-14 |
|
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: 74.78 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRP--RDSSFQR---KTGYVQQQDLHLHT 929
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLL-----KTIMGLLpprSGSIRFDGRDitGLPPHERaraGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSALLRQPPQYTREekldyVEKVLD----LLNMRDYadaivgiPGEGLNVEQRKRLTIGVELAARPKLLLfL 1005
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKAR-----LERVYElfprLKERRKQ-------LAGTLSGGEQQMLAIARALMSRPKLLL-L 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1006 DEPTSGLDSQTSWSICNLMETLTKNGQAILcTIHQPSAMLFQRFDRLLLLAKgGKTVYFGD 1066
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLER-GRVVLEGT 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
855-1039 |
1.96e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 74.50 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGR-----PRDSSFQRKTGYVQQQ--- 923
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTF-----YMIVGLVkpdSGKILLDGQditklPMHKRARLGIGYLPQEasi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 --DLhlhtsTVRE----ALEFSALLRQppqyTREEKLDYVEKVLDLLNMRD-YADAIVGipGEglnveqRKRLTIGVELA 996
Cdd:cd03218 87 frKL-----TVEEnilaVLEIRGLSKK----EREEKLEELLEEFHITHLRKsKASSLSG--GE------RRRVEIARALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1799732068 997 ARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:cd03218 150 TNPKFLL-LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
857-1013 |
4.96e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvG---VVGGDMLVDGR------PRDssfqRKTGYV-QQQDL- 925
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIA-----GledPTSGEILIGGRdvtdlpPKD----RNIAMVfQSYALy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 926 -HLhtsTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGE---GlnveQRKRLTIGVELAARPKL 1001
Cdd:COG3839 88 pHM---TVYENIAFPLKLRKVPKAEIDRR---VREAAELLGLEDLLDR---KPKQlsgG----QRQRVALGRALVREPKV 154
|
170
....*....|..
gi 1799732068 1002 LLFlDEPTSGLD 1013
Cdd:COG3839 155 FLL-DEPLSNLD 165
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
856-1065 |
5.54e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.61 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRDS------SFQRKtgyVQQQDLHLHT 929
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS--SGEVRLNGRPLAAwspwelARRRA---VLPQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 S-TVREALefsALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIV----GipGEglnvEQRkrltigVELA-------- 996
Cdd:COG4559 89 PfTVEEVV---ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYqtlsG--GE----QQR------VQLArvlaqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 997 ---ARPKLLlFLDEPTSGLDsqtswsIC---NLME---TLTKNGQAILCTIHQPS-AMLFQrfDRLLLLaKGGKTVYFG 1065
Cdd:COG4559 154 pvdGGPRWL-FLDEPTSALD------LAhqhAVLRlarQLARRGGGVVAVLHDLNlAAQYA--DRILLL-HQGRLVAQG 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
843-1058 |
6.95e-14 |
|
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: 71.09 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYdvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGV---VGGDMLVDGRP----RDSSFQR 915
Cdd:cd03246 4 ENVSF--RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL-----GLlrpTSGRVRLDGADisqwDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYVQQQDLhLHTSTVREALeFSAllrqppqytreekldyvekvldllnmrdyadaivgipgeGlnveQRKRLTIGVEL 995
Cdd:cd03246 77 HVGYLPQDDE-LFSGSIAENI-LSG---------------------------------------G----QRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 996 AARPKLLlFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSamLFQRFDRLLLLAKG 1058
Cdd:cd03246 112 YGNPRIL-VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
857-1015 |
8.25e-14 |
|
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: 72.65 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP--RDSSFQRKTGYV-QQQDLHLHTsTVR 933
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGKDitNLPPHKRPVNTVfQNYALFPHL-TVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:cd03300 91 ENIAFGLRLKKLPKAEIKER---VAEALDLVQLEGYANR---KPSQ-LSGGQQQRVAIARALVNEPKVLL-LDEPLGALD 162
|
..
gi 1799732068 1014 SQ 1015
Cdd:cd03300 163 LK 164
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
836-1039 |
1.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.96 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 836 QTSIFHWENVCYDVkikSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPRDSS--- 912
Cdd:PRK13636 2 EDYILKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNG--ILKPSSGRILFDGKPIDYSrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 ---FQRKTGYV-QQQDLHLHTSTVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRDYadaivgiPGEGLNVEQRKR 988
Cdd:PRK13636 77 lmkLRESVGMVfQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1799732068 989 LTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLM-ETLTKNGQAILCTIH 1039
Cdd:PRK13636 150 VAIAGVLVMEPKVLV-LDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATH 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
162-380 |
1.61e-13 |
|
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: 71.41 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 162 NILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPaayinYHG--ITPKQMSTDFRGEAIY---TAEVDAH 236
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG-----LLKP-----TSGsiRVFGKPLEKERKRIGYvpqRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 237 YPqLSVGDtlyFASLARAPRHLPGGISSQEYAtHLRDVIMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYAP 316
Cdd:cd03235 83 FP-ISVRD---VVLMGLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 317 LQCWDNSTRGLDSANAVEFCRTLRTQSDVfGMTsCVAIYQAPQAAYNLFDKVIVLyEGHQIYFG 380
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRE-GMT-ILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
866-1039 |
1.63e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLANRTTVgvVGGDMLVDGRP---RDSSFQRKTGYVQQQDLHLHTSTVREALEFSALL 942
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTV--TSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 943 RQPPQytrEEkldyVEKV----LDLLNMRDYADAIVGIPGEGlnveQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSW 1018
Cdd:TIGR01257 2040 RGVPA---EE----IEKVanwsIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|.
gi 1799732068 1019 SICNLMETLTKNGQAILCTIH 1039
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
866-1058 |
2.20e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 71.08 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDG------RPRDssFQRKTGYVqQQDLHLHTSTVREAL 936
Cdd:cd03245 27 IRAGEKVAIIGRVGSGKSTLLKLLA-----GLYkptSGSVLLDGtdirqlDPAD--LRRNIGYV-PQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 937 EFSAllrqpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:cd03245 99 TLGA-----PLADDER----ILRAAELAGVTDFVnkhpnglDLQIGERGRGLSGGQRQAVALARALLNDPPILL-LDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTiHQPSamLFQRFDRLLLLAKG 1058
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDKTLIIIT-HRPS--LLDLVDRIIVMDSG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
163-340 |
2.59e-13 |
|
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: 70.59 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA-YINYHGITPKQMSTDFRGEAIYTAEVDAHYPQLS 241
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-----LLPPSAgEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTLYFAslarapRHLPGGISSQEYATHLrdviMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYAPLqcW- 320
Cdd:COG4133 92 VRENLRFW------AALYGLRADREAIDEA----LEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPL--Wl 154
|
170 180
....*....|....*....|.
gi 1799732068 321 -DNSTRGLDSANAVEFCRTLR 340
Cdd:COG4133 155 lDEPFTALDAAGVALLAELIA 175
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
855-1067 |
4.81e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.68 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDSSFQRKTGYV-------QQQd 924
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILapdSGEVLWDGEPLDPEDRRRIGYLpeerglyPKM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 lhlhtsTVREALEFSALLRQppqYTREEKLDYVEKVLDLLNMRDYADAivgipgeglNVE------QRKrltigVELAA- 997
Cdd:COG4152 87 ------KVGEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANK---------KVEelskgnQQK-----VQLIAa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 998 ---RPKLLLfLDEPTSGLD--SQtswsicNLMET----LTKNGQAILCTIHQpsaM-LFQRF-DRLLLLAKgGKTVYFGD 1066
Cdd:COG4152 144 llhDPELLI-LDEPFSGLDpvNV------ELLKDvireLAAKGTTVIFSSHQ---MeLVEELcDRIVIINK-GRKVLSGS 212
|
.
gi 1799732068 1067 I 1067
Cdd:COG4152 213 V 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
848-1043 |
8.21e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRTT----VGVVGGDMLVDGRP----RDSSFQRKTGY 919
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIelypEARVSGEVYLDGQDifkmDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 920 VQQQDLHLHTSTVREALEFSALLRQPPQyTREEKLDYVEKVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARP 999
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLNRLVK-SKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799732068 1000 KLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSA 1043
Cdd:PRK14247 166 EVLL-ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQA 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
852-1023 |
8.84e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.26 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 852 KSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTVGVVggdmLVDGRP---------RDssFQRKTGYV 920
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINllERPTSGSV----LVDGVDltalserelRA--ARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 921 QQQDLHLHTSTVRE----ALEFSALLRQppqyTREEKldyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELA 996
Cdd:COG1135 88 FQHFNLLSSRTVAEnvalPLEIAGVPKA----EIRKR---VAELLELVGLSDKADA---YPSQ-LSGGQKQRVGIARALA 156
|
170 180
....*....|....*....|....*..
gi 1799732068 997 ARPKLLLfLDEPTSGLDSQTSWSICNL 1023
Cdd:COG1135 157 NNPKVLL-CDEATSALDPETTRSILDL 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
859-1039 |
1.02e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLdvLANRTTVGVVGGDMLVDGRPRDSS------FQRKTGYV-QQQDLHLHTST 931
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLF--LHFNGILKPTSGEVLIKGEPIKYDkkslleVRKTVGIVfQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSALLRQPPQytrEEKLDYVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSG 1011
Cdd:PRK13639 96 VEEDVAFGPLNLGLSK---EEVEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIAGILAMKPEIIV-LDEPTSG 167
|
170 180
....*....|....*....|....*...
gi 1799732068 1012 LDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
856-1041 |
1.67e-12 |
|
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: 67.77 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPRD---SSFQRKTGYVQQQDLHLHT 929
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA-----GLLrpdSGEVRWNGTPLAeqrDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSALLRQPPQYTreekldyVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWI-LDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTIHQP 1041
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
856-1039 |
1.74e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLanrttVGVV---GGDMLVDGR-----PRDSSFQRKTGYVQQQDLHL 927
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV-----VGIVprdAGNIIIDDEdisllPLHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVREALefSALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIvgipGEGLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:PRK10895 91 RRLSVYDNL--MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFIL-LDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
849-1058 |
2.85e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 68.13 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 849 VKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDG-RP--RDSSFQRKTGYVQQ 922
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-----GLLqptSGEVRVAGlVPwkRRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 Q------DLhlhtsTVREALEF-SALLRQPPQYTREEkldyVEKVLDLLNMRDyadaIVGIPGEGLNVEQRKRLTIGVEL 995
Cdd:cd03267 102 QktqlwwDL-----PVIDSFYLlAAIYDLPPARFKKR----LDELSELLDLEE----LLDTPVRQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 996 AARPKlLLFLDEPTSGLDSQTSWSICNLMETLTKNGQA-ILCTIH--QPSAMLfqrFDRLLLLAKG 1058
Cdd:cd03267 169 LHEPE-ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTtVLLTSHymKDIEAL---ARRVLVIDKG 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
848-1074 |
3.59e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDS----SFQRKTGYV 920
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLtptAGTVLVAGDDVEAlsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 921 QQQDLHLHTSTVREALEFSallrQPPQYTREEKLD-----YVEKVLDllnmRDYADAIVGIPGEGLNVEQRKRLTIGVEL 995
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMG----RTPHRSRFDTWTetdraAVERAME----RTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 996 A-ARPKLLlfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSamLFQRF-DRLLLLAKGGKTvyfgDIGRESRI 1073
Cdd:PRK09536 155 AqATPVLL--LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLD--LAARYcDELVLLADGRVR----AAGPPADV 226
|
.
gi 1799732068 1074 L 1074
Cdd:PRK09536 227 L 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
163-387 |
3.65e-12 |
|
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: 67.91 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA---YINYHGITP----------KQMSTDFRGEAIY 229
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG-----LLRPDSgevLIDGEDISGlseaelyrlrRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 230 TAevdahypqLSVGDTLYFasLARAPRHLPggissqeyATHLRDVIM---AMFGIGHTINTRVGNdfvrgVSGGERKRVT 306
Cdd:cd03261 90 DS--------LTVFENVAF--PLREHTRLS--------EEEIREIVLeklEAVGLRGAEDLYPAE-----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 307 IAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTScVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAK 386
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTS-IMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 1799732068 387 A 387
Cdd:cd03261 226 A 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
155-380 |
4.60e-12 |
|
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: 66.50 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 155 GGKKRkinILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVDPAAYINYHGITPkqmstDFRGEAIYTAEVD 234
Cdd:cd03232 17 GGKRQ---LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDK-----NFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 235 AHYPQLSVGDTLYFASLaraprhlpggissqeyathlrdvimamfgightintrvgndfVRGVSGGERKRVTIAeAALSY 314
Cdd:cd03232 89 VHSPNLTVREALRFSAL------------------------------------------LRGLSVEQRKRLTIG-VELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 315 APLQCW-DNSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYNLFDKVIVLYE-GHQIYFG 380
Cdd:cd03232 126 KPSILFlDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
857-1066 |
5.27e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLL-----DVLANRTTVGVVGGDMlvdgRPRDSSFQR-KTGYV-QQQDLHLHT 929
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngIYLPQRGRVKVMGREV----NAENEKWVRsKVGLVfQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSallrqpPQ---YTREEKLDYVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:PRK13647 95 STVWDDVAFG------PVnmgLDKDEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV-LD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1007 EPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLfQRFDRLLLLaKGGKTVYFGD 1066
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVL-KEGRVLAEGD 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
856-1041 |
5.60e-12 |
|
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: 66.36 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVGVVGGDMLVDGRPRDSsFQRKTGYVQQQDLHLHTSTVR 933
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFsallrqppqYTREEKLDYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:cd03231 92 ENLRF---------WHADHSDEQVEEALARVGLNGFEDRPVA----QLSAGQQRRVALARLLLSGRPLWI-LDEPTTALD 157
|
170 180
....*....|....*....|....*...
