|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
165-662 |
2.05e-163 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 485.54 E-value: 2.05e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 165 LMTEPTLPIYLKFAEVKYKVAVKGT-------------------------PREILSGISGSAAPGEVLALMGPSGSGKTT 219
Cdd:PLN03211 30 LLLSSCYPITLKFMDVCYRVKFENMknkgsnikrilghkpkisdetrqiqERTILNGVTGMASPGEILAVLGPSGSGKST 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 220 LLSILGGRVAGPGdVEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRLPRTMTRQEKEERTIDIIYE 299
Cdd:PLN03211 110 LLNALAGRIQGNN-FTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 300 LGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSS 379
Cdd:PLN03211 189 LGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 380 RLFHKFDKLILLGRGSLLYFGKASEAMPYFQSIGCTPLIAMNPAEFLLDLANGNTTDVSVpSELDdkvhmenqnlqtntk 459
Cdd:PLN03211 269 RVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGV-SERE--------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 460 ndyKPsaqDVHEYLVDAYENRVAYKAKKQLLDPLPISDDMKTTITSSKREWGTS-------WWQQYSILFCRGIKERRHD 532
Cdd:PLN03211 333 ---KP---NVKQSLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSdrisistWFNQFSILLQRSLKERKHE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 533 YLSWMRITQVIATSVILGLLWWHSDpstPKGLQDQAGLLFFIAVFWGFFPVFTAIFTFPQERAMLNKERAADMYKLSAYF 612
Cdd:PLN03211 407 SFNTLRVFQVIAAALLAGLMWWHSD---FRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYF 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1002256437 613 LARTTSDLPLDLFLPVIFMVIVYFMAGLKATAAHFFLSMLTVFLSIIAAQ 662
Cdd:PLN03211 484 MARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQ 533
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
191-662 |
1.39e-123 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 381.32 E-value: 1.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKSLNRRI-GFVTQDDVLFTHLTVK 269
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMIG-GSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:TIGR00955 118 EHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGKASEAMPYFQSIGCTPLIAMNPAEFLLD 428
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 429 LANGnttdvsVPSelddkvhmenqnlqtntkndYKPSAQDVHEYLVDAYENRVAYKAKKQL--LDPLPISDDMKTTITSS 506
Cdd:TIGR00955 278 VLAV------IPG--------------------SENESRERIEKICDSFAVSDIGRDMLVNtnLWSGKAGGLVKDSENME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 507 KREWGTSWWQQYSILFCRGIKE-RRHDYLSWMRITQVIATSVILGLLWWHSDPsTPKGLQDQAGLLFFIAVFWGFFPVFT 585
Cdd:TIGR00955 332 GIGYNASWWTQFYALLKRSWLSvLRDPLLLKVRLIQTMMTAILIGLIYLGQGL-TQKGVQNINGALFLFLTNMTFQNVFP 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 586 AIFTFPQERAMLNKERAADMYKLSAYFLARTTSDLPLDLFLPVIFMVIVYFMAGLKATAAHFFLSMLTVFLSIIAAQ 662
Cdd:TIGR00955 411 VINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVAT 487
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
172-400 |
1.08e-74 |
|
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: 238.99 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 172 PIYLKFAEVKYKVAVKGTP--REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdVEGCVSYNDEP-YCKS 248
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG-VSGEVLINGRPlDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 249 LNRRIGFVTQDDVLFTHLTVKETLTYAALLRlprtmtrqekeertidiiyelglercqdtmiggsfvrGVSGGERKRVCI 328
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 329 GNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFG 400
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
175-400 |
5.98e-73 |
|
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: 235.63 E-value: 5.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKSL-NRRI 253
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQfQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 254 GFVTQDDVLFTHLTVKETLTYAALLRLPRTMTRQEKEERTIDiiyeLGLERCQDTMIGGSFVRGVSGGERKRVCIGNEII 333
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVED----VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFG 400
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
150-646 |
7.00e-73 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 257.73 E-value: 7.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 150 DDNTMDIEAG--TPRKKLMTEPTLPIYLKFAE------------VKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGS 215
Cdd:TIGR00956 721 ASNKNDIEAGevLGSTDLTDESDDVNDEKDMEkesgedifhwrnLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 216 GKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRLPRTMTRQEKEERTID 295
Cdd:TIGR00956 801 GKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEE 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 296 IIYELGLERCQDTMIG--GSfvrGVSGGERKRVCIGNEIIINP-SLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVIT 372
Cdd:TIGR00956 881 VIKLLEMESYADAVVGvpGE---GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILC 957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 373 TIHQPSSRLFHKFDKLILLGRGS-LLYF---GKASEAM-PYFQSIG---CTPliAMNPAEFLLDLANGNTTdvsvpseld 444
Cdd:TIGR00956 958 TIHQPSAILFEEFDRLLLLQKGGqTVYFgdlGENSHTIiNYFEKHGapkCPE--DANPAEWMLEVIGAAPG--------- 1026
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 445 dkvhmenqnlqTNTKNDYkpsaqdvHEYlvdaYENRVAYKAKKQLLD----PLPISDDMKTtiTSSKREWGTSWWQQYSI 520
Cdd:TIGR00956 1027 -----------AHANQDY-------HEV----WRNSSEYQAVKNELDrleaELSKAEDDND--PDALSKYAASLWYQFKL 1082
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 521 LFCRGIKE--RRHDYLsWMRITQVIATSVILGLLWWHSDPSTpKGLQDQAGLLFFIAVFWG-----FFPVFTAiftfpQE 593
Cdd:TIGR00956 1083 VLWRTFQQywRTPDYL-YSKFFLTIFAALFIGFTFFKVGTSL-QGLQNQMFAVFMATVLFNpliqqYLPPFVA-----QR 1155
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 594 RAMLNKERAADMYKLSAYFLARTTSDLPLDLFLPVIFMVIVYFMAGLKATAAH 646
Cdd:TIGR00956 1156 DLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASK 1208
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
169-661 |
2.68e-69 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 247.33 E-value: 2.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 169 PTLP-IYLKFAEV---KYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAG-PGDVEGCVSYND- 242
Cdd:TIGR00956 48 PTFPnALLKILTRgfrKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfHIGVEGVITYDGi 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 243 --EPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRLPRT----MTRQEKEERTIDIIYE-LGLERCQDTMIGGSFV 315
Cdd:TIGR00956 128 tpEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYMAtYGLSHTRNTKVGNDFV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 316 RGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGK-TVITTIHQPSSRLFHKFDKLILLGRG 394
Cdd:TIGR00956 208 RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 395 SLLYFGKASEAMPYFQSIG--CTPLIAMnpAEFLldlangntTDVSVPSELDDKVHMENQNLQtnTKNDYKPSAQDVHEY 472
Cdd:TIGR00956 288 YQIYFGPADKAKQYFEKMGfkCPDRQTT--ADFL--------TSLTSPAERQIKPGYEKKVPR--TPQEFETYWRNSPEY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 473 L-----VDAYENRVAYKAKKQLLDPLPISDDMKTTITSSKreWGTSWWQQYSILFCRGIKERRHD---YLSwmRITQVIA 544
Cdd:TIGR00956 356 AqlmkeIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSP--YTVSFSMQVKYCLARNFLRMKGNpsfTLF--MVFGNII 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 545 TSVILGLLWWHSDPSTPKGLQdQAGLLFFiAVFWGFFPVFTAIFTFPQERAMLNKERAADMYKLSAYFLARTTSDLPLDL 624
Cdd:TIGR00956 432 MALILSSVFYNLPKNTSDFYS-RGGALFF-AILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKI 509
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002256437 625 FLPVIFMVIVYFMAGLKATAAHFFLSMLTVFLSIIAA 661
Cdd:TIGR00956 510 IESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAM 546
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
172-400 |
7.58e-63 |
|
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: 207.48 E-value: 7.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 172 PIYLKFAEVKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGpGDVEGCVSYNDEPYCKSLNR 251
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTA-GVITGEILINGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 252 RIGFVTQDDVLFTHLTVKETLTYAALLRlprtmtrqekeertidiiyelglercqdtmiggsfvrGVSGGERKRVCIGNE 331
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 332 IIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGR-GSLLYFG 400
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
151-659 |
8.16e-62 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 225.11 E-value: 8.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 151 DNTMDIEAGTPRKKLMTEPTLPIYLKFAEVKYKVAVKGTPRE---------ILSGISGSAAPGEVLALMGPSGSGKTTLL 221
Cdd:PLN03140 844 DSSLEAANGVAPKRGMVLPFTPLAMSFDDVNYFVDMPAEMKEqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLM 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 222 SILGGRVAGpGDVEGCVSYNDEPYCKSLNRRI-GFVTQDDVLFTHLTVKETLTYAALLRLPRTMTRQEKEeRTIDIIYEL 300
Cdd:PLN03140 924 DVLAGRKTG-GYIEGDIRISGFPKKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKM-MFVDEVMEL 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 301 -GLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSS 379
Cdd:PLN03140 1002 vELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 380 RLFHKFDKLILLGR-GSLLYFG----KASEAMPYFQSIGCTPLIA--MNPAEFLLDLAngnttdvSVPSELddkvhmenq 452
Cdd:PLN03140 1082 DIFEAFDELLLMKRgGQVIYSGplgrNSHKIIEYFEAIPGVPKIKekYNPATWMLEVS-------SLAAEV--------- 1145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 453 NLQTNTKNDYKPSAqdvheyLVDAYENRVaykakKQLLDPLPISDDMKTTITSSKREWG---TSWWQQYSILFcrgikeR 529
Cdd:PLN03140 1146 KLGIDFAEHYKSSS------LYQRNKALV-----KELSTPPPGASDLYFATQYSQSTWGqfkSCLWKQWWTYW------R 1208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 530 RHDYlSWMRITQVIATSVILGLLWWH--SDPSTPKGLQDQAGLLFFIAVFWGFFPVFTAIFTFPQERAMLNKERAADMYK 607
Cdd:PLN03140 1209 SPDY-NLVRFFFTLAAALMVGTIFWKvgTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYS 1287
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 608 LSAYFLARTTSDLPLDLFLPVIFMVIVYFMAGLKATAAHFFLSMLTVFLSII 659
Cdd:PLN03140 1288 ALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFL 1339
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
191-400 |
1.36e-47 |
|
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: 166.67 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKSLN---RRIGFVTQDDVLFTHLT 267
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAEkypGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAAllrlprtmtrqekeertidiiyelgleRCQdtmiGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03233 100 VRETLDFAL---------------------------RCK----GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 348 LDSTTALRIIQLLHDIA-EDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFG 400
Cdd:cd03233 149 LDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
191-404 |
2.14e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG---------RVAGpgdvegcVSYNDEPycKSLNRRIGFVTQDDV 261
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllrptsgevRVLG-------EDVARDP--AEVRRRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTYAALLRlprTMTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:COG1131 84 LYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRK-----VGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPS--SRLfhkFDKLILLGRGSLLYFGKASE 404
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEeaERL---CDRVAIIDKGRIVADGTPDE 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
187-665 |
1.98e-38 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 153.85 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKSLNRRI-GFVTQDDVLFTH 265
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTsAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLTYAALLR-------LPRTMTRQEKE-----ERTIDIIYE-------------------LGLERCQDTMIGGSF 314
Cdd:PLN03140 254 MTVKETLDFSARCQgvgtrydLLSELARREKDagifpEAEVDLFMKatamegvksslitdytlkiLGLDICKDTIVGDEM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 315 VRGVSGGERKRVCIGnEIIINPS-LLFLDEPTSGLDSTTALRIIQLLHDIAE-DGKTVITTIHQPSSRLFHKFDKLILLG 392
Cdd:PLN03140 334 IRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 393 RGSLLYFGKASEAMPYFQSIGCTPLIAMNPAEFLLDlangnttdvsVPSELDDKVHMENQNlqtntkndyKP-SAQDVHE 471
Cdd:PLN03140 413 EGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQE----------VTSKKDQEQYWADRN---------KPyRYISVSE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 472 YLVDAYENRVAYKAKKQLLDPLPISDDMKTTI-----TSSKREWGTSWWQQYSILFcrgikeRRHDYLSWMRITQVIATS 546
Cdd:PLN03140 474 FAERFKSFHVGMQLENELSVPFDKSQSHKAALvfskySVPKMELLKACWDKEWLLM------KRNAFVYVFKTVQIIIVA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 547 VILGLLWWHSDPSTpKGLQDQA---GLLFF---IAVFWGFFPVFTAIFTFPqeraMLNKERAADMYKLSAYFLARTTSDL 620
Cdd:PLN03140 548 AIASTVFLRTEMHT-RNEEDGAlyiGALLFsmiINMFNGFAELALMIQRLP----VFYKQRDLLFHPPWTFTLPTFLLGI 622
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 621 PLDLFLPVIFMVIVYFMAGLKATAAHFFLSMLTVFL---------SIIAAQIRT 665
Cdd:PLN03140 623 PISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLiqqmaagifRLIASVCRT 676
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
191-404 |
7.23e-38 |
|
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: 141.15 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKS---LNRRIGFVTQDDVLFTHLT 267
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK-PD--SGSILIDGEDVRKEpreARRQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAALLRLprtMTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:COG4555 91 VRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRR-----VGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIHQPS--SRLfhkFDKLILLGRGSLLYFGKASE 404
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQevEAL---CDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
188-396 |
8.08e-38 |
|
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: 140.32 E-value: 8.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEP-YCKS-------LNRRIGFVTQD 259
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRP--TSGEVRVDGTDiSKLSekelaafRRRHIGFVFQS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHLTVKETLTYAALLrlpRTMTRQEKEERTIDIIYELGLERCQDTmiggsFVRGVSGGERKRVCIGNEIIINPSLL 339
Cdd:cd03255 91 FNLLPDLTALENVELPLLL---AGVPKKERRERAEELLERVGLGDRLNH-----YPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIHQPssRLFHKFDKLILLGRGSL 396
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
175-371 |
1.37e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.10 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagpgDV--EGCVSYNDEPyCKSL--- 249
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL-----DRptSGEVLIDGQD-ISSLser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 250 ------NRRIGFVTQDDVLFTHLTVKETLTYAALLrlpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGER 323