gi 1799732068 1014 SQTSWSICNLMETLTKNGQAILCTIHQP 1041
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
843-1035 |
7.26e-12 |
|
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: 66.87 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVC--YDvkiksETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRP-RD---SSFQRK 916
Cdd:cd03253 4 ENVTfaYD-----PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFR--FYDVSSGSILIDGQDiREvtlDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 917 TGYVQQqDLHLHTSTVREALEFSAllrqpPQYTREEKLDyVEKVLDL----LNMRDYADAIVGIPGEGLNVEQRKRLTIg 992
Cdd:cd03253 77 IGVVPQ-DTVLFNDTIGYNIRYGR-----PDATDEEVIE-AAKAAQIhdkiMRFPDGYDTIVGERGLKLSGGEKQRVAI- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 993 velaARPKL----LLFLDEPTSGLDSQTSWSICNLMETLTKNGQAIL 1035
Cdd:cd03253 149 ----ARAILknppILLLDEATSALDTHTEREIQAALRDVSKGRTTIV 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
858-1039 |
8.86e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP---RDSSFQRKTGYVQQQDLHLHTSTVRE 934
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPvpsRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALE-FSALLRQPPQYTREEkldyVEKVLDLLNMRDYADAIVGIPGEGLnveqRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK13537 100 NLLvFGRYFGLSAAAARAL----VPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVLV-LDEPTTGLD 170
|
170 180
....*....|....*....|....*.
gi 1799732068 1014 SQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTH 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
157-380 |
1.41e-11 |
|
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: 65.85 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 157 KKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG---------ETHGFQV--DPAAYINYHGITPKQMstdfrg 225
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfaTVDGFDVvkEPAEARRRLGFVSDST------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 226 eaiytaevdAHYPQLSVGDTL-YFASLAraprhlpgGISSQEYATHLRDVImAMFGIGHTINTRVGndfvrGVSGGERKR 304
Cdd:cd03266 88 ---------GLYDRLTARENLeYFAGLY--------GLKGDELTARLEELA-DRLGMEELLDRRVG-----GFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 305 VTIAEAALSYAPLQCWDNSTRGLD---SANAVEFCRTLRTQSDVFGMTSCVAiyqapQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDvmaTRALREFIRQLRALGKCILFSTHIM-----QEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
868-1066 |
1.49e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 868 PGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRDS----SFQRKTGYVQQQDLHLHTSTVREALefsALLR 943
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESwsskAFARKVAYLPQQLPAAEGMTVRELV---AIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 944 QP-----PQYTREEKlDYVEKVLDLLNMRDYADAIVgipgEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSW 1018
Cdd:PRK10575 111 YPwhgalGRFGAADR-EKVEEAISLVGLKPLAHRLV----DSLSGGERQRAWIAMLVAQDSRCLL-LDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799732068 1019 SICNLMETLTK-NGQAILCTIHQPSaMLFQRFDRLLLLaKGGKTVYFGD 1066
Cdd:PRK10575 185 DVLALVHRLSQeRGLTVIAVLHDIN-MAARYCDYLVAL-RGGEMIAQGT 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
858-1058 |
1.71e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA-----NRTTVGVVGGDM-LVDGRPRDSSFQRKTGYVQQQDLHLHTST 931
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgSSGEVSLVGQPLhQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSALLRQppqytrEEKLDYVEKVLDLLNMRDYADAIVGIPGEGLNVEQrKRLTIGVELAARPKlLLFLDEPTSG 1011
Cdd:PRK10584 105 ALENVELPALLRG------ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQ-QRVALARAFNGRPD-VLFADEPTGN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 1012 LDSQTSWSICNLMETLTKN-GQAILCTIHQPSamLFQRFDRLLLLAKG 1058
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREhGTTLILVTHDLQ--LAARCDRRLRLVNG 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
163-380 |
2.12e-11 |
|
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: 64.38 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGEthgfqvdpaayinyhgITPKQmstdfrGEaIYTAEVDAHypQLSv 242
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL----------------LKPSS------GE-ILLDGKDLA--SLS- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 gdtlyfaSLARApRHLpgGISSQeyathlrdvIMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYAPLQCWDN 322
Cdd:cd03214 68 -------PKELA-RKI--AYVPQ---------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 323 STRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQaPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHD-LNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
151-418 |
3.42e-11 |
|
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: 67.62 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 151 YQFLGGKKRkinILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGEThGFQVDPAAYINYHGITPKQMSTDFRGEAIYT 230
Cdd:COG1123 12 VRYPGGDVP---AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGEVLLDGRDLLELSEALRGRRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 231 --AEVDAHYPQLSVGDTLYFASLARaprhlpgGISSQEYATHLRDViMAMFGIGHtintrVGNDFVRGVSGGERKRVTIA 308
Cdd:COG1123 88 vfQDPMTQLNPVTVGDQIAEALENL-------GLSRAEARARVLEL-LEAVGLER-----RLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 309 EAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTsCVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAKAY 388
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTT-VLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260 270
....*....|....*....|....*....|
gi 1799732068 389 FERLGFLcPESQTTADFLTSMSSPTERIIR 418
Cdd:COG1123 234 PQALAAV-PRLGAARGRAAPAAAAAEPLLE 262
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
846-1058 |
3.42e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 846 CYDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGV------VGGDMLVDGRPRDS----SFQR 915
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLAAidapRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYVQQQdlhlhtstVREALEFSA----LLRQPPQYTREEKLDYVEK-VLDLLNMRDYADAIVGIPGEGLNVEQRKRLT 990
Cdd:PRK13547 84 LRAVLPQA--------AQPAFAFSAreivLLGRYPHARRAGALTHRDGeIAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 991 IGVELA--------ARPKLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQ-AILCTIHQPSamLFQRF-DRLLLLAKG 1058
Cdd:PRK13547 156 FARVLAqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPN--LAARHaDRIAMLADG 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
848-1058 |
3.62e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.09 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGrprdssfqrktgyvqqQDLhL 927
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG----------------EDI-T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVREALEFSALLRQPPqytreEKLDYVeKVLDLLnmRDYadaivgipGEGLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:cd03217 68 DLPPEERARLGIFLAFQYP-----PEIPGV-KNADFL--RYV--------NEGFSGGEKKRNEILQLLLLEPDLAI-LDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKG 1058
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDG 181
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
856-1058 |
4.47e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRdSSFQRktgyvQQQDLHL-----HTS 930
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGRPL-ADWSP-----AELARRRavlpqHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 -----TVREALefsALLRQPPQYTREEKLDYVEKVLDLLNMRDYAD----AIVGipGEglnvEQRkrltigVELA----- 996
Cdd:PRK13548 87 lsfpfTVEEVV---AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGrdypQLSG--GE----QQR------VQLArvlaq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 997 ----ARPKLLLFLDEPTSGLD--SQTswsicNLMETL----TKNGQAILCTIHQPSamLFQRF-DRLLLLAKG 1058
Cdd:PRK13548 152 lwepDGPPRWLLLDEPTSALDlaHQH-----HVLRLArqlaHERGLAVIVVLHDLN--LAARYaDRIVLLHQG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
829-1058 |
4.94e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 829 STIGVEKQTSIFHWENVcydvkiksetrriLDHVDGWIKPGTLTALMGSSGAGKTTLLDV--LANRTTVGVVG-GDMLVD 905
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTV-------------LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 906 G-RPRDS------SFQRKTGYV-QQQDLHLHtstvREALEfsALLRQPPQYTREEKLDYVEKVLDLLnmrdyadAIVGIP 977
Cdd:PRK11264 69 TaRSLSQqkglirQLRQHVGFVfQNFNLFPH----RTVLE--NIIEGPVIVKGEPKEEATARARELL-------AKVGLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 978 GEG------LNVEQRKRLTIGVELAARPKLLLFlDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQpsaMLFQR--F 1049
Cdd:PRK11264 136 GKEtsyprrLSGGQQQRVAIARALAMRPEVILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFARdvA 211
|
....*....
gi 1799732068 1050 DRLLLLAKG 1058
Cdd:PRK11264 212 DRAIFMDQG 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
856-1041 |
5.03e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVGVVGGDmlvDGRPRDSSFQRKTGYVQQQDLHLHTSTVR 933
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIKLD---GGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEF-SALLRQPPQytreekldYVEKVLDLLNMRDYADaivgIPGEGLNVEQRKRLTIGVELAA-RPklLLFLDEPTSG 1011
Cdd:PRK13539 92 ENLEFwAAFLGGEEL--------DIAAALEAVGLAPLAH----LPFGYLSAGQKRRVALARLLVSnRP--IWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1012 LDSQTSWSICNLMET-LTKNGQAILCTiHQP 1041
Cdd:PRK13539 158 LDAAAVALFAELIRAhLAQGGIVIAAT-HIP 187
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
155-375 |
5.24e-11 |
|
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: 64.05 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 155 GGKKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG---ETHGfQVdpaaYINyhGITPKQMS----TDFRGEA 227
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldrPTSG-EV----RVD--GTDISKLSekelAAFRRRH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 228 IytAEVDAHY---PQLSVGD----TLYFASLARAPRHlpggissqEYATHLrdviMAMFGIGHTINTRVGNdfvrgVSGG 300
Cdd:cd03255 84 I--GFVFQSFnllPDLTALEnvelPLLLAGVPKKERR--------ERAEEL----LERVGLGDRLNHYPSE-----LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 301 ERKRVTIAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQaPQAAyNLFDKVIVLYEGH 375
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELA-EYADRIIELRDGK 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
857-1012 |
1.30e-10 |
|
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: 63.08 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRP--RDSSFQRKT---GYVQQ-----Q 923
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLL-----KAISGLLpprSGSIRFDGEDitGLPPHRIARlgiGYVPEgrrifP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 DLhlhtsTVREALEFSALLRQPPQYTREEkldyVEKVLDLL-NMRDYADAIVGIPGEGlnveQRKRLTIGVELAARPKLL 1002
Cdd:COG0410 92 SL-----TVEENLLLGAYARRDRAEVRAD----LERVYELFpRLKERRRQRAGTLSGG----EQQMLAIGRALMSRPKLL 158
|
170
....*....|
gi 1799732068 1003 LfLDEPTSGL 1012
Cdd:COG0410 159 L-LDEPSLGL 167
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
164-383 |
1.31e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 164 LQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGFQVdPAAYINYHGITPK---QMSTDFRGEAIYTAEVDAHYP-- 238
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-AGSHIELLGRTVQregRLARDIRKSRANTGYIFQQFNlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 239 -QLSVGDTLYFASLARAP--RHLPGGISSQEYATHLRdvIMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYA 315
Cdd:PRK09984 99 nRLSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQ--ALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 316 PLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQApQAAYNLFDKVIVLYEGHQIYFGAAH 383
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV-DYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
858-1013 |
1.52e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 62.66 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGR------PRDssfqRKTGYV-QQQDLHL 927
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTL-----RMIAGLEeptSGRIYIGGRdvtdlpPKD----RDIAMVfQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTsTVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRD-YADAIVGipGeglnveQRKRLTIGVELAARPKLLLfLD 1006
Cdd:cd03301 86 HM-TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDrKPKQLSG--G------QRQRVALGRAIVREPKVFL-MD 155
|
....*..
gi 1799732068 1007 EPTSGLD 1013
Cdd:cd03301 156 EPLSNLD 162
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
839-1039 |
2.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 839 IFHWENVCYDVKIKSE-TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVGVVG-GDMLVDGRPRDSSFQ 914
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 915 ---RKTGYVQQ-QDLHLHTSTVREALEFSallrqpPQ---YTREEKLDYVEKVLDLLNM-RDYADAIvgiPGEgLNVEQR 986
Cdd:PRK13643 81 pvrKKVGVVFQfPESQLFEETVLKDVAFG------PQnfgIPKEKAEKIAAEKLEMVGLaDEFWEKS---PFE-LSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 987 KRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK13643 151 RRVAIAGILAMEPEVLV-LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
847-1040 |
2.48e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 847 YDVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGG--DMLVDGRPRDSSfqrktgyvqqqd 924
Cdd:COG2401 34 FGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGcvDVPDNQFGREAS------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 lhlhtstVREALefsallrqppqYTREEKLDYVEkvldLLNMRDYADAIVGI--PGEgLNVEQRKRLTIGVELAARPKLL 1002
Cdd:COG2401 102 -------LIDAI-----------GRKGDFKDAVE----LLNAVGLSDAVLWLrrFKE-LSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTK--NGQAILCTIHQ 1040
Cdd:COG2401 159 V-IDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHY 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
859-1030 |
2.64e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTlldvLANRTT--VGVVGGDMLVDGRP-RD---SSFQRKTGYVQQQdLHLHTSTV 932
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST----IANLLTrfYDIDEGEILLDGHDlRDytlASLRNQVALVSQN-VHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 933 REALEFSAllrqPPQYTREE---------KLDYVEKvldllnMRDYADAIVGIPGEGLNVEQRKRLTIgvelaARPKL-- 1001
Cdd:PRK11176 434 ANNIAYAR----TEQYSREQieeaarmayAMDFINK------MDNGLDTVIGENGVLLSGGQRQRIAI-----ARALLrd 498
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1002 --LLFLDEPTSGLDSQTSWSICNLMETLTKN 1030
Cdd:PRK11176 499 spILILDEATSALDTESERAIQAALDELQKN 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
847-1066 |
2.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 847 YDVKIKSETRrILDHVDGWIKPGTLTALMGSSGAGKTTLL--------------------DVLANRTTVGVVGGDMLVDG 906
Cdd:PRK13651 12 FNKKLPTELK-ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtgtiewifkdEKNKKKTKEKEKVLEKLVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 907 RPRDSSFQ------RKTGYVQQ-QDLHLHTSTVREALEFSAL-LRQPPQYTREEKLDYVEkvldllnmrdyadaIVGIPG 978
Cdd:PRK13651 91 KTRFKKIKkikeirRRVGVVFQfAEYQLFEQTIEKDIIFGPVsMGVSKEEAKKRAAKYIE--------------LVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 979 E-------GLNVEQRKRLTIGVELAARPKLLlFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLfQRFDR 1051
Cdd:PRK13651 157 SylqrspfELSGGQKRRVALAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKR 234
|
250
....*....|....*
gi 1799732068 1052 LLLLaKGGKTVYFGD 1066
Cdd:PRK13651 235 TIFF-KDGKIIKDGD 248
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
866-1058 |
2.66e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLanrttvgvVG-----GDMLVDGRP-RD---SSFQRKTGYVqQQDLHLHTSTVREAL 936
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNAL--------LGflpyqGSLKINGIElREldpESWRKHLSWV-GQNPQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 937 efsaLLRQpPQYTREEkldyVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:PRK11174 444 ----LLGN-PDASDEQ----LQQALENAWVSEFLpllpqglDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL-LDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1010 SGLDSQTSWSIcnlMETLTKN--GQAILCTIHQPSAMlfQRFDRLLLLAKG 1058
Cdd:PRK11174 514 ASLDAHSEQLV---MQALNAAsrRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
859-1015 |
3.78e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGrpRDSS----FQRKTGYV-QQQDLHLHTsTVR 933
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PTAGQIMLDG--VDLShvppYQRPINMMfQSYALFPHM-TVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFSalLRQpPQYTREEKLDYVEKVLDLLNMRDYAdaivGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK11607 110 QNIAFG--LKQ-DKLPKAEIASRVNEMLGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLL-LDEPMGALD 181
|
..
gi 1799732068 1014 SQ 1015
Cdd:PRK11607 182 KK 183
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
866-1058 |
4.01e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.36 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTT---LLDVLANRTtvgvvGGDMLVDGRP----RDSSFQRKTGYVQQQDLhLHTSTVREALEF 938
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTvaaLLQNLYQPT-----GGQVLLDGVPlvqyDHHYLHRQVALVGQEPV-LFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 939 SAllrqppQYTREEKLDYVEKVLD----LLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDS 1014
Cdd:TIGR00958 578 GL------TDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799732068 1015 QTSWSICNLMEtltKNGQAILCTIHQPSamLFQRFDRLLLLAKG 1058
Cdd:TIGR00958 651 ECEQLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
859-1035 |
4.41e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGR------PRDSsfqRKTG-YVQQQDLHLH 928
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVYqpdSGEILLDGEpvrfrsPRDA---QAAGiAIIHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TS-TVREALefsALLRQPpqyTREEKLDY------VEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKL 1001
Cdd:COG1129 92 PNlSVAENI---FLGREP---RRGGLIDWramrrrARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSRDARV 161
|
170 180 190
....*....|....*....|....*....|....
gi 1799732068 1002 LLfLDEPTSGLDSQTSWSICNLMETLTKNGQAIL 1035
Cdd:COG1129 162 LI-LDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
857-1035 |
5.31e-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: 59.75 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPrdssfqrktgyvqqqdlhLHTSTVR 933
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYkpdSGEILVDGKE------------------VSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFS-ALLRQppqytreekldyvekvldllnmrdyadaivgipgegLNVEQRKRLTIGVELAARPKLLLfLDEPTSGL 1012
Cdd:cd03216 71 DARRAGiAMVYQ------------------------------------LSVGERQMVEIARALARNARLLI-LDEPTAAL 113
|
170 180
....*....|....*....|...
gi 1799732068 1013 DSQTSWSICNLMETLTKNGQAIL 1035
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVI 136
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
858-1058 |
7.60e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVL-----ANRttvgvvgGDMLVDGRP-RDSSFQ--RKTGYVQQQDLHLHT 929
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdPQQ-------GEILLNGQPiADYSEAalRQAISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 STVREALEFSAllrqpPQYTREEKLDYVEKV-LD-LLNMRDYADAIVGIPGEGLNVEQRKRLTIgvelaARPKL----LL 1003
Cdd:PRK11160 428 ATLRDNLLLAA-----PNASDEALIEVLQQVgLEkLLEDDKGLNAWLGEGGRQLSGGEQRRLGI-----ARALLhdapLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 1004 FLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HRLTGL--EQFDRICVMDNG 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
852-1062 |
7.71e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 852 KSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTVGVV---GGDMLVDGRPRDSSFQRKTGYVQQQDLh 926
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVglESPSQGNVswrGEPLAKLNRAQRKAFRRDIQMVFQDSI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 lhtSTVREALEFSALLRQPPQY-TREEKLDYVEKVLDLLNMRDYADAIVG-IPGEgLNVEQRKRLTIGVELAARPKLLLf 1004
Cdd:PRK10419 100 ---SAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDkRPPQ-LSGGQLQRVCLARALAVEPKLLI- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 1005 LDEPTSGLDSQTSWSICNLMETL-TKNGQAILCTIHQPSamLFQRFDRLLLLAKGGKTV 1062
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLR--LVERFCQRVMVMDNGQIV 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
858-1016 |
8.77e-10 |
|
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: 60.63 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRtTVGVVGGDMLVDGRP-RD---SSFQRKTGYVqQQDLHLHTSTVR 933
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-ER-FYDPTSGEILLDGVDiRDlnlRWLRSQIGLV-SQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYadaIVGIPgEGLNVE-----------QRKRLTIGVELAARPKLL 1002
Cdd:cd03249 95 ENIRYGK-----PDATDEE----VEEAAKKANIHDF---IMSLP-DGYDTLvgergsqlsggQKQRIAIARALLRNPKIL 161
|
170
....*....|....
gi 1799732068 1003 LfLDEPTSGLDSQT 1016
Cdd:cd03249 162 L-LDEATSALDAES 174
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
163-340 |
9.28e-10 |
|
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: 63.15 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG--ETHGFQVdpaayiNYHGITPKQMSTDFRGEAIYTAEVDAHYPQL 240
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGllDPLQGEV------TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 241 SVGDTLYFASlaraprhlpGGISSQEYATHLRDVIMAMF--GIGHTINTRVGNDFVRgVSGGERKRVTIAEAALSYAPLQ 318
Cdd:TIGR02868 424 TVRENLRLAR---------PDATDEELWAALERVGLADWlrALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPIL 493
|
170 180
....*....|....*....|..
gi 1799732068 319 CWDNSTRGLDSANAVEFCRTLR 340
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLL 515
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
856-1058 |
1.20e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP-RDSSFQRktGYVQQQDLHLHTSTVRE 934
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPvEGPGAER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALEFSALLRQPPQYTREekldyvEKVLDLLnmrdyadAIVGIPGEG------LNVEQRKRLTIGVELAARPKLLLfLDEP 1008
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRL------EIAHQML-------KKVGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLL-LDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1009 TSGLDSQTSWSICNLMETL-TKNGQAILCTIHQPSAMLFQRFDrLLLLAKG 1058
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATE-LVLLSPG 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
858-1058 |
2.05e-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: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLanRTTVGVVGGDMLVDGRPRdSSFQ---RKTGYVQQQDLHLHTSTVRE 934
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLL--TGDLKPQQGEITLDGVPV-SDLEkalSSLISVLNQRPYLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALefsallrqppqytreekldyvekvldllnmrdyadaivgipGEGLNVEQRKRLTIgvelaARPKL----LLFLDEPTS 1010
Cdd:cd03247 94 NL-----------------------------------------GRRFSGGERQRLAL-----ARILLqdapIVLLDEPTV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 1011 GLDSQTSWSICNLMETLTKNGQAILCTiHQPSAMlfQRFDRLLLLAKG 1058
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWIT-HHLTGI--EHMDKILFLENG 172
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
848-1066 |
2.24e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGR------PRDS-------SFQ 914
Cdd:PRK09580 6 DLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKdllelsPEDRagegifmAFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 915 RKT---GYVQQQDLHLHTSTVREalefsalLRQPPQYTREEKLDYVEKVLDLLNMRdyADAIVGIPGEGLNVEQRKRLTI 991
Cdd:PRK09580 86 YPVeipGVSNQFFLQTALNAVRS-------YRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVNVGFSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 992 gVELAARPKLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKgGKTVYFGD 1066
Cdd:PRK09580 157 -LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQ-GRIVKSGD 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
868-1013 |
2.33e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 868 PGTLTALMGSSGAGKTTLLDVLANRTTV--GVVGGDMlVDGRPRD----SSFQRKT------GYVQQ---QDLHLHTS-- 930
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPdaGEVHYRM-RDGQLRDlyalSEAERRRllrtewGFVHQhprDGLRMQVSag 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 -TVREALefSALLRQPPQYTREEKLDYVEKV-LDLLNMRDYADAIVGipgeGLnveqRKRLTIGVELAARPKlLLFLDEP 1008
Cdd:PRK11701 110 gNIGERL--MAVGARHYGDIRATAGDWLERVeIDAARIDDLPTTFSG----GM----QQRLQIARNLVTHPR-LVFMDEP 178
|
....*
gi 1799732068 1009 TSGLD 1013
Cdd:PRK11701 179 TGGLD 183
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
866-1030 |
2.39e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.67 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLaNR---TTVGV-VGGDMLVDGRP-----------RdssfqRKTGYVQQQDLHLHTS 930
Cdd:COG1117 34 IPENKVTALIGPSGCGKSTLLRCL-NRmndLIPGArVEGEILLDGEDiydpdvdvvelR-----RRVGMVFQKPNPFPKS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 tVREALEFSALLRQppqYTREEKLDY-VEKVL----------DLLNMrdyadaivgiPGEGLNVEQRKRLTIGVELAARP 999
Cdd:COG1117 108 -IYDNVAYGLRLHG---IKSKSELDEiVEESLrkaalwdevkDRLKK----------SALGLSGGQQQRLCIARALAVEP 173
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1000 KLLLfLDEPTSGLDSQTSWSICNLMETLTKN 1030
Cdd:COG1117 174 EVLL-MDEPTSALDPISTAKIEELILELKKD 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
157-341 |
2.77e-09 |
|
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: 59.06 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 157 KKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGE---THGFqvdpaAYINYHGITpKQMStDFRGEAIYTAEV 233
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrpTSGT-----AYINGYSIR-TDRK-AARQSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 234 DAHYPQLSVGDTLYFasLARApRHLPGGISSQEYATHLRdvimaMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALS 313
Cdd:cd03263 84 DALFDELTVREHLRF--YARL-KGLPKSEIKEEVELLLR-----VLGLTDKANKRART-----LSGGMKRKLSLAIALIG 150
|
170 180 190
....*....|....*....|....*....|....
gi 1799732068 314 YAPLQCWDNSTRGLDSA------NAVEFCRTLRT 341
Cdd:cd03263 151 GPSVLLLDEPTSGLDPAsrraiwDLILEVRKGRS 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
829-1058 |
3.61e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 829 STIGVEKQTSIFHwenvcydvkikseTRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTT--------VGVVGG 900
Cdd:PRK09984 3 TIIRVEKLAKTFN-------------QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshIELLGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 901 DMLVDGR-PRDSSFQR-KTGYVQQQDLHLHTSTVREALEFSALLRQP------PQYTREEKlDYVEKVLDLLNMRDYADA 972
Cdd:PRK09984 70 TVQREGRlARDIRKSRaNTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 973 IVGIPGEGlnveQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSAMLfqRF-D 1050
Cdd:PRK09984 149 RVSTLSGG----QQQRVAIARALMQQAKVIL-ADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL--RYcE 221
|
....*...
gi 1799732068 1051 RLLLLAKG 1058
Cdd:PRK09984 222 RIVALRQG 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
855-1013 |
4.88e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvgvvgGDMLVDG----RPRDSsfqrKTGYVQQQDLHLHTS 930
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA---------GELEPDSgevsIPKGL----RIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREAL------------EFSALLRQPPQYTRE-EKLDYVEKVLDLLNMRDY---ADAIV---GIPGEGLNVE------- 984
Cdd:COG0488 77 TVLDTVldgdaelraleaELEELEAKLAEPDEDlERLAELQEEFEALGGWEAearAEEILsglGFPEEDLDRPvselsgg 156
|
170 180 190
....*....|....*....|....*....|...
gi 1799732068 985 QRKRltigVELA----ARPKLLLfLDEPTSGLD 1013
Cdd:COG0488 157 WRRR----VALArallSEPDLLL-LDEPTNHLD 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
856-1038 |
5.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTT---LLDVL-----ANRTTVGVVG----GDMLVDGRprdssfqRKTGYV-QQ 922
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLllpddNPNSKITVDGitltAKTVWDIR-------EKVGIVfQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 QDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLL 1002
Cdd:PRK13640 93 PDNQFVGATVGDDVAFGLENRAVP---RPEMIKIVRDVLADVGMLDYIDS----EPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTI 1038
Cdd:PRK13640 166 I-LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
866-1069 |
5.85e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLAnrttvG---VVGGDMLVDGRP--RDSSFQRKtgyV----QQQDL--HLhtsTVRE 934
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIA-----GflpPDSGRILWNGQDltALPPAERP---VsmlfQENNLfpHL---TVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 --ALEFSALLRqppqYTREEKLDyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRltigVELA-----ARPKLLlfLDE 1007
Cdd:COG3840 91 niGLGLRPGLK----LTAEQRAQ-VEQALERVGLAGLLDR---LPGQ-LSGGQRQR----VALArclvrKRPILL--LDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKNGQA-ILCTIHQPSAMLfqRF-DRLLLLAkGGKTVYFGDIGR 1069
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLtVLMVTHDPEDAA--RIaDRVLLVA-DGRIAADGPTAA 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
831-1058 |
5.95e-09 |
|
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: 57.48 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 831 IGVEKQTsiFHWENVcydvkiKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvgvvgGDM-LVDGRpr 909
Cdd:cd03250 1 ISVEDAS--FTWDSG------EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL---------GELeKLSGS-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 910 dSSFQRKTGYVQQQDLHLHTsTVREALEFSAllrqppQYtREEKLDYV------EKVLDLLNMRDyaDAIVGIPGEGLNV 983
Cdd:cd03250 62 -VSVPGSIAYVSQEPWIQNG-TIRENILFGK------PF-DEERYEKVikacalEPDLEILPDGD--LTEIGEKGINLSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 984 EQRKRLTigveLA----ARPKLLLfLDEPTSGLDSQTSWSICN--LMETLTKNGQAILCTiHQPSamLFQRFDRLLLLAK 1057
Cdd:cd03250 131 GQKQRIS----LAravySDADIYL-LDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVT-HQLQ--LLPHADQIVVLDN 202
|
.