Cdd:COG1136 79 elarlrRRHIGFVFQFFNLLPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLD-----HRPSQLSGGQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002256437 324 KRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVI 371
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIV 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
187-394 |
5.56e-36 |
|
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: 134.90 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPGDVEGCVSYNDEPY----CKSLNRRIGFVTQD-DV 261
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL---LGPTSGEVLVDGKDLtklsLKELRRKVGLVFQNpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTYAALLRlprTMTRQEKEERTIDIIYELGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:cd03225 87 QFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSP-----FTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPsSRLFHKFDKLILLGRG 394
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
194-346 |
2.54e-34 |
|
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: 127.76 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPY----CKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLtddeRKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 270 ETLTYAALLrlpRTMTRQEKEERTIDIIYELGLERCQDTMIgGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:pfam00005 78 ENLRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPV-GERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
187-375 |
2.85e-34 |
|
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: 130.32 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGcvsYNDEPYCKSLNRRIGFVTQDDVLF 263
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrptSGTAYING---YSIRTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAALLR-LPRTMTRQEKEErtidIIYELGLERCQDTmiggsFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:cd03263 88 DELTVREHLRFYARLKgLPKSEIKEEVEL----LLRVLGLTDKANK-----RARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEdGKTVITTIH 375
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK-GRSIILTTH 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
191-406 |
4.96e-34 |
|
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: 129.76 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCKS----LNRRIGFVTQ--DDVLFt 264
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-LLKP--TSGEVLVDGKDITKKnlreLRRKVGLVFQnpDDQLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAAL-LRLPRtmtrQEKEERTIDIIYELGLERCQDtmiggsfvRGV---SGGERKRVCIGNEIIINPSLLF 340
Cdd:COG1122 90 APTVEEDVAFGPEnLGLPR----EEIRERVEEALELVGLEHLAD--------RPPhelSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSrLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
191-404 |
1.80e-33 |
|
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: 128.39 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgdVEGCVSYNDEPYCK-------SLNRRIGFVTQDDVLF 263
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-P--DSGEVLIDGEDISGlseaelyRLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:cd03261 90 DSLTVFENV--AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQPSSrLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
191-404 |
3.24e-33 |
|
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: 127.79 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgdVEGCVSYNDEPYCK-------SLNRRIGFVTQDDVLF 263
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-P--DSGEILVDGQDITGlsekelyELRRRIGMLFQGGALF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAalLRLPRTMTRQEKEERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:COG1127 95 DSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADKMPS-----ELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQPSSrLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEE 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
191-406 |
6.01e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLL-SILGgrVAGPgdVEGCVSYNDEPYCKSlNRRIGFVTQD---DVLFThL 266
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILG--LLPP--TSGTVRLFGKPPRRA-RRRIGYVPQRaevDWDFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAAL--LRLPRTMTRQEKeERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:COG1121 93 TVRDVVLMGRYgrRGLFRRPSRADR-EAVDEALERVGLEDLADRPIG-----ELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 345 TSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSrLFHKFDKLILLGRGsLLYFGKASEAM 406
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
187-371 |
9.62e-33 |
|
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: 126.05 E-value: 9.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCkSLNRRIGFVTQDDVLFTHL 266
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-PT--SGEVLVDGEPVT-GPGPDRGYVFQQDALLPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:cd03293 89 TVLDNVALG--LEL-QGVPKAEARERAEELLELVGLSGFEN-----AYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180
....*....|....*....|....*.
gi 1002256437 347 GLDSTTALRIIQLLHDI-AEDGKTVI 371
Cdd:cd03293 161 ALDALTREQLQEELLDIwRETGKTVL 186
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
193-400 |
1.02e-32 |
|
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: 125.71 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG--RVAGpgdveGCVSYNDE------PYckslNRRIGFVTQDDVLFT 264
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS-----GEILIDGRdvtgvpPE----RRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:cd03259 86 HLTVAENIAFG--LKL-RGVPKAEIRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 345 TSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQPSSRLFHKfDKLILLGRGSLLYFG 400
Cdd:cd03259 158 LSALDAKLREELREELKELqRELGITTIYVTHDQEEALALA-DRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
191-396 |
1.04e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGC----VSYNDEPYcksLNRRIGFVTQDDVLF 263
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErptSGQVLVNGQdlsrLKRREIPY---LRRRIGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:COG2884 92 PDRTVYENVALP--LRV-TGKSRKEIRRRVREVLDLVGLSD-----KAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSsrLFHKFDKLIL-LGRGSL 396
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPKRVLeLEDGRL 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
166-371 |
4.16e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.20 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 166 MTEPtlPIYLKFAEVKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPy 245
Cdd:COG1116 1 MSAA--APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK---PTSGEVLVDGKP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 246 CKSLNRRIGFVTQDDVLFTHLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKR 325
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFED-----AYPHQLSGGMRQR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 326 VCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVI 371
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVL 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
184-424 |
7.11e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.41 E-value: 7.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 184 VAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYCKS----LNRRIGFVTQD 259
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELsealRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 -DVLFTHLTVKETLTYAALLRLprtMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSL 338
Cdd:COG1123 92 pMTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLER-----RLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQPsSRLFHKFDKLILLGRGSLLYFGKASEAMPYFQSIGCTPL 417
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPR 242
|
....*..
gi 1002256437 418 IAMNPAE 424
Cdd:COG1123 243 LGAARGR 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
202-400 |
7.44e-32 |
|
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: 123.17 E-value: 7.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 202 APGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEPY---CKSLN-----RRIGFVTQDDVLFTHLTVKETLT 273
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDG---GTIVLNGTVLfdsRKKINlppqqRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 YAalLRLPRTMTRQEKEERTIDIiyeLGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:cd03297 98 FG--LKRKRNREDRISVDELLDL---LGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256437 354 LRIIQLLHDIAED-GKTVITTIHQPsSRLFHKFDKLILLGRGSLLYFG 400
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
191-406 |
1.49e-31 |
|
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: 123.62 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYC----KSLNRRIGFVTQDDVLFTHL 266
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PS--SGEVLLDGRDLAslsrRELARRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLtyaALLRLP-RTMTRQEKEErTIDIIYE----LGLERCQDtmiggsfvRGV---SGGERKRVCIGNEIIINPSL 338
Cdd:COG1120 91 TVRELV---ALGRYPhLGLFGRPSAE-DREAVEEalerTGLEHLAD--------RPVdelSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIHQPS--SRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNlaARY---ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
191-396 |
6.54e-31 |
|
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: 119.04 E-value: 6.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGcVSYNDEPycKSLNRRIGFVTQDDVLFTHLT 267
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkpdSGEIKVLG-KDIKKEP--EEVKRRIGYLPEEPSLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYaallrlprtmtrqekeertidiiyelglercqdtmiggsfvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03230 90 VRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIHQPS--SRLfhkFDKLILLGRGSL 396
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILEeaERL---CDRVAILNNGRI 173
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
521-662 |
1.07e-30 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 119.69 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 521 LFCRGIKER-RHDYLSWMRITQVIATSVILGLLWWHSDpsTPKGLQDQAGLLFFIAVFWGFFPVFTAIFTFPQERAMLNK 599
Cdd:pfam01061 1 LLKREFLRRwRDPSLGLWRLIQPILMALIFGTLFGNLG--NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 600 ERAADMYKLSAYFLARTTSDLPLDLFLPVIFMVIVYFMAGLKATAAHFFLSMLTVFLSIIAAQ 662
Cdd:pfam01061 79 ELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAAS 141
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
191-394 |
2.02e-30 |
|
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: 117.67 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLT 267
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleePDSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYaallrlprtmtrqekeertidiiyelglercqdtmiggsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03229 93 VLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256437 348 LDSTTALRIIQLLHDI-AEDGKTVITTIHQPSSrLFHKFDKLILLGRG 394
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDG 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
190-376 |
3.42e-30 |
|
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: 118.40 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLL-------SILGGRVAgpgdVEGCVSYNDEPYCKSLNRRIGFVTQDDVL 262
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrcinlleEPDSGTII----IDGLKLTDDKKNINELRQKVGMVFQQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAalLRLPRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:cd03262 88 FPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKAD-----AYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
188-394 |
4.07e-30 |
|
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: 116.71 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagpgDV-EGCVSYNDEPYCK----SLNRRIGFVTQDDVL 262
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY----DPtSGEILIDGVDLRDldleSLRKNIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FtHLTVKETLtyaallrlprtmtrqekeertidiiyelglercqdtmiggsfvrgVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:cd03228 88 F-SGTIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAeDGKTVITTIHQPSSrlFHKFDKLILLGRG 394
Cdd:cd03228 122 EATSALDPETEALILEALRALA-KGKTVIVIAHRLST--IRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
191-406 |
5.66e-30 |
|
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: 125.26 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYC----KSLNRRIGFVTQDDVLFtHL 266
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP---PYSGSILINGVDLSdldpASWRRQIAWVPQNPYLF-AG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAAllrlpRTMTRQEKEE-----RTIDIIYEL--GLercqDTMIG--GsfvRGVSGGERKRVCIGNEIIINPS 337
Cdd:COG4988 426 TIRENLRLGR-----PDASDEELEAaleaaGLDEFVAALpdGL----DTPLGegG---RGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSRlfHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL--AQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
188-404 |
6.30e-30 |
|
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: 118.44 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGpgdVEGCVSYNDEPYCK-------SLNRRIGFVTQDD 260
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGSVLIDGTDINKlkgkalrQLRRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFTHLTVKET-----LTYAALLR-LPRTMTRQEKeERTIDIIYELGLE-----RCqDTMiggsfvrgvSGGERKRVCIG 329
Cdd:cd03256 88 NLIERLSVLENvlsgrLGRRSTWRsLFGLFPKEEK-QRALAALERVGLLdkayqRA-DQL---------SGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 330 NEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIHQPSsrLFHKF-DKLILLGRGSLLYFGKASE 404
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVD--LAREYaDRIVGLKDGRIVFDGPPAE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
191-393 |
1.05e-29 |
|
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: 116.81 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYCK---SLNRRIGFVTQDDVLFTHLT 267
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP---PSAGEVLWNGEPIRDareDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLT-YAALLRLPRTmtrqekEERTIDIIYELGLERCQDTmiggsFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:COG4133 92 VRENLRfWAALYGLRAD------REAIDEALEAVGLAGLADL-----PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTVITTIHQPssrLFHKFDKLILLGR 393
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
191-371 |
1.10e-29 |
|
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: 117.98 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPY----CKSLNRRIGFVTQD--DVLFT 264
Cdd:COG1124 18 VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER---PWSGEVTFDGRPVtrrrRKAFRRRVQMVFQDpyASLHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLtyAALLRLprtMTRQEKEERTIDIIYELGLercqDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:COG1124 95 RHTVDRIL--AEPLRI---HGLPDREERIAELLEQVGL----PPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180
....*....|....*....|....*...