gi 1799732068 1058 G 1058
Cdd:cd03250 203 G 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
163-387 |
1.03e-08 |
|
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: 57.68 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA-YINYHGITPKQMSTD------------FRGEAIY 229
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-----LLRPDSgEILVDGQDITGLSEKelyelrrrigmlFQGGALF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 230 TAevdahypqLSVGDTLYFaslaraP--RHlpGGISSQEyathLRDVIM---AMFGIGHTINTrvgndFVRGVSGGERKR 304
Cdd:COG1127 95 DS--------LTVFENVAF------PlrEH--TDLSEAE----IRELVLeklELVGLPGAADK-----MPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 305 VTIAEA-ALSyaP-LQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTScVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAA 382
Cdd:COG1127 150 VALARAlALD--PeILLYDEPTAGLDPITSAVIDELIRELRDELGLTS-VVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
....*
gi 1799732068 383 HDAKA 387
Cdd:COG1127 227 EELLA 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
858-1060 |
1.30e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVvgGDMLVDGRP---RDSSFQRKTGYVQQQDLHLHTSTVRE 934
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPvpaRARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 AL-EFSALLRQppqYTREEKlDYVEKVLDLLNMRDYADAIVGIPGEGLnveqRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK13536 134 NLlVFGRYFGM---STREIE-AVIPSLLEFARLESKADARVSDLSGGM----KRRLTLARALINDPQLLI-LDEPTTGLD 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 1014 SQTSWSICNLMETLTKNGQAILCTIHQPSAMlfQRF-DRLLLLAKGGK 1060
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTHFMEEA--ERLcDRLCVLEAGRK 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
856-1039 |
1.31e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.35 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRP--RDSSFQRKT---GYVQQQ---- 923
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTF-----YMIVGLVkpdSGRIFLDGEDitHLPMHKRARlgiGYLPQEasif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 924 -DLhlhtsTVRE----ALEfsalLRQPPQYTREEKLDYVEKVLDLLNMRD-YADAIVGipGEglnveqRKRLTIGVELAA 997
Cdd:COG1137 91 rKL-----TVEDnilaVLE----LRKLSKKEREERLEELLEEFGITHLRKsKAYSLSG--GE------RRRVEIARALAT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:COG1137 154 NPKFIL-LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
164-340 |
1.49e-08 |
|
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: 59.22 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 164 LQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA-YINYHGITPKQMSTDFRGEAIytaevdAHYPQLSv 242
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-----FVDPTEgSIAVNGVPLADADADSWRDQI------AWVPQHP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 gdTLYFASLARAPRHLPGGISSQEYATHLRDVIMAMF--GIGHTINTRVGNDfVRGVSGGERKRVTIAEAALSYAPLQCW 320
Cdd:TIGR02857 406 --FLFAGTIAENIRLARPDASDAEIREALERAGLDEFvaALPQGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180
....*....|....*....|
gi 1799732068 321 DNSTRGLDSANAVEFCRTLR 340
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALR 502
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
849-1014 |
1.63e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 849 VKIKSETRR-----ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA---NRTtvgvvGGDMLVDGRP-RDSSFQ-RKTG 918
Cdd:PRK11432 7 VVLKNITKRfgsntVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAgleKPT-----EGQIFIDGEDvTHRSIQqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 YV-QQQDLHLHTStVREALEFSALLRQPPQYTREEKLDYVEKVLDLLNMRD-YADAIVGipgeglnvEQRKRLTIGVELA 996
Cdd:PRK11432 82 MVfQSYALFPHMS-LGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDrYVDQISG--------GQQQRVALARALI 152
|
170
....*....|....*...
gi 1799732068 997 ARPKLLLFlDEPTSGLDS 1014
Cdd:PRK11432 153 LKPKVLLF-DEPLSNLDA 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
856-1015 |
1.66e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA-----NRTTVGVVGGDMlvdgrPRDSSFQRKTGYV-QQQDLHLHT 929
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglehqTSGHIRFHGTDV-----SRLHARDRKVGFVfQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 sTVREALEFSalLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPGEgLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:PRK10851 90 -TVFDNIAFG--LTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALAVEPQILL-LDEPF 164
|
....*.
gi 1799732068 1010 SGLDSQ 1015
Cdd:PRK10851 165 GALDAQ 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
855-1059 |
1.98e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.95 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGRP----RDSSFQRKTGYVQQQDLHLHTS 930
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQSGTVFLGDKPismlSSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSallRQP--PQYTREEKLDY--VEKVLDLLNMRDYADAIVgipgEGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:PRK11231 92 TVRELVAYG---RSPwlSLWGRLSAEDNarVNQAMEQTRINHLADRRL----TDLSGGQRQRAFLAMVLAQDTPVVL-LD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 1007 EPTSGLDSQTSWSICNLMETLTKNGQAILCTIH---QPSamlfqRF-DRLLLLAKGG 1059
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS-----RYcDHLVVLANGH 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
806-1058 |
2.66e-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: 58.87 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 806 CQHDEERTQAPVIQNEKHSEGPDSTIGVekQTSIFHWE------NVCYD--VKI-KSETRRILDHVDGWIKPGTLTALMG 876
Cdd:TIGR01257 886 CSTREERALEKTEPLTEEMEDPEHPEGI--NDSFFERElpglvpGVCVKnlVKIfEPSGRPAVDRLNITFYENQITAFLG 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 877 SSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPRDSSF---QRKTGYVQQQDLHLHTSTVREALEFSALLRQPPQYTREEK 953
Cdd:TIGR01257 964 HNGAGKTTTLSILTG--LLPPTSGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 954 LDYVEKVLDLLNMRDYAdaivgipGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQA 1033
Cdd:TIGR01257 1042 MEAMLEDTGLHHKRNEE-------AQDLSGGMQRKLSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
250 260
....*....|....*....|....*
gi 1799732068 1034 ILCTIHQPSAMLFQrfDRLLLLAKG 1058
Cdd:TIGR01257 1114 IMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
843-1058 |
3.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETR-RILDHVDGWIKPGTLTALMGSSGAGKTTLLDvLANRTTVGVVG----GDMLVDGRPRD----SSF 913
Cdd:PRK13645 10 DNVSYTYAKKTPFEfKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTNGLIISETGqtivGDYAIPANLKKikevKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 914 QRKTGYVQQ-QDLHLHTSTVREALEFSallrqpPQYTREEKLDYVEKVLDLLNM----RDYADAIvgiPGEgLNVEQRKR 988
Cdd:PRK13645 89 RKEIGLVFQfPEYQLFQETIEKDIAFG------PVNLGENKQEAYKKVPELLKLvqlpEDYVKRS---PFE-LSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 989 LTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQPSAMLfQRFDRLLLLAKG 1058
Cdd:PRK13645 159 VALAGIIAMDGNTLV-LDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVL-RIADEVIVMHEG 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
866-1013 |
3.47e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGR---PRDSSFQRKTGYV--Q-QQ---DLhlhtsTVR 933
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLT-----GILvptSGEVRVLGYvpfKRRKEFARRIGVVfgQrSQlwwDL-----PAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEfsaLLRQ-----PPQYtrEEKLDYVEKVLDLlnmrdyaDAIVGIPGEGLNVEQRKRltigVELAA----RPKLLlF 1004
Cdd:COG4586 115 DSFR---LLKAiyripDAEY--KKRLDELVELLDL-------GELLDTPVRQLSLGQRMR----CELAAallhRPKIL-F 177
|
....*....
gi 1799732068 1005 LDEPTSGLD 1013
Cdd:COG4586 178 LDEPTIGLD 186
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
859-1067 |
3.64e-08 |
|
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: 55.80 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVVG---GDMLVDGR-----PRDssfQRKTGYVQQQDLHLHTS 930
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIKpdsGKILLNGKditnlPPE---KRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSALLRQPPQYTREEKLDYVEKVLD---LLNmRDyadaivgiPgEGLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGidhLLN-RK--------P-ETLSGGEQQRVAIARALVVNPKILL-LDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1008 PTSGLDSQTSWSICNLMETLTKN-GQAILCTIH--QPSAMLfqrFDRLLLLaKGGKTVYFGDI 1067
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHdfEEAWAL---ADKVAIM-LNGKLIQVGKP 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
836-1015 |
4.42e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.18 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 836 QTSIFHWENVCYdvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLanrttVGVV---GGDMLVDGRPRDSS 912
Cdd:PRK13635 2 KEEIIRVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL-----NGLLlpeAGTITVGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 ----FQRKTGYV-QQQDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRK 987
Cdd:PRK13635 75 tvwdVRRQVGMVfQNPDNQFVGATVQDDVAFGLENIGVP---REEMVERVDQALRQVGMEDFLNR---EPHR-LSGGQKQ 147
|
170 180
....*....|....*....|....*...
gi 1799732068 988 RLTIGVELAARPKLLLfLDEPTSGLDSQ 1015
Cdd:PRK13635 148 RVAIAGVLALQPDIII-LDEATSMLDPR 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
856-1037 |
6.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRTTVGVVG----GDMLVDGRP----RDS-SFQRKTGYVQQQDLH 926
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDKVSGyrysGDVLLGGRSifnyRDVlEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 LHTSTVREALefsALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:PRK14271 113 FPMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL-LD 188
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1007 EPTSGLDSQTSWSICNLMETLTKNGQAILCT 1037
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
856-1040 |
6.07e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaN---RTTVGVV--GGDMLVDG-RPRD-SSFQRKTGYVQQQDLH-L 927
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHL-NgllQPTSGTVtiGERVITAGkKNKKlKPLRKKVGIVFQFPEHqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVREALEFSallrqpPQ---YTREEKLDYVEKVLDLlnmrdyadaiVGIPGEGLNVE-------QRKRLTIGVELAA 997
Cdd:PRK13634 99 FEETVEKDICFG------PMnfgVSEEDAKQKAREMIEL----------VGLPEELLARSpfelsggQMRRVAIAGVLAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQ--AILCTiHQ 1040
Cdd:PRK13634 163 EPEVLV-LDEPTAGLDPKGRKEMMEMFYKLHKEKGltTVLVT-HS 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
163-375 |
6.28e-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: 53.40 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGEthgfqvdpaayinyhgITPKQMSTDFRGEAIytaevdahypqlsv 242
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----------------LKPTSGEILIDGKDI-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 gdtlyfaslaraprhlpggisSQEYATHLRDvimamfgightintRVGndFVRGVSGGERKRVTIAEAALSYAPLQCWDN 322
Cdd:cd00267 64 ---------------------AKLPLEELRR--------------RIG--YVPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 323 STRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAYnLFDKVIVLYEGH 375
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAEL-AADRVIVLKDGK 157
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
856-1041 |
8.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNRTtVGVVGGDMLVDG----------RPRDSSFQRKTGYVQQQDL 925
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRL-IEIYDSKIKVDGkvlyfgkdifQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 926 HLHTSTVREALEFSalLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfL 1005
Cdd:PRK14246 101 PFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL-M 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1799732068 1006 DEPTSGLDSQTSWSICNLMETLtKNGQAILCTIHQP 1041
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
856-1058 |
8.33e-08 |
|
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: 54.78 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPRdSSFQRKtgYvqqqdLHLHTSTV-RE 934
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEN--FYQPQGGQVLLDGKPI-SQYEHK--Y-----LHSKVSLVgQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALEFSALLRQPPQYTREEK-LDYVEKVLDLLNMRDYA-------DAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:cd03248 97 PVLFARSLQDNIAYGLQSCsFECVKEAAQKAHAHSFIselasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI-LD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1007 EPTSGLDSQTSWSI-CNLMETLTKngQAILCTIHQPSamLFQRFDRLLLLAKG 1058
Cdd:cd03248 176 EATSALDAESEQQVqQALYDWPER--RTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
855-1013 |
8.56e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnRtTVGVVGGDMLVDGRPRDSSFQR---KTGYVQQQDLHLHTS- 930
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-R-LLPPDSGEVLVDGLDVATTPSRelaKRLAILRQENHINSRl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSallRQPpqYTR----EEKLDYVEKVLDLLNMRDYADAIV-----GipgeglnveQRKRLTIGVELAARPKL 1001
Cdd:COG4604 91 TVRELVAFG---RFP--YSKgrltAEDREIIDEAIAYLDLEDLADRYLdelsgG---------QRQRAFIAMVLAQDTDY 156
|
170
....*....|..
gi 1799732068 1002 LLfLDEPTSGLD 1013
Cdd:COG4604 157 VL-LDEPLNNLD 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
866-1031 |
1.27e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVL-----ANRTTVGVVGGDMLVDGRPRDS---SFQRKTGYV-QQQDL--HLhtsTVRE 934
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVLnllemPRSGTLNIAGNHFDFSKTPSDKairELRRNVGMVfQQYNLwpHL---TVQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 alefsALLRQPPQ---YTREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLFlDEPTSG 1011
Cdd:PRK11124 102 -----NLIEAPCRvlgLSKDQALARAEKLLERLRLKPYADR---FPLH-LSGGQQQRVAIARALMMEPQVLLF-DEPTAA 171
|
170 180
....*....|....*....|
gi 1799732068 1012 LDSQTSWSICNLMETLTKNG 1031
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETG 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
843-1076 |
1.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.61 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYdvKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLanrttVGVV---GGDMLVDGRPRDSS----FQR 915
Cdd:PRK13632 11 ENVSF--SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKIL-----TGLLkpqSGEIKIDGITISKEnlkeIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYV-QQQDLHLHTSTVREALEFSALLRQ-PPQYTREEKLDYVEKVldllNMRDYADAivgipgEGLNVE--QRKRLTI 991
Cdd:PRK13632 84 KIGIIfQNPDNQFIGATVEDDIAFGLENKKvPPKKMKDIIDDLAKKV----GMEDYLDK------EPQNLSggQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 992 GVELAARPKLLLFlDEPTSGLDSQTSWSICNLMETLTKNGQAILCTI-HQPSAMLFQrfDRLLLLAKgGKTVYfgdIGRE 1070
Cdd:PRK13632 154 ASVLALNPEIIIF-DESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVFSE-GKLIA---QGKP 226
|
....*.