gi 1002256437 345 TSGLDSTTALRIIQLLHDI-AEDGKTVI 371
Cdd:COG1124 166 TSALDVSVQAEILNLLKDLrEERGLTYL 193
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
190-404 |
4.95e-29 |
|
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: 115.36 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLLSIL--------GGRVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQDDV 261
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipGAPDEGEVLLDGKDIYDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFtHLTVKETLTYAalLRLprtmtRQEKEERTIDIIYELGLERCQ--DTMIGGSFVRGVSGGERKRVCIGNEIIINPSLL 339
Cdd:cd03260 92 PF-PGSIYDNVAYG--LRL-----HGIKLKEELDERVEEALRKAAlwDEVKDRLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITT--IHQpSSRLfhkFDKLILLGRGSLLYFGKASE 404
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ-AARV---ADRTAFLLNGRLVEFGPTEQ 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
186-371 |
6.12e-29 |
|
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: 115.30 E-value: 6.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 186 VKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLL-SILG-GRVAGpgdveGCVSYNDEPYCKSLN-------RRIGFV 256
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLArAILGlLKPTS-----GSIIFDGKDLLKLSRrlrkirrKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQD--DVLFTHLTVKETLtyAALLRLPRTMTRQEKEERTIDIIYE-LGL-ERCQDtmiggSFVRGVSGGERKRVCIGNEI 332
Cdd:cd03257 88 FQDpmSSLNPRMTIGEQI--AEPLRIHGKLSKKEARKEAVLLLLVgVGLpEEVLN-----RYPHELSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002256437 333 IINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVI 371
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLL 200
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
191-355 |
8.39e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.12 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPyCKSLN---RRIGFVTQDDVLFTHLT 267
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRR-LTALPaeqRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAallrLPRTMTRQEKEERTIDIIYELGLercqdtmiGGSFVRGV---SGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:COG4136 93 VGENLAFA----LPPTIGRAQRRARVEQALEEAGL--------AGFADRDPatlSGGQRARVALLRALLAEPRALLLDEP 160
|
170
....*....|.
gi 1002256437 345 TSGLDstTALR 355
Cdd:COG4136 161 FSKLD--AALR 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
184-396 |
9.76e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 184 VAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILggrvAG--PGDvEGCVSYNDEPYcKSLN-----RRIGFV 256
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL----ADldPPT-SGEIYLDGKPL-SAMPppewrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQDDVLFTHlTVKETLTYAALLRlprtmTRQEKEERTIDIIYELGLErcqDTMIGGSFVRgVSGGERKRVCIGNEIIINP 336
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLR-----ERKFDRERALELLERLGLP---PDILDKPVER-LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHD-IAEDGKTVITTIHQP--SSRLfhkFDKLILLGRGSL 396
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPeqIERV---ADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
191-394 |
1.72e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.57 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagpgdvegcvsyndepyckslnrrigFVTQDDVLFTHLTVKE 270
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL--------------------------KPTSGEILIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TLTYAALLRLprtmtrqekeertidiiyelglercqdtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDS 350
Cdd:cd00267 66 LPLEELRRRI--------------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002256437 351 TTALRIIQLLHDIAEDGKTVITTIHQPSSrLFHKFDKLILLGRG 394
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDG 156
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
188-406 |
1.84e-28 |
|
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: 120.64 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYC----KSLNRRIGFVTQDDVLF 263
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD---PQSGSITLGGVDLRdldeDDLRRRIAVVPQRPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYAA--------------------LLRLPRtmtrqekeertidiiyelGLercqDTMIG--GsfvRGVSGG 321
Cdd:COG4987 422 DT-TLRENLRLARpdatdeelwaalervglgdwLAALPD------------------GL----DTWLGegG---RRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 322 ERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSsrLFHKFDKLILLGRGSLLYFGK 401
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDGRIVEQGT 552
|
....*
gi 1002256437 402 ASEAM 406
Cdd:COG4987 553 HEELL 557
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
194-404 |
2.90e-28 |
|
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: 113.58 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYN--DEPYCKSLNRRIGFVTQDDVLFTHLTVKET 271
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAG-FIKP--DSGKILLNgkDITNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 272 LTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDST 351
Cdd:cd03299 92 IAYG--LKK-RKVDKKEIERKVLEIAEMLGIDHLLN-----RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 352 TALRIIQLLHDIAEDGKTviTTIHqpssrLFHKF-------DKLILLGRGSLLYFGKASE 404
Cdd:cd03299 164 TKEKLREELKKIRKEFGV--TVLH-----VTHDFeeawalaDKVAIMLNGKLIQVGKPEE 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
182-371 |
4.12e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.85 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 182 YKVAVKGTPReILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgdVEGCVSYNDEPYC-------KSLNRRIG 254
Cdd:COG1123 270 YPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-P--TSGSILFDGKDLTklsrrslRELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 255 FVTQD--DVLFTHLTVKETLTYAalLRLPRTMTRQEKEERtidiIYELgLERCQ-DTMIGGSFVRGVSGGERKRVCIGNE 331
Cdd:COG1123 346 MVFQDpySSLNPRMTVGDIIAEP--LRLHGLLSRAERRER----VAEL-LERVGlPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002256437 332 IIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVI 371
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYL 459
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
191-406 |
3.30e-27 |
|
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: 110.40 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAgpgDV-EGCVSYNDEPY----CKSLNRRIGFVTQDDVLFtH 265
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFY---DVsSGSILIDGQDIrevtLDSLRRAIGVVPQDTVLF-N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLTYAALLRLPRTMTRQEKEERTIDIIyeLGLERCQDTMIGGsfvRGV--SGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:cd03253 89 DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKI--MRFPDGYDTIVGE---RGLklSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLST--IVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
191-400 |
3.49e-27 |
|
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: 109.55 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagPGDvEGCVSYNDEPYCKSlNRRIGFVTQ-DDVLFTH-LTV 268
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL--KPT-SGSIRVFGKPLEKE-RKRIGYVPQrRSIDRDFpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAAL--LRLPRTMTRQEKeERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:cd03235 88 RDVVLMGLYghKGLFRRLSKADK-AKVDEALERVGLSELADRQIG-----ELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSrLFHKFDKLILLGRGsLLYFG 400
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
191-400 |
5.30e-27 |
|
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: 108.29 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGpgdVEGCVSYNDEPY----CKSLNRRIGFVTQddVLfthl 266
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP---SSGEILLDGKDLaslsPKELARKIAYVPQ--AL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 tvketltyaALLRLprtmtrQEKEERTIDiiyELglercqdtmiggsfvrgvSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:cd03214 83 ---------ELLGL------AHLADRPFN---EL------------------SGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 347 GLDSTTALRIIQLLHDIA-EDGKTVITTIHQPSSRLFHkFDKLILLGRGSLLYFG 400
Cdd:cd03214 127 HLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARY-ADRVILLKDGRIVAQG 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
193-400 |
5.36e-27 |
|
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: 109.20 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGeVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEP---YCKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP---PSSGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAALLRlpRTMTRQEKEeRTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:cd03264 91 EFLDYIAWLK--GIPSKEVKA-RVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 350 STTALRIIQLLHDIAEDgKTVITTIHQPSSRLFHkFDKLILLGRGSLLYFG 400
Cdd:cd03264 163 PEERIRFRNLLSELGED-RIVILSTHIVEDVESL-CNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
188-406 |
8.47e-27 |
|
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: 116.47 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILggrvAG---PgdVEGCVSYNDEPYCK----SLNRRIGFVTQDD 260
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL----LGlyeP--TSGRILIDGIDLRQidpaSLRRQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFtHLTVKETLTYAAllrlpRTMTRQEKEERT-----IDIIYEL--GLercqDTMIG--GSfvrGVSGGERKRVCIGNE 331
Cdd:COG2274 559 FLF-SGTIRENITLGD-----PDATDEEIIEAArlaglHDFIEALpmGY----DTVVGegGS---NLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 332 IIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSS-RLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTiRL---ADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
194-396 |
1.45e-26 |
|
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: 107.88 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvAGPgdVEGCVSYNDEPYCK-------SLNRRIGFVTQDDVLFTHL 266
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-ELP--TSGTIRVNGQDVSDlrgraipYLRRKIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAalLRLPRTmTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:cd03292 94 NVYENVAFA--LEVTGV-PPREIRKRVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTVITTIHqpSSRLFHKFDK-LILLGRGSL 396
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRHrVIALERGKL 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
194-400 |
2.77e-26 |
|
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: 107.45 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGcVSYNDEPycKSLNRRIGFVTQDDVLFTHLTVKE 270
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLepdAGFATVDG-FDVVKEP--AEARRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TLTYAALLRlprTMTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDS 350
Cdd:cd03266 98 NLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVGG-----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 351 TTALRIIQLLHDIAEDGKTVITTIH--QPSSRLfhkFDKLILLGRGSLLYFG 400
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
191-379 |
4.03e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILggrvagPG--DV-EGCVSYNDEPYC----KSLNRRIGFVTQDDVLF 263
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL------LRfyDPtSGRILIDGVDIRdltlESLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 tHLTVKETLTYAALlrlprTMTRQEKEE--RTI---DIIYEL--GLercqDTMIGGsfvRGV--SGGERKRVCIGNEIII 334
Cdd:COG1132 427 -SGTIRENIRYGRP-----DATDEEVEEaaKAAqahEFIEALpdGY----DTVVGE---RGVnlSGGQRQRIAIARALLK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSS 379
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLST 537
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
200-406 |
6.20e-26 |
|
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: 109.81 E-value: 6.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 200 SAAPGEVLALMGPSGSGKTTLLSILGG--RVAgpgdvEGCVSYNDEPYCKSLN--------RRIGFVTQDDVLFTHLTVK 269
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGleRPD-----SGRIRLGGEVLQDSARgiflpphrRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAallrlprtMTRQEKEERTID---IIYELG----LERcqdtmiggsFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:COG4148 96 GNLLYG--------RKRAPRAERRISfdeVVELLGighlLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 343 EPTSGLDSTTALRIIQLL---------------HDIAEdgktVittihqpsSRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG4148 159 EPLAALDLARKAEILPYLerlrdeldipilyvsHSLDE----V--------ARL---ADHVVLLEQGRVVASGPLAEVL 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
166-378 |
1.17e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.98 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 166 MTEPTLPIyLKFAEVKYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVEGC----VSY 240
Cdd:COG4181 1 MSSSSAPI-IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPTSGTVRLAgqdlFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 241 NDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRlprtmTRQEKEERTIDIIYELGL-ERCqdtmigGSFVRGVS 319
Cdd:COG4181 80 DEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGLgHRL------DHYPAQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 320 GGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQPS 378
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
187-404 |
1.31e-25 |
|
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: 106.03 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPGDVEGCVSYNdepyckSLNRRIGFVTQD 259
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvpeNGRVLVDGHDLALADPA------WLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHlTVKETLtyaALLRLPRTMTRQEKEERTI---DIIYELGLErcQDTMIGGSFVrGVSGGERKRVCIGNEIIINP 336
Cdd:cd03252 85 NVLFNR-SIRDNI---ALADPGMSMERVIEAAKLAgahDFISELPEG--YDTIVGEQGA-GLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHDIAeDGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYFGKASE 404
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDE 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
192-371 |
1.74e-25 |
|
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: 105.21 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLL-SILG------GRVA-GPGDVEGCVSYndepyckSLNRR-IGFVTQDDVL 262
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLkTIMGllpprsGSIRfDGRDITGLPPH-------ERARAgIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAALLRlprtmtRQEKEERTIDIIYEL--GLERCQDTMiGGSFvrgvSGGERKRVCIGNEIIINPSLLF 340
Cdd:cd03224 87 FPELTVEENLLLGAYAR------RRAKRKARLERVYELfpRLKERRKQL-AGTL----SGGEQQMLAIARALMSRPKLLL 155
|
170 180 190
....*....|....*....|....*....|.
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
192-396 |
3.99e-25 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.97 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVE------GCVSYNDEPYCKslNRRIGFVTQDDVLFT 264
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGlDNPTSGEVLfngqslSKLSSNERAKLR--NKKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAALLRlprTMTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:TIGR02211 97 DFTALENVAMPLLIG---KKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 345 TSGLDSTTALRIIQLLHDIAEDGKT--VITTiHQPssRLFHKFDKLILLGRGSL 396
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTsfLVVT-HDL--ELAKKLDRVLEMKDGQL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
203-429 |
7.05e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 106.73 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PG-EVLALMGPSGSGKTTLLSILGGRVAGPgdvEGCVSYNDEPYCKSL--------NRRIGFVTQDDVLFTHLTVKETLT 273
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRPD---EGEIVLNGRTLFDSRkgiflppeKRRIGYVFQEARLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 YAalLRLPRTMTRQEKEERTIDIiyeLGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:TIGR02142 98 YG--MKRARPSERRISFERVIEL---LGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 354 LRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGKASEAMpyfqSIGCTPLIAMNPAEFLLDL 429
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW----ASPDLPWLAREDQGSLIEG 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
193-375 |
7.45e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG--RVAgpgdvEGCVSYNDE------PYckslNRRIGFVTQDDVLFT 264
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPD-----SGRILLDGRdvtglpPE----KRNVGMVFQDYALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:COG3842 91 HLTVAENVAFG--LRM-RGVPKAEIRARVAELLELVGLEGLADRY-----PHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 345 TSGLDSTTALRIIQLLHDI-AEDGktvITTIH 375
Cdd:COG3842 163 LSALDAKLREEMREELRRLqRELG---ITFIY 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
191-377 |
1.72e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGP--GDVEgcvsyndepycKSLNRRIGFVTQ----DDVLft 264
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG-VLRPtsGTVR-----------RAGGARVAYVPQrsevPDSL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYA--ALLRLPRTMTRqEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:NF040873 71 PLTVRDLVAMGrwARRGLWRRLTR-DDRAAVDDALERVGLAD-----LAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
194-375 |
2.99e-24 |
|
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: 103.62 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILG---------GRVAGPgDVegcVSYNDEpycksLNRRIGFVTQDDVLFT 264
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTtllrptsgtARVAGY-DV---VREPRK-----VRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLT-YAALLRLPRtmtrQEKEERtidiIYELgLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:TIGR01188 80 DLTGRENLEmMGRLYGLPK----DEAEER----AEEL-LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
191-375 |
3.06e-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: 101.18 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYC-KSLNRRIGFVTQD--DVLFTHlT 267
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK---ESSGSILLNGKPIKaKERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLtyaaLLRLPRTmtrQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03226 89 VREEL----LLGLKEL---DAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180
....*....|....*....|....*...
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
191-406 |
3.44e-24 |
|
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: 102.08 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPgDVE------GCVSYNDepycksLNRRIGFVTQD-- 259
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptYGN-DVRlfgerrGGEDVWE------LRKRIGLVSPAlq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHLTVKET-LT--YAALlRLPRTMTRQEkEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINP 336
Cdd:COG1119 89 LRFPRDETVLDVvLSgfFDSI-GLYREPTDEQ-RERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTI-HQ----PSSrlfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHveeiPPG-----ITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
192-375 |
5.66e-24 |
|
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: 99.80 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEP--YCKS----LNRRIGFVTQ--DDVLF 263
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQS---GAVLIDGEPldYSRKglleRRQRVGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYAallrlPRTM--TRQEKEERTIDIIYELGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:TIGR01166 83 AA-DVDQDVAFG-----PLNLglSEAEVERRVREALTAVGASGLRERPT-----HCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
191-398 |
9.57e-24 |
|
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: 99.60 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV-AGPGDVE--GcVSYNDEpycKSLNRRIGFVTQDDVLFTHLT 267
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITfdG-KSYQKN---IEALRRIGALIEAPGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAALLrlprTMTRQEKEERTIDIIyelGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03268 89 ARENLRLLARL----LGIRKKRIDEVLDVV---GLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIHQpSSRLFHKFDKLILLGRGSLLY 398
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
187-396 |
1.02e-23 |
|
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: 99.97 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSYNDEPYCK----SLNRRIGFVTQDDVL 262
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-LYKPT--SGSVLLDGTDIRQldpaDLRRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHlTVKETLTYAALLrlprtmtrqEKEERTIDIIYELGLE-------RCQDTMIG--GsfvRGVSGGERKRVCIGNEII 333
Cdd:cd03245 90 FYG-TLRDNITLGAPL---------ADDERILRAAELAGVTdfvnkhpNGLDLQIGerG---RGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDgKTVITTIHQPSsrLFHKFDKLILLGRGSL 396
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
194-371 |
1.45e-23 |
|
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: 99.82 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDE------PYckSLNRR-IGFVTQDDVLFTHL 266
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-PT--SGSVLFDGEditglpPH--EIARLgIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAALLRLPRTMT-----RQEKE--ERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLL 339
Cdd:cd03219 91 TVLENVMVAAQARTGSGLLlararREEREarERAEELLERVGLADLADRPAG-----ELSYGQQRRLEIARALATDPKLL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
187-372 |
3.62e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.55 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKSLNRRiGFVTQDDVLFTHL 266
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA-PS--SGEITLDGVPVTGPGADR-GVVFQKDALLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:COG4525 92 NVLDNVAFG--LRL-RGVPKAERRARAEELLALVGLAD-----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180
....*....|....*....|....*....
gi 1002256437 347 GLDSTTALRIIQLLHDI-AEDGKTV--IT 372
Cdd:COG4525 164 ALDALTREQMQELLLDVwQRTGKGVflIT 192
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
191-375 |
4.00e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 98.89 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagPGDvEGCVSYNDEPYCKS-LNRR----IGFVTQDDVLFTH 265
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLV--RPD-AGKILIDGQDITHLpMHERarlgIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLTyaALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMiGGSfvrgVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:TIGR04406 91 LTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNK-AMS----LSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
188-394 |
6.60e-23 |
|
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: 98.07 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPG-DVEGcVSYNdepyckSLNRRIGFVTQD 259
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGhDVRD-YTLA------SLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHlTVKETLTYAAllrlpRTMTRQEKEE--RTI---DIIYEL--GLercqDTMIGgsfVRGV--SGGERKRVCIGN 330
Cdd:cd03251 85 VFLFND-TVAENIAYGR-----PGATREEVEEaaRAAnahEFIMELpeGY----DTVIG---ERGVklSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 331 EIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDgKTVITTIHQPSSrlFHKFDKLILLGRG 394
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRLST--IENADRIVVLEDG 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
193-376 |
8.25e-23 |
|
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: 96.97 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETL 272
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-PD--SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 273 TYAALLRlprTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTT 352
Cdd:cd03269 92 VYLAQLK---GLKKEEARRRIDEWLERLELSEYAN-----KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180
....*....|....*....|....
gi 1002256437 353 ALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQ 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
192-377 |
1.29e-22 |
|
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: 102.05 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEPYCK----SLNRRIGFVTQDDVLFtHLT 267
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ---GEVTLDGVPVSSldqdEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAALLRLPRTMTRQEKEERTIDIIYEL--GLercqDTMIGGSFVRgVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVGLADWLRALpdGL----DTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 346 SGLDSTTALRIIQLLHDiAEDGKTVITTIHQP 377
Cdd:TIGR02868 500 EHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
192-376 |
2.06e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLL--------------SILGGRVAGPGDVEGCVSYNDEPYCKSLNRRIGFVT 257
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLrcinflekpsegsiVVNGQTINLVRDKDGQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 258 QDDVLFTHLTVKETLTYAALLRLprTMTRQEKEERTIDIIYELGL-ERCQdtmigGSFVRGVSGGERKRVCIGNEIIINP 336
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIdERAQ-----GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
191-406 |
2.26e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.11 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGpgdVEGCVSYNDEPYCK----SLNRRIGFVTQDDVLFTHL 266
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTP---SSGEVRLNGRPLAAwspwELARRRAVLPQHSSLAFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETltyAALLRLPRTMTRQEKEERTIDIiyelgLERCQDTMIGGSFVRGVSGGERKRV------C-IGNEIIINPSLL 339
Cdd:COG4559 91 TVEEV---VALGRAPHGSSAAQDRQIVREA-----LALVGLAHLAGRSYQTLSGGEQQRVqlarvlAqLWEPVDGGPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPS-SRLFHkfDKLILLGRGSLLYFGKASEAM 406
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQGRLVAQGTPEEVL 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
191-375 |
2.42e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagPGDvEGCVSYNDE-----PycksLNRR----IGFVTQDDV 261
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV--KPD-SGRIFLDGEdithlP----MHKRarlgIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLtyAALLRLpRTMTRQEKEERTIDIIYELGLERCQDTMiGGSfvrgVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:COG1137 89 IFRKLTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKSK-AYS----LSGGERRRVEIARALATNPKFILL 160
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
191-404 |
2.51e-22 |
|
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: 96.07 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKS-LNRR----IGFVTQDDVLFTH 265
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-PD--SGKILLDGQDITKLpMHKRarlgIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLtyAALLRLpRTMTRQEKEERTIDIIYELGLERCQDTMiGGSfvrgVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:cd03218 90 LTVEENI--LAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSK-ASS----LSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTIHQpSSRLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
192-371 |
2.62e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 96.22 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVagpgDVEGcVSYNDEPycKSLN---RRIGFVTQDDV 261
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI----TVDG-EDLTDSK--KDINklrRKVGMVFQQFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTYAalLRLPRTMTRQEKEERTIDIIYELGL-ERCQdtmiggSFVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:COG1126 88 LFPHLTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGLaDKAD------AYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190
....*....|....*....|....*....|.
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
191-378 |
9.08e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVaGPGDVE--GCVSYNDEP-YCKSLNRRIGFVTQDD 260
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTI-RVGDITidTARSLSQQKgLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFTHLTVKETLTYAALlrLPRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:PRK11264 95 NLFPHRTVLENIIEGPV--IVKGEPKEEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPS 378
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
193-377 |
1.32e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGP-GDV----EGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLT 267
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSsGEVslvgQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAALLRlprTMTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:PRK10584 105 ALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|.
gi 1002256437 348 LDSTTALRIIQLLHDIAED-GKTVITTIHQP 377
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
192-371 |
1.35e-21 |
|
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: 94.28 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLL-SILGgrVAGPgdVEGCVSYNDEPycksLNRR---------IGFVTQDDV 261
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLkAISG--LLPP--RSGSIRFDGED----ITGLpphriarlgIGYVPEGRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTYAALLRLPRtmtrqEKEERTIDIIYEL--GLERCQDTMiGGSfvrgVSGGERKRVCIGNEIIINPSLL 339
Cdd:COG0410 89 IFPSLTVEENLLLGAYARRDR-----AEVRADLERVYELfpRLKERRRQR-AGT----LSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTIL 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
185-406 |
1.38e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.58 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 185 AVKGtpREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagPGDvEGCVSYNDE-----PYCKSLNRRIGFVTQD 259
Cdd:PRK10895 12 AYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV--PRD-AGNIIIDDEdisllPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHLTVKETLTyaALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMiGGSfvrgVSGGERKRVCIGNEIIINPSLL 339
Cdd:PRK10895 87 ASIFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-GQS----LSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLfHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
192-375 |
1.63e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.14 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEP--YCKS--LNRR--IGFVTQ--DDVLF 263
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNG-ILKP--TSGEVLIKGEPikYDKKslLEVRktVGIVFQnpDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYAAL-LRLPRtmtrQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK13639 93 AP-TVEEDVAFGPLnLGLSK----EEVEKRVKEALKAVGMEGFENKP-----PHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
193-406 |
1.77e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPY----CKSLNRRIGFVTQDDVLFTHLTV 268
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PT--AGTVLVAGDDVealsARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLPRTMTRQEKEERTIdiiyELGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAV----ERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVITTIHQPSsrLFHKF-DKLILLGRGSLLYFGKASEAM 406
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLD--LAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
192-375 |
2.14e-21 |
|
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: 93.20 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDVEGCVSYND---EPycKSLNRRIGFVTQDDVLFTHLTV 268
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT-LLKPTSGRATVAGHDvvrEP--REVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETL-TYAALLRLPRtmtrQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03265 91 WENLyIHARLYGVPG----AERRERIDELLDFVGLLEAADRL-----VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180
....*....|....*....|....*....
gi 1002256437 348 LDSTTALRIIQLLHDI-AEDGKTVITTIH 375
Cdd:cd03265 162 LDPQTRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
179-401 |
5.26e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 179 EVKYKVAVKGtpreilsgISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVagpgDVEGCVSYNDEpycKSLNR 251
Cdd:COG4586 31 EYREVEAVDD--------ISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvptSGEV----RVLGYVPFKRR---KEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 252 RIGFV----TQddvLFTHLTVKETLT-YAALLRLPRtmtrQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRv 326
Cdd:COG4586 96 RIGVVfgqrSQ---LWWDLPAIDSFRlLKAIYRIPD----AEYKKRLDELVELLDLGELLDTP-----VRQLSLGQRMR- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 327 CignEIII----NPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIH------QPSSRlfhkfdkLILLGRGS 395
Cdd:COG4586 163 C---ELAAallhRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHdmddieALCDR-------VIVIDHGR 232
|
....*.