gi 1799732068 1071 SRILMD 1076
Cdd:PRK13632 227 KEILNN 232
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1242-1383 |
1.50e-07 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 53.28 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1242 ARERQSKTY--------SWQAFVVTNILVELAWNSIMAIFCFLVWFYPVGLfhnaeytdTLHSRSTLAFLFIWVTFLFAS 1313
Cdd:COG0842 27 AREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGV--------PLRGLSLLLLLLVLLLFALAF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1314 SLAHMLIAGI-ESEEIASSLSNILAIMMYAFCGILAGPGALPGFWIFMYRVNPFTYLVSGLLSTSLGEAPM 1383
Cdd:COG0842 99 SGLGLLISTLaRSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLGGAGL 169
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
856-1016 |
1.59e-07 |
|
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: 55.98 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLL-------DVLanrttvgvvGGDMLVDGRP-RD---SSFQRKTGYVQQqD 924
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVT---------SGRILIDGQDiRDvtqASLRAAIGIVPQ-D 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 LHLHTSTVREALEFSAllrqpPQYTREEkldyVEKVLDLLNMRDYadaIVGIP-------GE-GLNVE--QRKRLTIGVE 994
Cdd:COG5265 441 TVLFNDTIAYNIAYGR-----PDASEEE----VEAAARAAQIHDF---IESLPdgydtrvGErGLKLSggEKQRVAIART 508
|
170 180
....*....|....*....|..
gi 1799732068 995 LAARPKLLLFlDEPTSGLDSQT 1016
Cdd:COG5265 509 LLKNPPILIF-DEATSALDSRT 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
860-1015 |
1.72e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 860 DHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTvgvvGGDMLVDGRP--RDSSFQ--RKtGYVQQ-QDLHLHTS-T 931
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPT----GGTILLRGQHieGLPGHQiaRM-GVVRTfQHVRLFREmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALE-----------FSALLRQpPQYTR--EEKLDYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAAR 998
Cdd:PRK11300 97 VIENLLvaqhqqlktglFSGLLKT-PAFRRaeSEALDRAATWLERVGLLEHANRQAG----NLAYGQQRRLEIARCMVTQ 171
|
170
....*....|....*..
gi 1799732068 999 PKLLLfLDEPTSGLDSQ 1015
Cdd:PRK11300 172 PEILM-LDEPAAGLNPK 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
174-380 |
2.03e-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: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 174 GEQLCVLGPPGSGCSTFLKTIAgethGFQVDPAAYINYHGITPKQMSTDFRGEAIYTAEVDAhYPQLSVGDTLyfaSLAR 253
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQNV---GLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 254 APR-HLPggiSSQEYATHlrdVIMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYAPLQCWDNSTRGLDSANA 332
Cdd:cd03298 96 SPGlKLT---AEDRQAIE---VALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 333 VEFCRTLRTQSDVFGMTSCVAIYQaPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQ-PEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
170-380 |
2.03e-07 |
|
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: 53.45 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 170 LVLPGEQLCVLGPPGSGCSTFLKTIAGethgFQVDPAAYINYHGI----TPKQMSTDFRGEAI-YTAEVDAHYPQLSVGD 244
Cdd:cd03297 19 FDLNEEVTGIFGASGAGKSTLLRCIAG----LEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIgLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 245 TLYFAslarAPRHLPGGISSQEyathlrDVIMAMFGIGHTINTRVGndfvrGVSGGERKRVTIAEAALSYAPLQCWDNST 324
Cdd:cd03297 95 NLAFG----LKRKRNREDRISV------DELLDLLGLDHLLNRYPA-----QLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 325 RGLDSANAVEFCRTLRTQSDVFGMTsCVAIYQAPQAAYNLFDKVIVLYEGHQIYFG 380
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIP-VIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
163-330 |
2.08e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.95 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA-YINYHGitPKQMSTDFRGEAIYTAEVDAHYPQLS 241
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG-----LLPPAAgTIKLDG--GDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTLYF-ASLaraprhlpggissqeYATHLRDVIMAM--FGIGHTINTRVGNdfvrgVSGGERKRVTIAEAALSYAPLQ 318
Cdd:PRK13539 90 VAENLEFwAAF---------------LGGEELDIAAALeaVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|..
gi 1799732068 319 CWDNSTRGLDSA 330
Cdd:PRK13539 150 ILDEPTAALDAA 161
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
856-1030 |
2.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.28 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVG--VVGGDMLVDGRPRDSSFQRKTGYV-QQQDLHLHTS 930
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllKPTSGkiIIDGVDITDKKVKLSDIRKKVGLVfQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSallrqpPQYTREEKLDYVEKVLDLLNMrdyadaiVGIPGEG--------LNVEQRKRLTIGVELAARPKLL 1002
Cdd:PRK13637 100 TIEKDIAFG------PINLGLSEEEIENRVKRAMNI-------VGLDYEDykdkspfeLSGGQKRRVAIAGVVAMEPKIL 166
|
170 180
....*....|....*....|....*...
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKN 1030
Cdd:PRK13637 167 I-LDEPTAGLDPKGRDEILNKIKELHKE 193
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
841-1039 |
2.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 841 HWENVCYDVKIKS--ETRRILDhVDGWIKPGTLTALMGSSGAGKTTLLDVL-----ANRTTVGVVGGDMLVDGRPRDSSF 913
Cdd:PRK13649 4 NLQNVSYTYQAGTpfEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLnglhvPTQGSVRVDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 914 QRKT-GYV-QQQDLHLHTSTVREALEFSallrqpPQ---YTREEKLDYVEKVLdllnmrdyadAIVGI--------PGEg 980
Cdd:PRK13649 83 IRKKvGLVfQFPESQLFEETVLKDVAFG------PQnfgVSQEEAEALAREKL----------ALVGIseslfeknPFE- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799732068 981 LNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
867-1048 |
2.30e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 867 KPGTLTALMGSSGAGKTTLLDVL--ANRTTVG--VVGGDMLVDGRPRDSSFQ------------RKTGYVQQQDLHLHTS 930
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCInfLEKPSEGsiVVNGQTINLVRDKDGQLKvadknqlrllrtRLTMVFQHFNLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALEFSA-LLRQPPQYTREEKLDYVEKV-LDLLNMRDYADAIVGipgeglnvEQRKRLTIGVELAARPKLLLFlDEP 1008
Cdd:PRK10619 109 VLENVMEAPIqVLGLSKQEARERAVKYLAKVgIDERAQGKYPVHLSG--------GQQQRVSIARALAMEPEVLLF-DEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 1009 TSGLDSQTSWSICNLMETLTKNGQAILCTIHQpsaMLFQR 1048
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHE---MGFAR 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
856-1041 |
2.80e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLA--NRTTvgvvGGDMLVDGRPR---DSSFQRKTGYVQQQ-----DL 925
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAglARPD----AGEVLWQGEPIrrqRDEYHQDLLYLGHQpgiktEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 926 hlhtsTVREALEFSALLRQPpqYTREEKLDYVEKVldllNMRDYADAIVGIPGEGlnveQRKRltigVELA----ARPKL 1001
Cdd:PRK13538 90 -----TALENLRFYQRLHGP--GDDEALWEALAQV----GLAGFEDVPVRQLSAG----QQRR----VALArlwlTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 1002 LLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQP 1041
Cdd:PRK13538 151 WI-LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
858-1065 |
2.92e-07 |
|
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: 52.88 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLldVLANRTTVGVVGGDMLVDGRPRdSSFQRKTgyVQQ------QDLHLHTST 931
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRLVELSSGSILIDGVDI-SKIGLHD--LRSrisiipQDPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALE-FSallrqppQYTREEKLDYVEKV-----LDLLNMRDYADAIVGipGEGLNVEQRKRLTIGVELAARPKLLLfL 1005
Cdd:cd03244 94 IRSNLDpFG-------EYSDEELWQALERVglkefVESLPGGLDTVVEEG--GENLSVGQRQLLCLARALLRKSKILV-L 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 1006 DEPTSGLDSQTSWSICNLMETLTKNgqailCTI----HQPSAMLfqRFDRLLLLAKgGKTVYFG 1065
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAFKD-----CTVltiaHRLDTII--DSDRILVLDK-GRVVEFD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
857-1039 |
6.56e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVL--ANRTTVGVVggdmLVDGRPRdsSFQRKTGYVQQ------QDLHLH 928
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILsgNYQPDAGSI----LIDGQEM--RFASTTAALAAgvaiiyQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TS-TVREALefsaLLRQPPQytreeKLDYVEKVLDLLNMRDYADAIvgipGEGLNVEQR-KRLTIG----VELA---ARP 999
Cdd:PRK11288 92 PEmTVAENL----YLGQLPH-----KGGIVNRRLLNYEAREQLEHL----GVDIDPDTPlKYLSIGqrqmVEIAkalARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 1000 KLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
155-341 |
7.48e-07 |
|
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: 52.01 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 155 GGKKrkinILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHgfqvdPAAyinyhGITPKQMSTDFRGEAI------ 228
Cdd:COG1119 14 GGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP-----PTY-----GNDVRLFGERRGGEDVwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 229 ---YTAEVDAHYPQ-LSVGDTL---YFASLARAPRHlpggisSQEYATHLRDvIMAMFGIGHTINTRVGNdfvrgVSGGE 301
Cdd:COG1119 80 iglVSPALQLRFPRdETVLDVVlsgFFDSIGLYREP------TDEQRERARE-LLELLGLAHLADRPFGT-----LSQGE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799732068 302 RKRVTIAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRT 341
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDK 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
861-1065 |
7.83e-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: 51.34 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 861 HVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDG----------RPRDSSFQRKTGYVqqqdlHLhts 930
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtaappadRPVSMLFQENNLFA-----HL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALefsALLRQPPQYTREEKLDYVEKVLdllnmrdyadAIVGI-------PGEgLNVEQRKRLTIGVELaARPKLLL 1003
Cdd:cd03298 86 TVEQNV---GLGLSPGLKLTAEDRQAIEVAL----------ARVGLaglekrlPGE-LSGGERQRVALARVL-VRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1004 FLDEPTSGLDSQTSWSICNLMETL-TKNGQAILCTIHQPSAMLfqRFDRLLLLAKGGKTVYFG 1065
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK--RLAQRVVFLDNGRIAAQG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
856-1039 |
1.15e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVVGGDMLVDGRPRdssfQRKTGYVQQQdLHLHTSTvreA 935
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGLVAPDEGVIKRNG----KLRIGYVPQK-LYLDTTL---P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 936 LEFSALLRQPPQYTREEKLDYVEKVldllnmrdYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQ 1015
Cdd:PRK09544 84 LTVNRFLRLRPGTKKEDILPALKRV--------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV-LDEPTQGVDVN 154
|
170 180
....*....|....*....|....*
gi 1799732068 1016 TSWSICNLMETL-TKNGQAILCTIH 1039
Cdd:PRK09544 155 GQVALYDLIDQLrRELDCAVLMVSH 179
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
853-1013 |
1.22e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.38 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 853 SETRRiLDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV--GGDMLVDGRP-RDSSFQ---RKTGYVQQQDLH 926
Cdd:COG4138 7 AVAGR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-----GLLpgQGEILLNGRPlSDWSAAelaRHRAYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 LHTSTVREALEfsalLRQPPQYTREEKLDYVEKVLDLLNMRDYAD----AIVGipGEglnvEQRKRLTiGVELAARPKL- 1001
Cdd:COG4138 81 PFAMPVFQYLA----LHQPAGASSEAVEQLLAQLAEALGLEDKLSrpltQLSG--GE----WQRVRLA-AVLLQVWPTIn 149
|
170
....*....|....*.
gi 1799732068 1002 ----LLFLDEPTSGLD 1013
Cdd:COG4138 150 pegqLLLLDEPMNSLD 165
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1039-1164 |
1.28e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 52.60 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1039 HQPSAMLFQRFDRLLLLAKGGKTVYFGDIgresRILMDYFTrNGGPALPPGSNPAEH---MLEVIgAAPGAKSEIDW--- 1112
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPV----KKVEEYFA-GLGINVPERVNPPDHfidILEGI-VKPSTSSGVDYkql 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1113 PAVWRNSPEYqNVRHE-LSNLRALANQPSPISDTNEKSSYAEFAAPFATQFMQ 1164
Cdd:pfam19055 75 PVRWMLHNGY-PVPPDmLQNADGIAASSGENSSNGTNPGVGSEEQSFAGELWQ 126
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
855-1076 |
1.42e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVL--ANRTTVGVVggdmLVDGRP-RD---SSFQRKTGYVQQQDLHLH 928
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrVFDPQSGRI----LIDGTDiRTvtrASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 929 TST---------------VREALEfsallrqppqytREEKLDYVEKVLDLLnmrdyaDAIVGIPGEGLNVEQRKRLTIgv 993
Cdd:PRK13657 423 RSIednirvgrpdatdeeMRAAAE------------RAQAHDFIERKPDGY------DTVVGERGRQLSGGERQRLAI-- 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 994 elaARPKL----LLFLDEPTSGLDSQTSWSICNLMETLTKNGQAI-----LCTIHQPSAMLF---------QRFDRllLL 1055
Cdd:PRK13657 483 ---ARALLkdppILILDEATSALDVETEAKVKAALDELMKGRTTFiiahrLSTVRNADRILVfdngrvvesGSFDE--LV 557
|
250 260
....*....|....*....|.