gi 1002256437 396 LLYFGK 401
Cdd:COG4586 233 IIYDGS 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
192-376 |
7.16e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.46 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLL-------SILGGRVAgpgdVEGcVSYNDEPYCKSLNRR-IGFVTQDDVLF 263
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleEITSGDLI----VDG-LKVNDPKVDERLIRQeAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAAllRLPRTMTRQEKEERTIDIIYELGL-ERcqdtmiGGSFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK09493 90 PHLTALENVMFGP--LRVRGASKEEAEKQARELLAKVGLaER------AHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
192-371 |
7.87e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.75 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------------GGRvagpgDVegcvsyNDEPyckSLNRRIGFVTQ 258
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledptsgeiliGGR-----DV------TDLP---PKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 259 DDVLFTHLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSL 338
Cdd:COG3839 83 SYALYPHMTVYENIAFP--LKL-RKVPKAEIDRRVREAAELLGLEDLLD-----RKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002256437 339 LFLDEPTSGLDSttALRI-----IQLLHdiAEDGKTVI 371
Cdd:COG3839 155 FLLDEPLSNLDA--KLRVemraeIKRLH--RRLGTTTI 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
192-406 |
8.62e-21 |
|
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: 91.83 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPgdVEGCVSYNDEpYCKSLN-----RRIGFVTQDDVLFThL 266
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-RFYDP--TSGEILLDGV-DIRDLNlrwlrSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAallRLPRTMTRQEKEERTIDIiYEL--GLERCQDTMIGGsfvRGV--SGGERKRVCIGNEIIINPSLLFLD 342
Cdd:cd03249 92 TIAENIRYG---KPDATDEEVEEAAKKANI-HDFimSLPDGYDTLVGE---RGSqlSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
161-391 |
1.08e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.20 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 161 PRKKLMTEPTLPIYLKFAEVKYKVAvkgtpREILSGISGSAAPGEVLALMGPSGSGKTTLLSILggrvAGPGDV-EGCVS 239
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYPGR-----RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL----LGFVDPtEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 240 YNDEPYC----KSLNRRIGFVTQDDVLFTHlTVKETLtyaaLLRLP---RTMTRQEKEERTIDIIYElGLERCQDTMIGG 312
Cdd:TIGR02857 381 VNGVPLAdadaDSWRDQIAWVPQHPFLFAG-TIAENI----RLARPdasDAEIREALERAGLDEFVA-ALPQGLDTPIGE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 313 SfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSRlfHKFDKLILL 391
Cdd:TIGR02857 455 G-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA--ALADRIVVL 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
192-400 |
1.09e-20 |
|
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: 91.63 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGCVSYNDEpycKSLNRRIGFVT-QDDVLFTHLT 267
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqptSGEVRVAGLVPWKRR---KKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLtyaallRLPRTMTRQEKEE--RTIDIIYE-LGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:cd03267 112 VIDSF------YLLAAIYDLPPARfkKRLDELSElLDLEELLDTP-----VRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 345 TSGLDSTTALRIIQLLHDI-AEDGKTVITTIH--QPSSRLfhkFDKLILLGRGSLLYFG 400
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
202-400 |
1.16e-20 |
|
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: 91.02 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 202 APGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVegCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLtyaALLRL 280
Cdd:cd03298 22 AQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRV--LINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNV---GLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 281 PRTMTRQEKEERTIDIIYELGLE----RCQDTMiggsfvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSttALR- 355
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAglekRLPGEL---------SGGERQRVALARVLVRDKPVLLLDEPFAALDP--ALRa 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 356 -IIQLLHDI-AEDGKTVITTIHQPSSRLfHKFDKLILLGRGSLLYFG 400
Cdd:cd03298 166 eMLDLVLDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
193-406 |
1.28e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.71 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPGdvEGCVSYNdepyCKSLNRRIGFVTQDDVLFTH 265
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDG--VPLVQYD----HHYLHRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 lTVKETLTYAALLRLPRTMTRQEKEERTIDIIYElgLERCQDTMIG--GSFvrgVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIME--FPNGYDTEVGekGSQ---LSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 344 PTSGLDSttalRIIQLLHDIAE-DGKTVITTIHQPSsrLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:TIGR00958 644 ATSALDA----ECEQLLQESRSrASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
187-406 |
1.81e-20 |
|
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: 90.75 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPreILSGISGSAAPGEVLALMGPSGSGKTTLLSILgGRVAGPGdvEGCVSYNDEPYC----KSLNRRIGFVTQDDVL 262
Cdd:cd03254 14 EKKP--VLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MRFYDPQ--KGQILIDGIDIRdisrKSLRSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHlTVKETLTYAallRLPRTMTRQEKEERTIDIIYEL-GLERCQDTMIG--GSfvrGVSGGERKRVCIGNEIIINPSLL 339
Cdd:cd03254 89 FSG-TIMENIRLG---RPNATDEEVIEAAKEAGAHDFImKLPNGYDTVLGenGG---NLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSRLFHkfDKLILLGRGSLLYFGKASEAM 406
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDELL 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
194-371 |
2.03e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 92.81 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTL-LSILgGRVAGPGDVEGCVSYNDEP--------YCKSLNRRIGFVTQDDvlFT 264
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLaRAIL-GLLPPPGITSGEILFDGEDllklsekeLRKIRGREIQMIFQDP--MT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HL----TVKETLTYAalLRLPRTMTRQEKEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:COG0444 98 SLnpvmTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPERRL--DRYPHELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAED-GKTVI 371
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRElGLAIL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
200-406 |
2.79e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.20 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 200 SAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKSL--NRRIGFVTQDDVLFTHLTVKETLtyaAL 277
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLP-PD--SGRILWNGQDLTALPpaERPVSMLFQENNLFPHLTVAQNI---GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 -----LRLprtmTRQEKeERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDStt 352
Cdd:COG3840 95 glrpgLKL----TAEQR-AQVEQALERVGLAGLLDRLPG-----QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP-- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 353 ALR--IIQLLHDIA-EDGKTVITTIHQPS--SRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:COG3840 163 ALRqeMLDLVDELCrERGLTVLMVTHDPEdaARI---ADRVLLVADGRIAADGPTAALL 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
188-406 |
2.90e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 95.17 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPGdvEGCVSYNDEPY----CKSLNRRIGFVTQDDVLF 263
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP-RFYEPD--SGQILLDGHDLadytLASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYAALLRLPRtmtrqEKEERTIDIIYEL----GLERCQDTMIGGSFVRgVSGGERKRVCIGNEIIINPSLL 339
Cdd:TIGR02203 419 ND-TIANNIAYGRTEQADR-----AEIERALAAAYAQdfvdKLPLGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 340 FLDEPTSGLDSTTAlRIIQLLHDIAEDGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:TIGR02203 492 ILDEATSALDNESE-RLVQAALERLMQGRTTLVIAHRLST--IEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
184-410 |
3.53e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.81 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 184 VAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCV--------SYNDEpyckSLNRRIGF 255
Cdd:COG4618 338 VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG-VWPP--TAGSVrldgadlsQWDRE----ELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 256 VTQDDVLFTHlTVKETLTyaallRLPrtmtrQEKEERTI---------DIIyeLGLERCQDTMIG--GSfvrGVSGGERK 324
Cdd:COG4618 411 LPQDVELFDG-TIAENIA-----RFG-----DADPEKVVaaaklagvhEMI--LRLPDGYDTRIGegGA---RLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 325 RVCI-----GneiiiNPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSsrLFHKFDKLILLGRGSLLYF 399
Cdd:COG4618 475 RIGLaralyG-----DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAF 547
|
250
....*....|.
gi 1002256437 400 GKASEAMPYFQ 410
Cdd:COG4618 548 GPRDEVLARLA 558
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
192-360 |
3.67e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.87 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCKS--------LNRRIGFVTQddvlF 263
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTP--TSGDVIFNGQPMSKLssaakaelRNQKLGFIYQ----F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKET-LTYAALLRLPRTMTRQEKEERTIDIIYELGLERcqdtmiggsfvRG------VSGGERKRVCIGNEIIINP 336
Cdd:PRK11629 96 HHLLPDFTaLENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-----------RAnhrpseLSGGERQRVAIARALVNNP 164
|
170 180
....*....|....*....|....
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLL 360
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLL 188
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
188-394 |
6.67e-20 |
|
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: 87.66 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLS-ILGGRVAGPGDVE-GCVSYNDEpYCKSLNRRIGFVTQDDVLFth 265
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLLRPTSGRVRlDGADISQW-DPNELGDHVGYLPQDDELF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 ltvketltyaallrlprtmtrqekeERTI-DIIyelglercqdtmiggsfvrgVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:cd03246 89 -------------------------SGSIaENI--------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002256437 345 TSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSsrLFHKFDKLILLGRG 394
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
194-373 |
1.67e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.59 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILggrvAG---PgDvEGCVSYNDEPYCKSL---NRRIGFVTQDDVLFTHLT 267
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRII----AGletP-D-SGRIVLNGRDLFTNLpprERRVGFVFQHYALFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLtyAALLRLpRTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:COG1118 92 VAENI--AFGLRV-RPPSKAEIRARVEELLELVQLEG-----LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 348 LDS--TTALR--IIQLLHDIaeDGKTVITT 373
Cdd:COG1118 164 LDAkvRKELRrwLRRLHDEL--GGTTVFVT 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
192-373 |
2.18e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILG-------G--RVAGPGdvegcVSYNDEPYCK---SLNRRIGFVTQD 259
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlletpdsGqlNIAGHQ-----FDFSQKPSEKairLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHLTVKETLTYAALLRLprTMTRQEKEERTIDIiyelgLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLL 339
Cdd:COG4161 91 YNLWPHLTVMENLIEAPCKVL--GLSKEQAREKAMKL-----LARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKT-VITT 373
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITqVIVT 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
194-406 |
2.21e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILgGRVAGPgdVEGCVSYNDEPYCK----SLNRRIGFVTQDDVLFTHLTVK 269
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIEP--TSGEIFIDGEDIREqdpvELRRKIGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETL-TYAALLRLPrtmtRQEKEERTIDIIYELGLERCQdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:cd03295 94 ENIaLVPKLLKWP----KEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 349 DSTTALRIIQLLHDIAED-GKTVITTIH--QPSSRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:cd03295 167 DPITRDQLQEEFKRLQQElGKTIVFVTHdiDEAFRL---ADRIAIMKNGEIVQVGTPDEIL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
191-406 |
3.17e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.90 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYC----KSLNRRIGFVTQDDVLFTHL 266
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS-PD--SGEVRLNGRPLAdwspAELARRRAVLPQHSSLSFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLtyaALLRLPRTMTRQEKEErtidiIYELGLERCQDTMIGGSFVRGVSGGERKRV----------CIGNEiiinP 336
Cdd:PRK13548 92 TVEEVV---AMGRAPHGLSRAEDDA-----LVAAALAQVDLAHLAGRDYPQLSGGEQQRVqlarvlaqlwEPDGP----P 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIH------QPSsrlfhkfDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnlaaRYA-------DRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
192-377 |
3.95e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG---------RVAGPgdvegCVSYNDEPYCKSLNRR-IGFVTQDDV 261
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCldkptsgtyRVAGQ-----DVATLDADALAQLRREhFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLT----VKETLTYAALlrlprtmTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPS 337
Cdd:PRK10535 97 LLSHLTaaqnVEVPAVYAGL-------ERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
191-350 |
4.42e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPGDVEGCVSYN--DEPYCKSLNRRIGFVTQDDVLFTHLTV 268
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQTSGHIRFHgtDVSRLHARDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYaALLRLPRtmtRQEKEERTIDIIYELGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK10851 92 FDNIAF-GLTVLPR---RERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
..
gi 1002256437 349 DS 350
Cdd:PRK10851 168 DA 169
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
192-376 |
4.70e-19 |
|
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: 86.87 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILG-------GRVAgpgdVEGC-VSYNDEPYCKSLNRRIGFVTQDDVLF 263
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINglerptsGSVL----VDGTdLTLLSGKELRKARRRIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAalLRLPRtMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:cd03258 95 SSRTVFENVALP--LEIAG-VPKAEIEERVLELLELVGLEDKAD-----AYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 344 PTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQ 376
Cdd:cd03258 167 ATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
193-396 |
6.59e-19 |
|
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: 84.67 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPgdvEGCVSYNDEP---YCKSLNRRIGFVTQDDVLFthltvk 269
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVPvsdLEKALSSLISVLNQRPYLF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 etltyaallrlprtmtrqekeertidiiyelglercqDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:cd03247 88 -------------------------------------DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 350 STTALRIIQLLHDIAEDgKTVITTIHQPSSrlFHKFDKLILLGRGSL 396
Cdd:cd03247 131 PITERQLLSLIFEVLKD-KTLIWITHHLTG--IEHMDKILFLENGKI 174
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
190-410 |
7.24e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPGdvEGCVSYNDEP---YCKS-LNRRIGFVTQDDVLFTH 265
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQ--QGEILLNGQPiadYSEAaLRQAISVVSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 lTVKETLTYAAllrlprtmtRQEKEERTIDIIYELGLERCQDTMIG-----GSFVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:PRK11160 429 -TLRDNLLLAA---------PNASDEALIEVLQQVGLEKLLEDDKGlnawlGEGGRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDgKTVITTIHqpssRLF--HKFDKLILLGRGSLLYFGKASEAMP----YFQ 410
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQN-KTVLMITH----RLTglEQFDRICVMDNGQIIEQGTHQELLAqqgrYYQ 569
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
191-375 |
8.11e-19 |
|
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: 85.38 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLL-------SILGGRV-AGPGDVegcvsyND-EPYckslNRRIGFVTQDDV 261
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLrmiagleEPTSGRIyIGGRDV------TDlPPK----DRDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:cd03301 83 LYPHMTVYDNIAFG--LKL-RKVPKDEIDERVREVAELLQIEHLLD-----RKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002256437 342 DEPTSGLDSttALRI-----IQLLHdiAEDGKTVITTIH 375
Cdd:cd03301 155 DEPLSNLDA--KLRVqmraeLKRLQ--QRLGTTTIYVTH 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
192-373 |
1.14e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.84 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILG-------GRVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQDDVLFT 264
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLNIAGNHFDFSKTPSDKAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAALLRLprTMTRQEKEERTIDIiyelgLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:PRK11124 96 HLTVQQNLIEAPCRVL--GLSKDQALARAEKL-----LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 345 TSGLDSTTALRIIQLLHDIAEDGKT-VITT 373
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITqVIVT 198
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
193-427 |
1.26e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSYNDEPY---CKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG-MTSPD--AGKITVLGVPVparARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAAllRLPRTMTRQEkeERTIDIIYELG-LERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK13536 133 ENLLVFG--RYFGMSTREI--EAVIPSLLEFArLESKADAR-----VSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVITTIH--QPSSRLfhkFDKLILLGRGSllyfgKASEAMPYF---QSIGCtPLIAM--- 420
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGR-----KIAEGRPHAlidEHIGC-QVIEIygg 274
|
....*..
gi 1002256437 421 NPAEFLL 427
Cdd:PRK13536 275 DPHELSS 281
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
194-404 |
1.41e-18 |
|
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: 85.47 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDveGCVSYNDEPYCK--SLNRRIGFVTQDDVLFTHLTVKET 271
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDvpVQERNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 272 LTYAalLRLPRTMTR---QEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:cd03296 95 VAFG--LRVKPRSERppeAEIRAKVHELLKLVQLDWLAD-----RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 349 DSTT--ALR-IIQLLHDiaEDGKTVITTIHQPSSRLfHKFDKLILLGRGSLLYFGKASE 404
Cdd:cd03296 168 DAKVrkELRrWLRRLHD--ELHVTTVFVTHDQEEAL-EVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
193-349 |
1.44e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 85.37 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVE-GCVSYNDEPYCKslnRRIGFVTQDDVLFTHLTVKE 270
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILlDGKDITNLPPHK---RPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 271 TLTYAalLRLpRTMTRQEKEERTIDIIYELGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:cd03300 92 NIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
191-381 |
1.49e-18 |
|
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: 89.88 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPG-DVEGcVSYndepycKSLNRRIGFVTQDDVL 262
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGRILIDGqDIRD-VTQ------ASLRAAIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHlTVKETLTYAallrlpRTMTRQEKEERTIDI--IYE--LGLERCQDTMIGGsfvRGV--SGGERKRVCIGNEIIINP 336
Cdd:COG5265 444 FND-TIAYNIAYG------RPDASEEEVEAAARAaqIHDfiESLPDGYDTRVGE---RGLklSGGEKQRVAIARTLLKNP 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002256437 337 SLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHqpssRL 381
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH----RL 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
191-396 |
1.66e-18 |
|
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: 85.22 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPGDvegCVSYNDEPYcksLNRRIGFVTQDDVLF 263
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVLLDGK---PISQYEHKY---LHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYA-ALLRLPRTMTRQEKEErTIDIIYELGLERCQDTMIGGSFVrgvSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:cd03248 101 AR-SLQDNIAYGlQSCSFECVKEAAQKAH-AHSFISELASGYDTEVGEKGSQL---SGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDgKTVITTIHQPSsrLFHKFDKLILLGRGSL 396
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGGRI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
194-400 |
2.58e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSY--NDEPYCKSLNRRI-------GFVTQDDVLFT 264
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELlgRTVQREGRLARDIrksrantGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAALLRLP--RTMTR---QEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLL 339
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwRTCFSwftREQKQRALQALTRVGMVH-----FAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAE-DGKTVITTIHQPSSRLFHkFDKLILLGRGSLLYFG 400
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRY-CERIVALRQGHVFYDG 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
193-406 |
3.55e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPgdVEGCVSYNDEPYC----KSLNRRIGFVTQDDVLFTHLTV 268
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTP--QSGTVFLGDKPISmlssRQLARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTY--AALLRLPRTMTRQEKEertidiIYELGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:PRK11231 94 RELVAYgrSPWLSLWGRLSAEDNA------RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTVITTIH--QPSSRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLHdlNQASRY---CDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
166-423 |
3.88e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 166 MTEPTLPIylKFAEVKYkvavkgTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILG--GRVAGPGDVEGCVSYNDE 243
Cdd:PRK14239 1 MTEPILQV--SDLSVYY------NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 244 ----PYCKS--LNRRIGFVTQDDVLFThLTVKETLTYAalLRLprtmtRQEKEERTIDIIYELGL----------ERCQD 307
Cdd:PRK14239 73 niysPRTDTvdLRKEIGMVFQQPNPFP-MSIYENVVYG--LRL-----KGIKDKQVLDEAVEKSLkgasiwdevkDRLHD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 308 TMIGgsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDgKTVITTIH--QPSSRLfhkF 385
Cdd:PRK14239 145 SALG------LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRsmQQASRI---S 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 1002256437 386 DKLILLGRGSLLYFGKASEampyfqsigctplIAMNPA 423
Cdd:PRK14239 215 DRTGFFLDGDLIEYNDTKQ-------------MFMNPK 239
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
194-406 |
5.85e-18 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 87.83 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILgGRVAGPgdVEGCVSYNDEPYC----KSLNRRIGFVTQDDVLFTHlTVK 269
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLL-LRFYDP--QSGRILLDGVDLRqldpAELRARMALVPQDPVLFAA-SVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAALlrlprTMTRQEKEERTIDII---YELGLERCQDTMIGGsfvRGV--SGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:TIGR02204 432 ENIRYGRP-----DATDEEVEAAARAAHaheFISALPEGYDTYLGE---RGVtlSGGQRQRIAIARAILKDAPILLLDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 345 TSGLDSTTALRIIQLLhDIAEDGKTVITTIHQPSSRLfhKFDKLILLGRGSLLYFGKASEAM 406
Cdd:TIGR02204 504 TSALDAESEQLVQQAL-ETLMKGRTTLIIAHRLATVL--KADRIVVMDQGRIVAQGTHAELI 562
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
206-406 |
8.83e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 206 VLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPYCKSLN--------RRIGFVTQDDVLFTHLTVKETLTYAal 277
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTR-PQ--KGRIVLNGRVLFDAEKgiclppekRRIGYVFQDARLFPHYKVRGNLRYG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 lrlprtMTRQEKEERTiDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRII 357
Cdd:PRK11144 101 ------MAKSMVAQFD-KIVALLGIEPLLD-----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 358 QLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGK-----ASEAM 406
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
183-375 |
1.09e-17 |
|
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: 81.80 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 183 KVAVKGtpREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPGdvegcvsYNdepyckslnrrigfVTQDDVL 262
Cdd:cd03217 7 HVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PK-------YE--------------VTEGEIL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 F-----THLTVKETltyaALLRLprTMTRQEKEE----RTIDiiyelglercqdtmiggsFVRGV----SGGERKRVCIG 329
Cdd:cd03217 61 FkgediTDLPPEER----ARLGI--FLAFQYPPEipgvKNAD------------------FLRYVnegfSGGEKKRNEIL 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 330 NEIIINPSLLFLDEPTSGLDsTTALRII-QLLHDIAEDGKTVITTIH 375
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLD-IDALRLVaEVINKLREEGKSVLIITH 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
188-394 |
1.37e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPreILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG--------------RVAGPGDVEGCVsyndepyckslnrri 253
Cdd:PRK11248 13 GKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfvpyqhgsitldgkPVEGPGAERGVV--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 254 gFvtQDDVLFTHLTVKETLTYAalLRLpRTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEII 333
Cdd:PRK11248 76 -F--QNEGLLPWRNVQDNVAFG--LQL-AGVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQPSSRLFHKFDkLILLGRG 394
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATE-LVLLSPG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
194-404 |
1.81e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 82.13 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDveGCVSYNDEPYCKSLNRRIgFVTQDDVLFTHLTVKETLt 273
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPTS--GGVILEGKQITEPGPDRM-VVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 YAALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 354 LRIIQLLHDIAED-GKTVITTIHQPSSRLFHKfDKLILLGRGSLLYFGKASE 404
Cdd:TIGR01184 151 GNLQEELMQIWEEhRVTVLMVTHDVDEALLLS-DRVVMLTNGPAANIGQILE 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
194-404 |
2.25e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 83.23 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLL-SILGgrVAGPgDvEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETL 272
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILG--ILAP-D-SGEVLWDGEPLDPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 273 TYaaLLRLpRTMTRQEKEERTIDIIYELGL-ERCQDTmiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDST 351
Cdd:COG4152 93 VY--LARL-KGLSKAEAKRRADEWLERLGLgDRANKK------VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 352 TALRIIQLLHDIAEDGKTVITTIHQPSS--RLfhkFDKLILLGRGSLLYFGKASE 404
Cdd:COG4152 164 NVELLKDVIRELAAKGTTVIFSSHQMELveEL---CDRIVIINKGRKVLSGSVDE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
180-360 |
3.25e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 180 VKYKVAVKGtpreilsgISGSAAPGEVLALMGPSGSGKTT----LLSILGGRvagpgdveGCVSYNDEPYCK-------S 248
Cdd:PRK15134 296 VDHNVVVKN--------ISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ--------GEIWFDGQPLHNlnrrqllP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 249 LNRRIGFVTQD--DVLFTHLTVKETLtyAALLRLPR-TMTRQEKEERTIDIIYELGLERCQDTMIGGSFvrgvSGGERKR 325
Cdd:PRK15134 360 VRHRIQVVFQDpnSSLNPRLNVLQII--EEGLRVHQpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQRQR 433
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 326 VCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLL 360
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALL 468
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
183-375 |
5.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 183 KVAVKGTPREI--LSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVEgcVSYNDE---------------- 243
Cdd:PRK13651 10 KIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlLLPDTGTIE--WIFKDEknkkktkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 244 ----------PYCKSLNRRIGFVTQ--DDVLFTHlTVKETLTYAallrlPRTM--TRQEKEERTIDIIYELGLErcQDTM 309
Cdd:PRK13651 88 viqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFG-----PVSMgvSKEEAKKRAAKYIELVGLD--ESYL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 310 IGGSFvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK13651 160 QRSPF--ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
194-380 |
7.07e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLL------------SIL----GGRV----AGPGDVegcvsyndepycksLN-RR 252
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLkciygnylpdsgSILvrhdGGWVdlaqASPREI--------------LAlRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 253 --IGFVTQddvlftHLTV-----KETLTYAALLRlpRTMTRQEKEERTIDIIYELGL-ERCQD----TmiggsFvrgvSG 320
Cdd:COG4778 93 rtIGYVSQ------FLRViprvsALDVVAEPLLE--RGVDREEARARARELLARLNLpERLWDlppaT-----F----SG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSR 380
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
191-349 |
7.81e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPGDVegcvsyndepyckslnrRIGFVTQDDVLF 263
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILagelepdSGEVSIPKGL-----------------RIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLtYAALLRLPRTMTRQEKEERTIDIIYELG--LERCQDTM--IGG----SFVRGV----------------- 318
Cdd:COG0488 74 DDLTVLDTV-LDGDAELRALEAELEELEAKLAEPDEDLerLAELQEEFeaLGGweaeARAEEIlsglgfpeedldrpvse 152
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 319 -SGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:COG0488 153 lSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
191-377 |
8.39e-17 |
|
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: 79.32 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYCK---SLNRRIGFVTQDDVLFTHLT 267
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR---PDSGEVRWNGTPLAEqrdEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLT-YAALLRlprtmtrqeKEERTI-DIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:TIGR01189 90 ALENLHfWAAIHG---------GAQRTIeDALAAVGLTGFEDLP-----AAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
184-377 |
9.79e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 184 VAVKGtpREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPG-DV-EGCVSYNDEpyckSL---------NRR 252
Cdd:COG0396 8 VSVEG--KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH---PKyEVtSGSILLDGE----DIlelspderaRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 253 IGFVTQDDVLFTHLTVKETLTYAALLRLPRTMTRQEKEERTIDIIYELGLERcqdtmiggSFV-RGV----SGGERKRvc 327
Cdd:COG0396 79 IFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE--------DFLdRYVnegfSGGEKKR-- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 328 igNEI----IINPSLLFLDEPTSGLDStTALRII-QLLHDIAEDGKTVITTIHQP 377
Cdd:COG0396 149 --NEIlqmlLLEPKLAILDETDSGLDI-DALRIVaEGVNKLRSPDRGILIITHYQ 200
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
193-414 |
1.26e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSYNDEP---YCKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG-LTHPD--AGSISLCGEPvpsRARHARQRVGVVPQFDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLtyaalLRLPR--TMTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:PRK13537 99 ENL-----LVFGRyfGLSAAAARALVPPLLEFAKLENKADAK-----VGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIH--QPSSRLFHkfdKLILLGRGSLLYFGKASEAMPyfQSIGC 414
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHfmEEAERLCD---RLCVIEEGRKIAEGAPHALIE--SEIGC 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
191-377 |
1.43e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYckslnRRIGFVTQDDVLFT-HLT-V 268
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARP--DAGEVLWQGEPI-----RRQRDEYHQDLLYLgHQPgI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK13538 86 KTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVP-----VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*....