gi 1799732068 1056 AKGGktvYFGDIGRESRILMD 1076
Cdd:PRK13657 558 ARGG---RFAALLRAQGMLQE 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
163-374 |
1.48e-06 |
|
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: 51.08 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIagethgFQV-DPAA---YINYHGITPKQMSTdFRgEAIytaevdAHYP 238
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL------FRFyDVSSgsiLIDGQDIREVTLDS-LR-RAI------GVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 239 QLSV--GDTLYF--------AS---LARAPRhlpggissqeyATHLRDVIMAM-FGIghtiNTRVGNdfvRGV--SGGER 302
Cdd:cd03253 82 QDTVlfNDTIGYnirygrpdATdeeVIEAAK-----------AAQIHDKIMRFpDGY----DTIVGE---RGLklSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 303 KRVTIAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDvfGMTSCV------AIYQApqaaynlfDKVIVLYEG 374
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIViahrlsTIVNA--------DKIIVLKDG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
174-375 |
1.51e-06 |
|
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: 49.88 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 174 GEQLCVLGPPGSGCSTFLKTIAGEthgfqvdpaayinyhgITPKQMSTDFRGEAIYTAEVDAHYPQLSVGdtLYFaslar 253
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCIAGL----------------EEPDSGSILIDGEDLTDLEDELPPLRRRIG--MVF----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 254 aprhlpggissQEYA--THLRdvimamfgightintrVGNDFVRGVSGGERKRVTIAEAALSYAPLQCWDNSTRGLDSAN 331
Cdd:cd03229 83 -----------QDFAlfPHLT----------------VLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799732068 332 AVEFCRTLRTQSDVFGMTSCVAIYQAPQAAYnLFDKVIVLYEGH 375
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAAR-LADRVVVLRDGK 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
163-328 |
1.55e-06 |
|
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: 50.00 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGEthgfqvdpaayinyhgITPKQmstdfrGEaIYTAEVDAHypqlSV 242
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGD----------------LKPQQ------GE-ITLDGVPVS----DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 GDTL--YFASLARAPrHLpggissqeYATHLRDVIMAMFgightintrvgndfvrgvSGGERKRVTIAEAALSYAPLQCW 320
Cdd:cd03247 70 EKALssLISVLNQRP-YL--------FDTTLRNNLGRRF------------------SGGERQRLALARILLQDAPIVLL 122
|
....*...
gi 1799732068 321 DNSTRGLD 328
Cdd:cd03247 123 DEPTVGLD 130
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
856-1017 |
1.64e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.24 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRP--RDSSFQRkTGYVQQ--QDLHLHTS- 930
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDSGSILIDGKDvtKLPEYKR-AKYIGRvfQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 --TVRE--ALefsALLR-QP----PQYTREEKLDYVEKVLDL-LNMRDYADAIVGIPGEGlnveQRKRLTIGVELAARPK 1000
Cdd:COG1101 96 smTIEEnlAL---AYRRgKRrglrRGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGG----QRQALSLLMATLTKPK 168
|
170
....*....|....*..
gi 1799732068 1001 LLLfLDEPTSGLDSQTS 1017
Cdd:COG1101 169 LLL-LDEHTAALDPKTA 184
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
843-1030 |
1.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYDVKIKSETRRI--LDHVDGWIKPGTLTALMGSSGAGKTTL---LDVLANRTtvgvvGGDMLVDGrpRDSS----- 912
Cdd:PRK13633 8 KNVSYKYESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPS-----EGKVYVDG--LDTSdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 --FQRKTGYV-QQQDLHLHTSTVREALEFSAL-LRQPPQYTREEkldyVEKVLDLLNMRDYADAivgiPGEGLNVEQRKR 988
Cdd:PRK13633 81 wdIRNKAGMVfQNPDNQIVATIVEEDVAFGPEnLGIPPEEIRER----VDESLKKVGMYEYRRH----APHLLSGGQKQR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799732068 989 LTIGVELAARPKLLLFlDEPTSGLDSQTSWSICNLMETLTKN 1030
Cdd:PRK13633 153 VAIAGILAMRPECIIF-DEPTAMLDPSGRREVVNTIKELNKK 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
858-1057 |
2.15e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP-RDSSFQRKTGYVQ-----QQDLhlhtST 931
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTaTRGDRSRFMAYLGhlpglKADL----ST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VrEALEFSALL--RQPPQYTreekldyvEKVLDLLNMRDYADAIVgipgEGLNVEQRKRLTIGvELAARPKLLLFLDEPT 1009
Cdd:PRK13543 100 L-ENLHFLCGLhgRRAKQMP--------GSALAIVGLAGYEDTLV----RQLSAGQKKRLALA-RLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRfDRLLLLAK 1057
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVR-TRMLTLEA 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
859-1035 |
2.27e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGR------PRDSsFQRKTGYVQQqdlHL-- 927
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY-----GLYqpdSGEILIDGKpvrirsPRDA-IALGIGMVHQ---HFml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 -HTSTVREALefsALLRQPPQYTREEKLDYVEKVLDLlnMRDY-----ADAIVgipgEGLNVEQRKRltigVE----LAA 997
Cdd:COG3845 92 vPNLTVAENI---VLGLEPTKGGRLDRKAARARIREL--SERYgldvdPDAKV----EDLSVGEQQR----VEilkaLYR 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAIL 1035
Cdd:COG3845 159 GARILI-LDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
866-1039 |
2.31e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDG----RPRDSSFQRKTGYVQQQDLHLHTSTVREALefsAL 941
Cdd:PRK10253 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAHGHVWLDGehiqHYASKEVARRIGLLAQNATTPGDITVQELV---AR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 942 LRQP--PQYT--REEKLDYVEKVLDLLNMRDYADAIVgipgEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTS 1017
Cdd:PRK10253 105 GRYPhqPLFTrwRKEDEEAVTKAMQATGITHLADQSV----DTLSGGQRQRAWIAMVLAQETAIML-LDEPTTWLDISHQ 179
|
170 180
....*....|....*....|...
gi 1799732068 1018 WSICNLMETLTK-NGQAILCTIH 1039
Cdd:PRK10253 180 IDLLELLSELNReKGYTLAAVLH 202
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
640-695 |
2.36e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 49.81 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799732068 640 LFASLTKTIQQALAPSSIILMALVLYTGFAIPVSYMRGWASWIRYLNPVAYGFEAI 695
Cdd:COG0842 104 LISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
857-1066 |
2.50e-06 |
|
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: 52.11 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRT-----TVGVVGGDMLVD-GRPRDSSFQRKTGYV----QQQDLH 926
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLeptsgEVNVRVGDEWVDmTKPGPDGRGRAKRYIgilhQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 927 LHtSTVREALEFSALLRQPPQYTReEKLDYVEKVLDLlnMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLfLD 1006
Cdd:TIGR03269 378 PH-RTVLDNLTEAIGLELPDELAR-MKAVITLKMVGF--DEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVI-LD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1007 EPTSGLDSQTSWSICN-LMETLTKNGQAILCTIHQpsaMLFQRF--DRLLLLaKGGKTVYFGD 1066
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHD---MDFVLDvcDRAALM-RDGKIVKIGD 511
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
874-1058 |
2.84e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 874 LMGSSGAGKTTLLD-----VLANRTTVGV---VGGDMLVDGRPRDSSFQRK----------TGYVQQ-QDLHLHTSTVRE 934
Cdd:PRK13631 57 IIGNSGSGKSTLVThfnglIKSKYGTIQVgdiYIGDKKNNHELITNPYSKKiknfkelrrrVSMVFQfPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALEFSALLRQPPQYTREEKLDYvekvldLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLFlDEPTSGLDS 1014
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKF------YLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF-DEPTAGLDP 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799732068 1015 QTSWSICNLMETLTKNGQAILCTIHQPSAMLfQRFDRLLLLAKG 1058
Cdd:PRK13631 210 KGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
866-1058 |
3.03e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLANrTTVGvvGGDMLVDGRP----RDSSFQRKTGYVQQQDLHLHTSTVREALEfsal 941
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAG-LLPG--SGSIQFAGQPleawSAAELARHRAYLSQQQTPPFAMPVFQYLT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 942 LRQPPQYTREEKLDYVEKVLDLLNMRDY----ADAIVGipGEGlnveQRKRLTiGVELAARPKL-----LLFLDEPTSGL 1012
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALGLDDKlgrsVNQLSG--GEW----QRVRLA-AVVLQVWPDInpagqLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 1013 D-SQTSWsICNLMETLTKNGQAILCTIHQPSAMLfQRFDRLLLLAKG 1058
Cdd:PRK03695 165 DvAQQAA-LDRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
869-1039 |
3.80e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 869 GTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDMLVDGRPRDSSFQRK-TGYVQQQdlhlhtstvrEALEFS-------- 939
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMG--FVRLASGKISILGQPTRQALQKNlVAYVPQS----------EEVDWSfpvlvedv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 940 ---------ALLRQPPQYTREekldYVEKVLDLLNMRDYADAIVGipgeGLNVEQRKRLTIGVELAARPKLLLfLDEPTS 1010
Cdd:PRK15056 101 vmmgryghmGWLRRAKKRDRQ----IVTAALARVDMVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVIL-LDEPFT 171
|
170 180
....*....|....*....|....*....
gi 1799732068 1011 GLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
858-1042 |
4.27e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLaNR----TTVGVVGGDMLVDGRPRDS------SFQRKTGYVQQQDLHL 927
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRllelNEEARVEGEVRLFGRNIYSpdvdpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 928 HTSTVRE----ALEFSALLRqpPQYTREEKLDYV-------EKVLDLLNmrDYADAIVGipgeglnvEQRKRLTIGVELA 996
Cdd:PRK14267 98 PHLTIYDnvaiGVKLNGLVK--SKKELDERVEWAlkkaalwDEVKDRLN--DYPSNLSG--------GQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1799732068 997 ARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPS 1042
Cdd:PRK14267 166 MKPKILL-MDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
157-375 |
4.65e-06 |
|
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: 49.00 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 157 KKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAgethGFQVDPAAYINYHGITPKQMSTDFRGEAIYT----AE 232
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN----GLLGPTSGEVLVDGKDLTKLSLKELRRKVGLvfqnPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 233 VdahypQLsVGDTLyFASLARAPRHLpgGISSQEyATHLRDVIMAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAeAAL 312
Cdd:cd03225 86 D-----QF-FGPTV-EEEVAFGLENL--GLPEEE-IEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIA-GVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 313 SYAP----LqcwDNSTRGLDSANAVEFCRTLRT-QSDvfGMTSCVAIYQaPQAAYNLFDKVIVLYEGH 375
Cdd:cd03225 150 AMDPdillL---DEPTAGLDPAGRRELLELLKKlKAE--GKTIIIVTHD-LDLLLELADRVIVLEDGK 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
163-375 |
5.66e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 48.68 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG-----ETHGfqvdpaaYINYHGITPKQMSTDFRGEAiytaevdahy 237
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyeVTEG-------EILFKGEDITDLPPEERARL---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 238 pqlsvGDTLYFASLARAPrhlpgGISSQEYathLRDVimamfgightintrvgNDfvrGVSGGERKRVTIAEAALSYAPL 317
Cdd:cd03217 78 -----GIFLAFQYPPEIP-----GVKNADF---LRYV----------------NE---GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 318 QCWDNSTRGLDSAN---AVEFCRTLRTQsdvfGMTSCVAIYQAPQAAYNLFDKVIVLYEGH 375
Cdd:cd03217 126 AILDEPDSGLDIDAlrlVAEVINKLREE----GKSVLIITHYQRLLDYIKPDRVHVLYDGR 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
872-1013 |
5.75e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 872 TALMGSSGAGKTTLLDVLANRTT--VG--VVGGDMLVDGRPRDS--SFQRKTGYVQQqdlhlhtstvrEALEFsallrqp 945
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRpqKGriVLNGRVLFDAEKGIClpPEKRRIGYVFQ-----------DARLF------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 946 PQYTREEKLDY-VEKVldllnMRDYADAIVGIPGEG---------LNVEQRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK11144 89 PHYKVRGNLRYgMAKS-----MVAQFDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLL-MDEPLASLD 160
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
173-310 |
6.02e-06 |
|
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: 49.06 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 173 PGEQLCVLGPPGSGCSTFLKTIAgethGFQVDPAAYINYHGitpkqmsTDFRGEAIYTAEV------DAHYPQLSVGDTL 246
Cdd:cd03259 25 PGEFLALLGPSGCGKTTLLRLIA----GLERPDSGEILIDG-------RDVTGVPPERRNIgmvfqdYALFPHLTVAENI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 247 YFAsLARaprhlpGGISSQEYATHLRDvIMAMFGIGHTINTRvgndfVRGVSGGERKRVTIAEA 310
Cdd:cd03259 94 AFG-LKL------RGVPKAEIRARVRE-LLELVGLEGLLNRY-----PHELSGGQQQRVALARA 144
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
848-1013 |
7.22e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.94 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrTTVGVVGGDMLVDGrpRDSSFQRKTGYVQQ----- 922
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA--SLISPTSGTLLFEG--EDISTLKPEIYRQQvsyca 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 QDLHLHTSTVREALEFSALLR-QPPQytreekldyVEKVLDLLNMRDYADAIVGIPGEGLNVEQRKRLTIGVELAARPKL 1001
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPWQIRnQQPD---------PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|..
gi 1799732068 1002 LLfLDEPTSGLD 1013
Cdd:PRK10247 159 LL-LDEITSALD 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
848-1013 |
8.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvVGGDMLVDGRPRDS-----SFQRKTGYVQQ 922
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQG-YSNDLTLFGRRRGSgetiwDIKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 923 QdLHLH---TSTVREAL-----EFSALLRQPPQytREEKLdyVEKVLDLLNMRDY-ADAivgiPGEGLNVEQRKRLTIGV 993
Cdd:PRK10938 344 S-LHLDyrvSTSVRNVIlsgffDSIGIYQAVSD--RQQKL--AQQWLDILGIDKRtADA----PFHSLSWGQQRLALIVR 414
|
170 180
....*....|....*....|
gi 1799732068 994 ELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK10938 415 ALVKHPTLLI-LDEPLQGLD 433
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
823-1016 |
9.54e-06 |
|
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: 48.75 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 823 HSEGPDSTIGVEKQTSIfhwENVCydVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLldVLANRTTVGVVGGDM 902
Cdd:cd03288 6 SGSSNSGLVGLGGEIKI---HDLC--VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 903 LVDGrprdssfqrktgyVQQQDLHLHTSTVR------EALEFSALLR---QPPQYTREEKLDYVEKVLDLLNMRDY---- 969
Cdd:cd03288 79 VIDG-------------IDISKLPLHTLRSRlsiilqDPILFSGSIRfnlDPECKCTDDRLWEALEIAQLKNMVKSlpgg 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 970 ADAIVGIPGEGLNVEQRKRLTIGVELaARPKLLLFLDEPTSGLDSQT 1016
Cdd:cd03288 146 LDAVVTEGGENFSVGQRQLFCLARAF-VRKSSILIMDEATASIDMAT 191
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
163-328 |
1.07e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGETHGfqvdPAAYINYHGitpKQMSTDFRGEAI-YTAEVDAHYPQLS 241
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHV----ESGQIQIDG---KTATRGDRSRFMaYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTLYF--ASLARAPRHLPGGIssqeyathlrdviMAMFGIGHTINTrvgndFVRGVSGGERKRVTIAEAALSYAPLQC 319
Cdd:PRK13543 99 TLENLHFlcGLHGRRAKQMPGSA-------------LAIVGLAGYEDT-----LVRQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 1799732068 320 WDNSTRGLD 328
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
860-1013 |
1.36e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 860 DHVDGWIKPGTLTALMGSSGAGKTT-------LLDVLAnrttvgvvgGDMLVDGRP---RDSSFQRKTGYVQQ-----QD 924
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASE---------GEAWLFGQPvdaGDIATRRRVGYMSQafslyGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 925 LhlhtsTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAIvgiPgEGLNVEQRKRLTIGVELAARPKLLLf 1004
Cdd:NF033858 354 L-----TVRQNLELHARLFHLP---AAEIAARVAEMLERFDLADVADAL---P-DSLPLGIRQRLSLAVAVIHKPELLI- 420
|
....*....