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
177-371 |
1.47e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 177 FAEVKYKVAVKgtpREILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPG-DVEGcVSYndepycKS 248
Cdd:PRK13657 337 FDDVSFSYDNS---RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGtDIRT-VTR------AS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 249 LNRRIGFVTQDDVLFTHlTVKETLtyaallRLPRT------MTRQEKEERTIDIIyeLGLERCQDTMIGGsfvRG--VSG 320
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNR-SIEDNI------RVGRPdatdeeMRAAAERAQAHDFI--ERKPDGYDTVVGE---RGrqLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI 525
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
184-406 |
1.57e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 184 VAVkgTPReiLSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDV---EGCVSynDEPYCKSLNRRIGFVTQDD 260
Cdd:PRK03695 6 VAV--STR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIqfaGQPLE--AWSAAELARHRAYLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFThLTVKETLTyaalLRLPrTMTRQEKEERTIDIIYE-LGLercQDTMigGSFVRGVSGGERKRVCIGNEII-----I 334
Cdd:PRK03695 80 PPFA-MPVFQYLT----LHQP-DKTRTEAVASALNEVAEaLGL---DDKL--GRSVNQLSGGEWQRVRLAAVVLqvwpdI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 335 NPS--LLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpSSRLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK03695 149 NPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD-LNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
180-363 |
2.89e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.42 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 180 VKYKVAVKGtpreilsgISGSAAPGEVLALMGPSGSGKTTL-LSILG-----GRVAgpgdvegcvsYNDEPY-------C 246
Cdd:COG4172 296 VGHVKAVDG--------VSLTLRRGETLGLVGESGSGKSTLgLALLRlipseGEIR----------FDGQDLdglsrraL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 247 KSLNRRIGFVTQDDvlFTHL----TVKETLTyAALLRLPRTMTRQEKEERTIDIIYELGLERcqDTMigGSFVRGVSGGE 322
Cdd:COG4172 358 RPLRRRMQVVFQDP--FGSLsprmTVGQIIA-EGLRVHGPGLSAAERRARVAEALEEVGLDP--AAR--HRYPHEFSGGQ 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002256437 323 RKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
193-397 |
5.05e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.69 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYC-------KSLNRRIGFVTQD--DVLF 263
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEKP--AQGTVSFRGQDLYqldrkqrRAFRRDVQLVFQDspSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGLercqDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:TIGR02769 103 PRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGL----RSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpSSRLFHKF-DKLILLGRGSLL 397
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAFGTAYLFITH-DLRLVQSFcQRVAVMDKGQIV 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
200-366 |
5.51e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 200 SAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEPYCKS--LNRRIGFVTQDDVLFTHLTVKETLtyaAL 277
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNGQDHTTTppSRRPVSMLFQENNLFSHLTVAQNI---GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 -----LRLprtmTRQEKEERTiDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDStt 352
Cdd:PRK10771 95 glnpgLKL----NAAQREKLH-AIARQMGIEDLLARLPG-----QLSGGQRQRVALARCLVREQPILLLDEPFSALDP-- 162
|
170
....*....|....*.
gi 1002256437 353 ALR--IIQLLHDIAED 366
Cdd:PRK10771 163 ALRqeMLTLVSQVCQE 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
191-406 |
5.88e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGD-----VEGCVSYNDEPYCK----SLNRRIGFVTQDDV 261
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgarVTGDVTLNGEPLAAidapRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 262 LFTHLTVKETLTyaaLLRLPRTMTRQEKEERTIDIIYElGLERCQDTMIGGSFVRGVSGGERKRVCIG---------NEI 332
Cdd:PRK13547 94 PAFAFSAREIVL---LGRYPHARRAGALTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQFArvlaqlwppHDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 333 IINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKT-VITTIHQPSSRLFHKfDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHA-DRIAMLADGAIVAHGAPADVL 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
194-371 |
6.23e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSYNDEPYC-----KSLNRRIGFVTQDDVLFTHLTV 268
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG-VYQPD--SGEILLDGEPVRfrsprDAQAAGIAIIHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLtyaALLRLPRT---MTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:COG1129 97 AENI---FLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTP-----VGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180
....*....|....*....|....*.
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
188-363 |
6.42e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 81.27 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKT-TLLSILGGRVAGPGDVEGCVSYNDEPYC----KSLNR----RIGFVTQ 258
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAHPSGSILFDGQDLLglseRELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 259 D-----DVLFthlTVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGL---ERCQDtmiggSFVRGVSGGERKRVCIGN 330
Cdd:COG4172 100 EpmtslNPLH---TIGKQI--AEVLRLHRGLSGAAARARALELLERVGIpdpERRLD-----AYPHQLSGGQRQRVMIAM 169
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 331 EIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDL 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
191-377 |
6.86e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgdVEGCVSYNDEPYCKSLNR-RIGFVTQDDVLFTHLTVK 269
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-P--AAGTIKLDGGDIDDPDVAeACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTY-AALLRlprtmTRQEKEERTIDIIyelGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK13539 92 ENLEFwAAFLG-----GEELDIAAALEAV---GLAPLAHLPFG-----YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*....
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
187-369 |
1.32e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYC-------KSLNRRIGFVTQD 259
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESP--SQGNVSWRGEPLAklnraqrKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DV--LFTHLTVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGLercqDTMIGGSFVRGVSGGERKRVCIGNEIIINPS 337
Cdd:PRK10419 98 SIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDL----DDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDIAEDGKT 369
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
203-375 |
1.52e-15 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 77.30 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEG--CVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAal 277
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLIeptSGKVLIDGqdIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFG-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 LRLpRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRII 357
Cdd:cd03294 127 LEV-QGVPRAEREERAAEALELVGLEGWEH-----KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170
....*....|....*....
gi 1002256437 358 QLLHDI-AEDGKTVITTIH 375
Cdd:cd03294 201 DELLRLqAELQKTIVFITH 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
191-406 |
1.53e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPGdvEGCVSYNDEPY----CKSLNRRIGFVTQDDVLFTHL 266
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-RHQPPS--EGEILLDAQPLeswsSKAFARKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLT------YAALLRLprtmtRQEKEERTIDIIYELGLercqdTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:PRK10575 101 TVRELVAigrypwHGALGRF-----GAADREKVEEAISLVGL-----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIH--QPSSRLfhkFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHdiNMAARY---CDYLVALRGGEMIAQGTPAELM 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
191-366 |
1.60e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSIL--------GGRVagpgdvEGCVSYNDEP-YCKSLN-----RRIGFV 256
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGARV------EGEILLDGEDiYDPDVDvvelrRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQDDVLFTHlTVKETLTYAalLRLPRTMTRQEKEERTI-------------DIIYELGLercqdtmiggsfvrGVSGGER 323
Cdd:COG1117 98 FQKPNPFPK-SIYDNVAYG--LRLHGIKSKSELDEIVEeslrkaalwdevkDRLKKSAL--------------GLSGGQQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002256437 324 KRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED 366
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
175-404 |
1.60e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYKVAvKGTprEILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCKS------ 248
Cdd:PRK13636 6 LKVEELNYNYS-DGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNG-ILKP--SSGRILFDGKPIDYSrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 249 LNRRIGFVTQ--DDVLFThLTVKETLTYAAL-LRLPRtmtrQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKR 325
Cdd:PRK13636 80 LRESVGMVFQdpDNQLFS-ASVYQDVSFGAVnLKLPE----DEVRKRVDNALKRTGIEHLKDKP-----THCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 326 VCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQPSSRLFHkFDKLILLGRGSLLYFGKASE 404
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLY-CDNVFVMKEGRVILQGNPKE 228
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
191-403 |
2.43e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 76.15 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagpgdvegcvsyndePYCKSLNRRIGFVTQDdvlFTHLTVKE 270
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH----------------PSYEVTSGTILFKGQD---LLELEPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 T-----------------LTYAALLRLPRTMTRQEKEERTIDII-YELGLERCQDTM-IGGSFVR-----GVSGGERKRv 326
Cdd:TIGR01978 74 RaraglflafqypeeipgVSNLEFLRSALNARRSARGEEPLDLLdFEKLLKEKLALLdMDEEFLNrsvneGFSGGEKKR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 327 cigNEI----IINPSLLFLDEPTSGLDsTTALRII-QLLHDIAEDGKTVITTIHQPssRLFH--KFDKLILLGRGSLLYF 399
Cdd:TIGR01978 153 ---NEIlqmaLLEPKLAILDEIDSGLD-IDALKIVaEGINRLREPDRSFLIITHYQ--RLLNyiKPDYVHVLLDGRIVKS 226
|
....
gi 1002256437 400 GKAS 403
Cdd:TIGR01978 227 GDVE 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
191-377 |
3.35e-15 |
|
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: 74.84 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCK---SLNRRIGFVTQDDVLFTHLT 267
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG-LSPP--LAGRVLLNGGPLDFqrdSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAAllrlprtmtRQEKEERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:cd03231 90 VLENLRFWH---------ADHSDEQVEEALARVGLNGFEDRPVA-----QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIHQP 377
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
175-375 |
4.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYkVAVKGTP--REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYND--------EP 244
Cdd:PRK13646 3 IRFDNVSY-TYQKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK---PTTGTVTVDDitithktkDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 245 YCKSLNRRIGFVTQ--DDVLFTHLTVKEtltyaaLLRLPRT--MTRQEKEERTIDIIYELGLERcqDTMIGGSFvrGVSG 320
Cdd:PRK13646 79 YIRPVRKRIGMVFQfpESQLFEDTVERE------IIFGPKNfkMNLDEVKNYAHRLLMDLGFSR--DVMSQSPF--QMSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIH 375
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
192-361 |
4.51e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG--RVAGpGDVE--GCVSYNDEPYckslNRRIGFVTQDDVLFTHLT 267
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRITS-GEIWigGRVVNELEPA----DRDIAMVFQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAalLRLpRTMTRQEKEERTIDI--IYELG--LERCQdtmiggsfvRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:PRK11650 93 VRENMAYG--LKI-RGMPKAEIEERVAEAarILELEplLDRKP---------RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180
....*....|....*....|...