gi 1799732068 1005 LDEPTSGLD 1013
Cdd:NF033858 421 LDEPTSGVD 429
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
848-1039 |
1.39e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGR------PRDSS-------FQ 914
Cdd:CHL00131 12 NLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGEsildlePEERAhlgiflaFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 915 RK---TGYVQQQDLHLHTSTVREALEFSALlrQPPQYtreekLDYVEKVLDLLNM------RDYADAIVGipGEglnveq 985
Cdd:CHL00131 92 YPieiPGVSNADFLRLAYNSKRKFQGLPEL--DPLEF-----LEIINEKLKLVGMdpsflsRNVNEGFSG--GE------ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 986 RKRLTIgVELAARPKLLLFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:CHL00131 157 KKRNEI-LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
857-1058 |
1.90e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.57 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAN--RTTVG-VVGGDMLVDGRPRDSSFQRKTGYVQQQDLHLHTSTVR 933
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSGrIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 934 EALEFSALLRQPPQYtrEEKLDYVEKVLDLLNMRDYADAIVGIPGEglnveqRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK11614 99 ENLAMGGFFAERDQF--QERIKWVYELFPRLHERRIQRAGTMSGGE------QQMLAIGRALMSQPRLLL-LDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799732068 1014 SQTSWSICNLMETLTKNGQAILcTIHQPSAMLFQRFDRLLLLAKG 1058
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
843-1040 |
2.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 843 ENVCYdvkIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLdvlanRTTVGVV---GGDMLVDGRPRDSS----FQR 915
Cdd:PRK13652 7 RDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLF-----RHFNGILkptSGSVLIRGEPITKEnireVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 916 KTGYV-QQQDLHLHTSTVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAIvgipGEGLNVEQRKRLTIGVE 994
Cdd:PRK13652 79 FVGLVfQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHR---VSSALHMLGLEELRDRV----PHHLSGGEKKRVAIAGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 995 LAARPKLLLfLDEPTSGLDSQTSWSICNLMETLTKN-GQAILCTIHQ 1040
Cdd:PRK13652 152 IAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
156-384 |
2.39e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 47.70 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 156 GKKRkinILQGLDgLVLP-GEQLCVLGPPGSGCSTFLKTIAgethgfqvdpaaYINyhgiTPKQMSTDFRGEAIytaevd 234
Cdd:PRK11231 13 GTKR---ILNDLS-LSLPtGKITALIGPNGCGKSTLLKCFA------------RLL----TPQSGTVFLGDKPI------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 235 AHYpqlsvGDTLYFASLARAPRHL--PGGISSQEYAT------------------HLRDVIMAMFGIGHTINTRVGNdfv 294
Cdd:PRK11231 67 SML-----SSRQLARRLALLPQHHltPEGITVRELVAygrspwlslwgrlsaednARVNQAMEQTRINHLADRRLTD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 295 rgVSGGERKRVTIAEAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAA-YnlFDKVIVLYE 373
Cdd:PRK11231 139 --LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASrY--CDHLVVLAN 213
|
250
....*....|.
gi 1799732068 374 GHQIYFGAAHD 384
Cdd:PRK11231 214 GHVMAQGTPEE 224
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1242-1388 |
2.98e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 48.16 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1242 ARERQSKTYSWQ--------AFVVTNILVELAWNSIMAIFCFLVWFYPVGLFHNaeytdtlhsrSTLAFLFIWVTFLFAS 1313
Cdd:pfam12698 184 VEEKESRIKERLlvsgvsplQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGN----------LGLLLLLFLLYGLAYI 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 1314 SLAHMLIAGIESEEIASSLSNILAIMMYAFCGILAGPGALPGFWIFMYRVNPFTYLVSGLLSTSLGEAPMYCAEN 1388
Cdd:pfam12698 254 ALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWEIAPS 328
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
844-1014 |
3.02e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 844 NVC--Y-DVKIKSetrrildHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDG-RPRD-SSFQRKTG 918
Cdd:PRK11000 8 NVTkaYgDVVISK-------DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEkRMNDvPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 919 YV-QQQDLHLHTStVREALEFSALLRQPPQYTREEKLDYVEKVLD---LLNMRDYAdaivgipgegLNVEQRKRLTIGVE 994
Cdd:PRK11000 79 MVfQSYALYPHLS-VAENMSFGLKLAGAKKEEINQRVNQVAEVLQlahLLDRKPKA----------LSGGQRQRVAIGRT 147
|
170 180
....*....|....*....|
gi 1799732068 995 LAARPKLLLfLDEPTSGLDS 1014
Cdd:PRK11000 148 LVAEPSVFL-LDEPLSNLDA 166
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
859-1040 |
4.25e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGRP------RDSsfQRKTGYVQQQDLHLHTS-T 931
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPlkasniRDT--ERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREAL----EFS---ALLRQPPQYTREEKLDYVEKVLDLLNMRDYADAIVGipgeglnveQRKRLTIGVELAARPKLLLf 1004
Cdd:TIGR02633 95 VAENIflgnEITlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGG---------QQQLVEIAKALNKQARLLI- 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1799732068 1005 LDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQ 1040
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
868-1068 |
4.73e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 868 PGTLTALMGSSGAGKTTLLDVLAN--RTTVGVVggdmLVDGRPRDSS-------FQRKTGYVQQQDLHLHTSTVREALEF 938
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGllRPQKGAV----LWQGKPLDYSkrgllalRQQVATVFQDPEQQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 939 SalLRQPpQYTREEKLDYVEKVLDLLNMRDYADAivgiPGEGLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLDSQTSW 1018
Cdd:PRK13638 102 S--LRNL-GVPEAEITRRVDEALTLVDAQHFRHQ----PIQCLSHGQKKRVAIAGALVLQARYLL-LDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799732068 1019 SICNLMETLTKNGQAILCTIHQPSaMLFQRFDRLLLLAKgGKTVYFGDIG 1068
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDID-LIYEISDAVYVLRQ-GQILTHGAPG 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
160-313 |
5.59e-05 |
|
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: 46.27 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 160 KINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDPAA-YINYHG--ITPkqMSTDFRGEA--IYTAEVD 234
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG-----LLPPRSgSIRFDGrdITG--LPPHERARAgiGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 235 AHYPQLSVGDTLYFASLARAPRHLPGGIssqeyathlrDVIMAMFGIGHTI-NTRVGNdfvrgVSGGERKRVTIAEAALS 313
Cdd:cd03224 85 RIFPELTVEENLLLGAYARRRAKRKARL----------ERVYELFPRLKERrKQLAGT-----LSGGEQQMLAIARALMS 149
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
857-1012 |
5.84e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLAnrttvGVV---GGDMLVDGRPR---DSSFQRKTG-YVQQQDLHLHT 929
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVppdSGTLEIGGNPCarlTPAKAHQLGiYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 S-TVREALefsaLLRQPPQYTREEKLdyvEKVLDLLNMRDYADAIVGIpgegLNVEQRKRLTI--GVELAARpklLLFLD 1006
Cdd:PRK15439 100 NlSVKENI----LFGLPKRQASMQKM---KQLLAALGCQLDLDSSAGS----LEVADRQIVEIlrGLMRDSR---ILILD 165
|
....*.
gi 1799732068 1007 EPTSGL 1012
Cdd:PRK15439 166 EPTASL 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
158-384 |
7.51e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 158 KRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGE------THGFQVDPAAYIN---YHGITPKQMStdfRGEAI 228
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaPRGARVTGDVTLNgepLAAIDAPRLA---RLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 229 YTAEVDAHYPqLSVGDTLyfaSLARAPRHLPGGissqEYATHLRDVIMAMFGIGHTiNTRVGNDfVRGVSGGERKRVTIA 308
Cdd:PRK13547 88 LPQAAQPAFA-FSAREIV---LLGRYPHARRAG----ALTHRDGEIAWQALALAGA-TALVGRD-VTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 309 ---------EAALSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMtSCVAIYQAPQAAYNLFDKVIVLYEGHQIYF 379
Cdd:PRK13547 158 rvlaqlwppHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNL-GVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
....*
gi 1799732068 380 GAAHD 384
Cdd:PRK13547 237 GAPAD 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
849-1045 |
9.51e-05 |
|
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: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 849 VKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgvVGGDMLVDGRPRDS-SFQ--RKTGYVQQQDL 925
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS---TEGEIQIDGVSWNSvTLQtwRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 926 HLHTSTVREALEFSAllrqppQYTREEkldyVEKVLDLLNMR-------DYADAIVGIPGEGLNVEQRKRLTIGVELAAR 998
Cdd:TIGR01271 1302 FIFSGTFRKNLDPYE------QWSDEE----IWKVAEEVGLKsvieqfpDKLDFVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 999 PKLLLfLDEPTSGLDSQTSWSICNLMETLTKNGQAILCTiHQPSAML 1045
Cdd:TIGR01271 1372 AKILL-LDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE-HRVEALL 1416
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
167-337 |
9.92e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 167 LDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgfqvdpaayinyhgITPKQMSTDFRGEAI--YTAEVDAHYpqlsvgd 244
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-----------------LLPGSGSIQFAGQPLeaWSAAELARH------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 245 TLYFASLARAP----------RHLPGGISSQEYATHLRDVImAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAAL-- 312
Cdd:PRK03695 71 RAYLSQQQTPPfampvfqyltLHQPDKTRTEAVASALNEVA-EALGLDDKLGRSVNQ-----LSGGEWQRVRLAAVVLqv 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1799732068 313 -----SYAPLQCWDNSTRGLDSANAV-------EFCR 337
Cdd:PRK03695 145 wpdinPAGQLLLLDEPMNSLDVAQQAaldrllsELCQ 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
857-1033 |
1.45e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 857 RILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGVVGGDMLVDGRP------RDSsfQRKTGYVQQQDLHLhts 930
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEElqasniRDT--ERAGIAIIHQELAL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 tVRE--ALEFSALLRQPpqyTREEKLDY------VEKVLDLLNMrdyaDAIVGIPGEGLNVEQRKRLTIGVELAARPKLL 1002
Cdd:PRK13549 94 -VKElsVLENIFLGNEI---TPGGIMDYdamylrAQKLLAQLKL----DINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190
....*....|....*....|....*....|.
gi 1799732068 1003 LfLDEPTSGLDSQTSWSICNLMETLTKNGQA 1033
Cdd:PRK13549 166 I-LDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
174-375 |
1.52e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.85 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 174 GEQLCVLGPPGSGCSTFLKTIAGETHgfqvDPAAYINYHGITPKQMSTDFRgeaiYTAEVDAHYP---QLSVGDTLYFAs 250
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEH----QTSGHIRFHGTDVSRLHARDR----KVGFVFQHYAlfrHMTVFDNIAFG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 251 LARAPRH-LPGGISSQEYATHLRDvimaMFGIGHtintrVGNDFVRGVSGGERKRVTIAEaALSYAP-LQCWDNSTRGLD 328
Cdd:PRK10851 99 LTVLPRReRPNAAAIKAKVTQLLE----MVQLAH-----LADRYPAQLSGGQKQRVALAR-ALAVEPqILLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799732068 329 SANAVEFCRTLRTQSDVFGMTScVAIYQAPQAAYNLFDKVIVLYEGH 375
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTS-VFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
167-375 |
2.16e-04 |
|
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: 43.54 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 167 LDGL---VLPGEQLCVLGPPGSGCSTFLKTIAGethgfQVDP-AAYINYHGITPKQMSTDFRGEAIYTAEVDAHYPQLSV 242
Cdd:cd03230 16 LDDIsltVEKGEIYGLLGPNGAGKTTLIKIILG-----LLKPdSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 243 GDTLYFaslaraprhlpggissqeyathlrdvimamfgightintrvgndfvrgvSGGERKRVTIAEAALSYAPLQCWDN 322
Cdd:cd03230 91 RENLKL-------------------------------------------------SGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 323 STRGLDSANAVEFCRTLRTQSD----VFgMTSCVaiyqaPQAAYNLFDKVIVLYEGH 375
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKegktIL-LSSHI-----LEEAERLCDRVAILNNGR 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
154-348 |
2.18e-04 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 44.02 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 154 LGGKKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGethgFQVDPAAYINYHGITPKQMSTDFRGEAIYTAEV 233
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG----LSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 234 DAHYPQLSVGDTLYFAslaraprHLPGGISSQEYAthLRDVIMAmfGIGHTIntrvgndfVRGVSGGERKRVTIAEAALS 313
Cdd:cd03231 82 PGIKTTLSVLENLRFW-------HADHSDEQVEEA--LARVGLN--GFEDRP--------VAQLSAGQQRRVALARLLLS 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1799732068 314 YAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGM 348
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGM 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
856-1020 |
2.92e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRPRDSsfqrktgyvqqqdlhLHTSTVREA 935
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPLSS---------------LSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 936 LefsALLRQPPQYTREEKLDYV--------EKVLDLLNMRDYADAIVGIP----------GEGLNVEQRKRLTIGVELAA 997
Cdd:PRK10790 417 V---AMVQQDPVVLADTFLANVtlgrdiseEQVWQALETVQLAELARSLPdglytplgeqGNNLSVGQKQLLALARVLVQ 493
|
170 180
....*....|....*....|...
gi 1799732068 998 RPKLLLfLDEPTSGLDSQTSWSI 1020
Cdd:PRK10790 494 TPQILI-LDEATANIDSGTEQAI 515
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
855-1059 |
3.60e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 855 TRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGvvGGDMLVDGRP----RDSSFQRKTGYVQQQDLhLHTS 930
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS--EGDIRFHDIPltklQLDSWRSRLAVVSQTPF-LFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 TVREALefsALLRqpPQYTREEkldyVEKVLDLLNMRD--------YaDAIVGIPGEGLNVEQRKRLTIgvelaARPKLL 1002
Cdd:PRK10789 404 TVANNI---ALGR--PDATQQE----IEHVARLASVHDdilrlpqgY-DTEVGERGVMLSGGQKQRISI-----ARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 1003 ----LFLDEPTSGLDSQTSWSIcnlMETLTKNGQ--AILCTIHQPSAMlfQRFDRLLLLAKGG 1059
Cdd:PRK10789 469 naeiLILDDALSAVDGRTEHQI---LHNLRQWGEgrTVIISAHRLSAL--TEASEILVMQHGH 526
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
866-1035 |
4.16e-04 |
|
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: 42.80 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLANRTTVgvVGGDMLVDGR------PRDSsFQRKTGYV---QQQDLHLHTSTVREAL 936
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPP--ASGEITLDGKpvtrrsPRDA-IRAGIAYVpedRKREGLVLDLSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 937 EFSALLrqppqytreekldyvekvldllnmrdyadaivgipgEGLNveQRKrLTIGVELAARPKLLLfLDEPTSGLDSQT 1016
Cdd:cd03215 100 ALSSLL------------------------------------SGGN--QQK-VVLARWLARDPRVLI-LDEPTRGVDVGA 139
|
170
....*....|....*....
gi 1799732068 1017 SWSICNLMETLTKNGQAIL 1035
Cdd:cd03215 140 KAEIYRLIRELADAGKAVL 158
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
179-406 |
6.65e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.11 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 179 VLGPPGSGCSTFLKTIAG--ETHGFQVDPAAYINYHGITPKQM-STDFRGEAIYTAEVDAHYPQLSVGDTLYFASLARap 255
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRliEIYDSKIKVDGKVLYFGKDIFQIdAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 256 rhlpgGISSQEYATHLRDVIMAMFGIGHTINTRVgNDFVRGVSGGERKRVTIAEAALSYAPLQCWDNSTRGLDSANAVEF 335
Cdd:PRK14246 119 -----GIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 336 CRTLrtqSDVFGMTSCVAIYQAPQAAYNLFDKVIVLYEGHQIYFGAAHDAkayferlgFLCPESQTTADFL 406
Cdd:PRK14246 193 EKLI---TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI--------FTSPKNELTEKYV 252
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
856-1013 |
8.12e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 856 RRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANrtTVGVVGGDM-LVDGrprdssfqRKTGYVQQQDLHLHTStvrE 934
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIgLAKG--------IKLGYFAQHQLEFLRA---D 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 935 ALEFSALLRQPPQYTREEKLDYV-------EKVLDllnmrdyadaivgiPGEGLNVEQRKRLTIGVELAARPKLLLfLDE 1007
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLRDYLggfgfqgDKVTE--------------ETRRFSGGEKARLVLALIVWQRPNLLL-LDE 456
|
....*.
gi 1799732068 1008 PTSGLD 1013
Cdd:PRK10636 457 PTNHLD 462
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
859-1039 |
9.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.89 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLD-----VLANRTTVGVVGGDMLVD-GRPRDSSFQRKTGYV-QQQDLHLHTST 931
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQhfnalLKPSSGTITIAGYHITPEtGNKNLKKLRKKVSLVfQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 932 VREALEFSAL-LRQPPQYTREEKLDYVEKV-LDllnmrdyADAIVGIPGEgLNVEQRKRLTIGVELAARPKLLLfLDEPT 1009
Cdd:PRK13641 103 VLKDVEFGPKnFGFSEDEAKEKALKWLKKVgLS-------EDLISKSPFE-LSGGQMRRVAIAGVMAYEPEILC-LDEPA 173
|
170 180 190
....*....|....*....|....*....|
gi 1799732068 1010 SGLDSQTSWSICNLMETLTKNGQAILCTIH 1039
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
837-1013 |
1.01e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.80 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 837 TSIFHWENVCYDVKiKSETRRILDHVDGWIKPGTLTALMGSSGAGKTT---LLDVLANRTTvgvvgGDMLVDGRPRDSS- 912
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAES-----GQIIIDGDLLTEEn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 913 ---FQRKTGYV-QQQDLHLHTSTVREALEFSALLRQPPqytREEKLDYVEKVLDLLNMRDYADAivgIPGEgLNVEQRKR 988
Cdd:PRK13650 76 vwdIRHKIGMVfQNPDNQFVGATVEDDVAFGLENKGIP---HEEMKERVNEALELVGMQDFKER---EPAR-LSGGQKQR 148
|
170 180
....*....|....*....|....*
gi 1799732068 989 LTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK13650 149 VAIAGAVAMRPKIII-LDEATSMLD 172
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
866-1013 |
1.14e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKTTLLDVLaNRtTVGVVGGDMLVDG----RPRDSSF----QRKTGYVQQQDLHLHTSTVREALE 937
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLL-NR-LIEPTRGQVLIDGvdiaKISDAELrevrRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799732068 938 FSALLRQPPQYTREEK-LDYVEKVldllNMRDYADaivGIPGEgLNVEQRKRLTIGVELAARPKLLLfLDEPTSGLD 1013
Cdd:PRK10070 129 FGMELAGINAEERREKaLDALRQV----GLENYAH---SYPDE-LSGGMRQRVGLARALAINPDILL-MDEAFSALD 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
844-1058 |
1.40e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 844 NVCYDVKIKSETrriLDHVDGWIKPGTLTALMGSSGAGKTTLLDVlanrttvgvvggdMLVDGRPRDSS---FQRKTGYV 920
Cdd:PLN03232 621 YFSWDSKTSKPT---LSDINLEIPVGSLVAIVGGTGEGKTSLISA-------------MLGELSHAETSsvvIRGSVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 921 QQQDLhLHTSTVREALEFSALLrQPPQYTREEKLDYVEKVLDLLNMRDYADaiVGIPGEGLNVEQRKRLTIGVELAARPK 1000
Cdd:PLN03232 685 PQVSW-IFNATVRENILFGSDF-ESERYWRAIDVTALQHDLDLLPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799732068 1001 LLLFlDEPTSGLDSQTSWSICN-LMETLTKNGQAILCT--IHqpsamLFQRFDRLLLLAKG 1058
Cdd:PLN03232 761 IYIF-DDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
163-310 |
1.51e-03 |
|
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: 41.84 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAgethGFQVDPAAYINYHG--ITP-----KQMSTDFRGEAIytaevda 235
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETPTSGEILLDGkdITNlpphkRPVNTVFQNYAL------- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 236 hYPQLSVGDTLYFAsLARapRHLPGGISSQEYATHLRDVIMAMFgightintrvGNDFVRGVSGGERKRVTIAEA 310
Cdd:cd03300 84 -FPHLTVFENIAFG-LRL--KKLPKAEIKERVAEALDLVQLEGY----------ANRKPSQLSGGQQQRVAIARA 144
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
164-386 |
1.57e-03 |
|
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: 41.59 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 164 LQGLDGLVLPGEQLCVLGPPGSG-------CSTFLKTIAGETH--GFQV--DPAAYINYHGITPKQMSTDfrgeaiytae 232
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGktttikmLTTLLKPTSGRATvaGHDVvrEPREVRRRIGIVFQDLSVD---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 233 vdahyPQLSVGDTLY-FASLAraprhlpgGISSQEYATHLRDVImAMFGIGHTINTRVGNdfvrgVSGGERKRVTIAEAA 311
Cdd:cd03265 86 -----DELTGWENLYiHARLY--------GVPGAERRERIDELL-DFVGLLEAADRLVKT-----YSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 312 LSYAPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGMTSCVAIYQAPQAAyNLFDKVIVLYEGHQIYFGAAHDAK 386
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAE-QLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
162-380 |
1.61e-03 |
|
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: 41.50 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 162 NILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGEThgfQVDpAAYINYHGitpKQMSTDFRGEAIYTAEVDAHYPQLS 241
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPD-SGEVLFDG---KPLDIAARNRIGYLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 242 VGDTL-YFASLARAPRHlpggissqeYATHLRDVIMAMFGIGHTINTRvgndfVRGVSGGERKRVTIAEAALSYAPLQCW 320
Cdd:cd03269 87 VIDQLvYLAQLKGLKKE---------EARRRIDEWLERLELSEYANKR-----VEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 321 DNSTRGLDSANAVEFCRTLRTQSDVfGMTSCVAIYQAPQAAyNLFDKVIVLYEGHQIYFG 380
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVE-ELCDRVLLLNKGRAVLYG 210
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
859-934 |
1.78e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVL--ANRTTVGVVGGDmlvDGRPRdssfqrktgyvqqqdlhlHTSTVRE 934
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALlgEEVQKTGAVRED---DSKGR------------------HTTTHRE 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
163-211 |
1.80e-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: 40.12 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGE---THGF-QVDPAAYINY 211
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepDEGIvTWGSTVKIGY 67
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
986-1037 |
2.03e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1799732068 986 RKRLTIGVELAARPKLLlFLDEPTSGLDSQTSWSICNLMETLTKNGQAILCT 1037
Cdd:NF000106 150 RRRLDLAASMIGRPAVL-YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
847-938 |
2.21e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.60 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 847 YDV-KIKSETRRILDHVDGWIKPGTlTALMGSSGAGKTTLLDVLANRTT--VGVVGGDmlvDGRPRdssfqrktgyvqqq 923
Cdd:pfam03193 84 YPVlFVSAKTGEGIEALKELLKGKT-TVLAGQSGVGKSTLLNALLPELDlrTGEISEK---LGRGR-------------- 145
|
90
....*....|....*
gi 1799732068 924 dlhlHTSTVREALEF 938
Cdd:pfam03193 146 ----HTTTHVELFPL 156
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
874-937 |
2.37e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 40.81 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799732068 874 LMGSSGAGKTTLL----DVLANRTTVGVVGGDMLVDgrpRDSSFQRKTGY-VQQ----QDLHLHTSTVREALE 937
Cdd:COG0378 18 LMGSPGSGKTTLLektiRALKDRLRIAVIEGDIYTT---EDAERLRAAGVpVVQintgGCCHLDASMVLEALE 87
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
155-197 |
2.44e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 42.36 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1799732068 155 GGKKrkinILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAGE 197
Cdd:COG0488 326 GDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
155-196 |
2.53e-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: 40.92 E-value: 2.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1799732068 155 GGKKRKINILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG 196
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG 52
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
866-1058 |
2.61e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 866 IKPGTLTALMGSSGAGKT-TLLDV--LANRTTVGVVGGDMLVDGRPR---------DSSFQRKTG----YVQQQDLhlhT 929
Cdd:PRK10261 39 LQRGETLAIVGESGSGKSvTALALmrLLEQAGGLVQCDKMLLRRRSRqvielseqsAAQMRHVRGadmaMIFQEPM---T 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 930 S-----TVREALEFSALLRQppQYTREEKLDYVEKVLDLLNMRDyADAIVGIPGEGLNVEQRKRLTIGVELAARPKLLLf 1004
Cdd:PRK10261 116 SlnpvfTVGEQIAESIRLHQ--GASREEAMVEAKRMLDQVRIPE-AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1799732068 1005 LDEPTSGLDSQTSWSICNLMETLTKNGQAILCTIHQPSAMLFQRFDRLLLLAKG 1058
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
851-897 |
2.65e-03 |
|
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: 40.83 E-value: 2.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1799732068 851 IKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTVGV 897
Cdd:pfam13481 15 LAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGK 61
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
847-938 |
2.72e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 847 YDV-KIKSETRRILDHVDGWIKPGTlTALMGSSGAGKTTLLDVL---ANRTTVGVVGgdmlVDGRPRdssfqrktgyvqq 922
Cdd:cd01854 63 YPVlAVSAKTGEGLDELRELLKGKT-SVLVGQSGVGKSTLLNALlpeLVLATGEISE----KLGRGR------------- 124
|
90
....*....|....*.
gi 1799732068 923 qdlhlHTSTVREALEF 938
Cdd:cd01854 125 -----HTTTHRELFPL 135
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
163-208 |
2.82e-03 |
|
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: 40.28 E-value: 2.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG---ETHG---------FQVDPAAY 208
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllrPTSGrvrldgadiSQWDPNEL 74
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
858-1013 |
2.86e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 858 ILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgVVGGDMLVDGR------PRDssfqRKTGYV-QQQDLHLHTS 930
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER--ITSGEIWIGGRvvnelePAD----RDIAMVfQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799732068 931 tVREALEFSALLRQPPQYTREEKldyVEKVLDLLNMRDYADAivgIPGEgLNVEQRKRLTIGVELAARPKLLLFlDEPTS 1010
Cdd:PRK11650 93 -VRENMAYGLKIRGMPKAEIEER---VAEAARILELEPLLDR---KPRE-LSGGQRQRVAMGRAIVREPAVFLF-DEPLS 163
|
...
gi 1799732068 1011 GLD 1013
Cdd:PRK11650 164 NLD 166
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
163-199 |
3.58e-03 |
|
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: 40.59 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1799732068 163 ILQGLDGLVLPGEQLCVLGPPGSGCSTFLKTIAG-ETH 199
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEP 52
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| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
859-889 |
9.27e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 9.27e-03
10 20 30
....*....|....*....|....*....|.
gi 1799732068 859 LDHVDGWIKPGTLTALMGSSGAGKTTLLDVL 889
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCL 44
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
848-922 |
9.36e-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: 38.20 E-value: 9.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799732068 848 DVKIKSETRRILDHVDGWIKPGTLTALMGSSGAGKTTLLDVLANRTTvgvvggdmLVDGRPRDSSfQRKTGYVQQ 922
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE--------PDEGIVTWGS-TVKIGYFEQ 70
|
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