gi 1002256437 344 PTSGLDSttALRI-----IQLLH 361
Cdd:PRK11650 161 PLSNLDA--KLRVqmrleIQRLH 181
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
192-378 |
4.74e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.65 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILG--------GRVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQDDVLF 263
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneeARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKET----LTYAALLRlprtmTRQEKEERTIDIIYELGL-ERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSL 338
Cdd:PRK14267 98 PHLTIYDNvaigVKLNGLVK-----SKKELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTiHQPS 378
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
193-400 |
4.76e-15 |
|
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: 74.84 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPgdVEGCVSYNDEPYCK----SLNRRIGFVTQDDVLFTHlTV 268
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVEL--SSGSILIDGVDISKiglhDLRSRISIIPQDPVLFSG-TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTyaallrlPRTmtrQEKEERTIDIiyelgLERCQ------------DTMI--GGSFVrgvSGGERKRVCIGNEIII 334
Cdd:cd03244 95 RSNLD-------PFG---EYSDEELWQA-----LERVGlkefveslpgglDTVVeeGGENL---SVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQLLHDiAEDGKTVITTIHqpssRL--FHKFDKLILLGRGSLLYFG 400
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLdtIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
194-371 |
6.05e-15 |
|
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: 73.62 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVEGC-VSYNDEPYCKSLNRRIGFVTQD---DVLFTHLTV 268
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGlRPPASGEITLDgKPVTRRSPRDAIRAGIAYVPEDrkrEGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLrlprtmtrqekeertidiiyelglercqdtmiggsfvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:cd03215 96 AENIALSSLL----------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180
....*....|....*....|...
gi 1002256437 349 DSTTALRIIQLLHDIAEDGKTVI 371
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVL 158
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
192-349 |
6.39e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDV--EGCVsYNDEPYCKslnRRIGFVTQDDVLFTHLTV 268
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDSGRImlDGQD-ITHVPAEN---RHVNTVFQSYALFPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAalLRLPRTmTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK09452 104 FENVAFG--LRMQKT-PAAEITPRVMEALRMVQLEE-----FAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
.
gi 1002256437 349 D 349
Cdd:PRK09452 176 D 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
193-395 |
6.42e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.04 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLS-ILG------GRVAGPGDVeGCVSynDEPYCksLNRRIgfvtQDDVLFT- 264
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGeleklsGSVSVPGSI-AYVS--QEPWI--QNGTI----RENILFGk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 ---HLTVKETLTYAALLRlprtmtrqekeertiDI-IYELGLErcqdTMIGgsfVRGV--SGGERKRVCIGNEIIINPSL 338
Cdd:cd03250 91 pfdEERYEKVIKACALEP---------------DLeILPDGDL----TEIG---EKGInlSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQ-LLHDIAEDGKTVITTIHQPSsrLFHKFDKLILLGRGS 395
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
186-371 |
6.43e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 186 VKG-TPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrvAGPGDvEGCVSYNDEPYC-----KSLNRRIGFVTQD 259
Cdd:COG1129 259 VEGlSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG--ADPAD-SGEIRLDGKPVRirsprDAIRAGIAYVPED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 ---DVLFTHLTVKETLTYAALLRLPRTMTRQEKEERTI--DIIYELGLeRCQDTmigGSFVRGVSGGERKRVCIGNEIII 334
Cdd:COG1129 336 rkgEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALaeEYIKRLRI-KTPSP---EQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
191-395 |
1.12e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLL-SILG------GRVAGPGDvegcvsyndepyckslnrrigfvtqDDVLF 263
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLrAIAGlwpygsGRIARPAG-------------------------ARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 ----THL---TVKETLTYAALlrlPRTMTRQEKEErtidIIYELGLERCQDTM-IGGSFVRGVSGGERKRVCIGNEIIIN 335
Cdd:COG4178 431 lpqrPYLplgTLREALLYPAT---AEAFSDAELRE----ALEAVGLGHLAERLdEEADWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 336 PSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGkTVITTIHQPSSRLFHKfDKLILLGRGS 395
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAFHD-RVLELTGDGS 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
196-375 |
1.15e-14 |
|
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: 77.15 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 196 GISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDVEGCVSYNDE--------PYCKS-LNRRIGFVTQDDVLFTHL 266
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG-VLEPTSGEVNVRVGDEwvdmtkpgPDGRGrAKRYIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAALLRLPRTMTR------------QEKEERTIdiiyelgLERCQDTMiggsfvrgvSGGERKRVCIGNEIII 334
Cdd:TIGR03269 381 TVLDNLTEAIGLELPDELARmkavitlkmvgfDEEKAEEI-------LDKYPDEL---------SEGERHRVALAQVLIK 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQ-LLHDIAEDGKTVITTIH 375
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
175-375 |
1.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYkVAVKGTPREI--LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEG--CVSYNDEPYCK 247
Cdd:PRK13641 3 IKFENVDY-IYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpsSGTITIAGyhITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 248 SLNRRIGFVTQ--DDVLFTHlTVKETLTYAallrlPRTM--TRQEKEERTIDIIYELGLErcQDTMIGGSFvrGVSGGER 323
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFG-----PKNFgfSEDEAKEKALKWLKKVGLS--EDLISKSPF--ELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 324 KRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
192-404 |
1.73e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILG--------GRVAGPGDVEGCVSYNDEpyCKSLNRRIGFVTQDDVLF 263
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielypeARVSGEVYLDGQDIFKMD--VIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLtyAALLRLPRTM-TRQEKEERTIDIIYELGL-ERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:PRK14247 95 PNLSIFENV--ALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDgKTVITTIHQP--SSRLfhkFDKLILLGRGSLLYFGKASE 404
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPqqAARI---SDYVAFLYKGQIVEWGPTRE 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
192-370 |
2.46e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPGDVEGCVSYNDE-----PYCKSLNRRIGFVTQDDVLFTHL 266
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD---PRATSGRIVFDGKditdwQTAKIMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAALLrlprtMTRQEKEERtIDIIYELgLERCQDTMIGGSFVrgVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:PRK11614 96 TVEENLAMGGFF-----AERDQFQER-IKWVYEL-FPRLHERRIQRAGT--MSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180
....*....|....*....|....
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTV 370
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTI 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
189-376 |
3.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 189 TPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCKS----LNRRIGFVTQ--DDVL 262
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNG-ILKP--TSGSVLIRGEPITKEnireVRKFVGLVFQnpDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHlTVKETLTYAallrlPRTMTRQEK--EERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:PRK13652 92 FSP-TVEQDIAFG-----PINLGLDEEtvAHRVSSALHMLGLEELRDRV-----PHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQ 376
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
190-375 |
4.84e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.65 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYND------------EPYCKSLNR-RIGFV 256
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA-PD--AGEVHYRMrdgqlrdlyalsEAERRRLLRtEWGFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQD--DVLFTHLT----VKETLT------YAALlrlprtmtRQEKE---ERTidiiyELGLERCQDTmiggsfVRGVSGG 321
Cdd:PRK11701 95 HQHprDGLRMQVSaggnIGERLMavgarhYGDI--------RATAGdwlERV-----EIDAARIDDL------PTTFSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 322 ERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHD-IAEDGKTVITTIH 375
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTH 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
182-374 |
5.43e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 182 YKVAVKGTPRE--ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagPGDvEGCVSYNDE------PYCKSlnRRI 253
Cdd:COG1101 8 SKTFNPGTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSL--PPD-SGSILIDGKdvtklpEYKRA--KYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 254 GFVTQDDVLFT--HLTVKETLTYAAL----LRLPRTMTRQEKEE-----RTIDiiyeLGLERCQDTMIGGsfvrgVSGGE 322
Cdd:COG1101 83 GRVFQDPMMGTapSMTIEENLALAYRrgkrRGLRRGLTKKRRELfrellATLG----LGLENRLDTKVGL-----LSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 323 RKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKtvITTI 374
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN--LTTL 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
188-363 |
1.57e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKT-TLLSILGGRVAGP-----GDV--EG-CVSYNDEPYCKSL-NRRIGFVT 257
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypsGDIrfHGeSLLHASEQTLRGVrGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 258 QDD-VLFTHL-TVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIIIN 335
Cdd:PRK15134 99 QEPmVSLNPLhTLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRL--TDYPHQLSGGERQRVMIAMALLTR 174
|
170 180
....*....|....*....|....*...
gi 1002256437 336 PSLLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
183-349 |
1.59e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 183 KVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEpyckslnRRIGFVTQDdvl 262
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA---PDEGVIKRNGK-------LRIGYVPQK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 fTHLTVKETLTYAALLRLpRTMTRQEkeertiDIIyeLGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK09544 76 -LYLDTTLPLTVNRFLRL-RPGTKKE------DIL--PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
....*..
gi 1002256437 343 EPTSGLD 349
Cdd:PRK09544 146 EPTQGVD 152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
191-375 |
1.84e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILG---GRVAG---PGDV----EGCVSYNDepyCKSLNRRIGFVTQDD 260
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGyrySGDVllggRSIFNYRD---VLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFTHLTVKETLTYAALLRL-PRTMTRQEKEERtidiIYELGLERCQDTMIGGSFVRgVSGGERKRVCIGNEIIINPSLL 339
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKLvPRKEFRGVAQAR----LTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAeDGKTVITTIH 375
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTH 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
188-379 |
5.23e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVagpgDV-EGCVSYNDEPYCK----SLNRRIGFVTQDDVL 262
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF----DVsEGDIRFHDIPLTKlqldSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHltvketlTYAALLRLPRTMTRQEKEERTI-------DIiyeLGLERCQDTMIGGsfvRGV--SGGERKRVCIGNEII 333
Cdd:PRK10789 401 FSD-------TVANNIALGRPDATQQEIEHVArlasvhdDI---LRLPQGYDTEVGE---RGVmlSGGQKQRISIARALL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALriiQLLHDIAE--DGKTVITTIHQPSS 379
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEH---QILHNLRQwgEGRTVIISAHRLSA 512
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
204-413 |
5.24e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSILGGRVAGPGDVEGCVSYNDEPYC----KSLNR----RIGFVTQDDV--LFTHLTVKETLT 273
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILnlpeKELNKlraeQISMIFQDPMtsLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 yaALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:PRK09473 122 --EVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRM--KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 354 LRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGKASE-----AMPYfqSIG 413
Cdd:PRK09473 198 AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDvfyqpSHPY--SIG 260
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
204-375 |
6.21e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSIlggrVAGPGDVE------GCVSYNDEPYCKslnRRIGFVTQDDVLFTHLTVKETLTYAAL 277
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRM----IAGLEDITsgdlfiGEKRMNDVPPAE---RGVGMVFQSYALYPHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 LRLPRTMTRQEKEERTIDIIyELG--LERCQdtmiggsfvRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSttALR 355
Cdd:PRK11000 102 LAGAKKEEINQRVNQVAEVL-QLAhlLDRKP---------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA--ALR 169
|
170 180
....*....|....*....|....*
gi 1002256437 356 I-----IQLLHDiaEDGKTVITTIH 375
Cdd:PRK11000 170 VqmrieISRLHK--RLGRTMIYVTH 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
179-375 |
6.22e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 179 EVK-YKVAVKGTprEILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagPgdvegcvSYNdepyckslnrrigfVT 257
Cdd:CHL00131 9 EIKnLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH---P-------AYK--------------IL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 258 QDDVLFTHLTVKET----------------------LTYAALLRLPRTMTRQEKEERTIDII--YELGLERCQDTMIGGS 313
Cdd:CHL00131 63 EGDILFKGESILDLepeerahlgiflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLefLEIINEKLKLVGMDPS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 314 FV-----RGVSGGERKRvcigNEI----IINPSLLFLDEPTSGLDsTTALRII-QLLHDIAEDGKTVITTIH 375
Cdd:CHL00131 143 FLsrnvnEGFSGGEKKR----NEIlqmaLLDSELAILDETDSGLD-IDALKIIaEGINKLMTSENSIILITH 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
192-375 |
7.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVEGCVSYNDEPYCKSLNRRIGFVTQD--DVLFThLTV 268
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAallrlPRTM--TRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:PRK13647 98 WDDVAFG-----PVNMglDKDEVERRVEEALKAVRMWDFRDKP-----PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180
....*....|....*....|....*....
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
189-464 |
8.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 189 TPREI--LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGR-------------VAGP-GDVEGCVSYNDEPYCKS---L 249
Cdd:PRK13631 35 QENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiYIGDkKNNHELITNPYSKKIKNfkeL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 250 NRRIGFVTQ--DDVLFTHLTVKETLTYAALLRLPRtmtrQEKEERTIDIIYELGLercqdtmiGGSFVR----GVSGGER 323
Cdd:PRK13631 115 RRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKK----SEAKKLAKFYLNKMGL--------DDSYLErspfGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 324 KRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLfHKFDKLILLGRGSLLYFGKas 403
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKGKILKTGT-- 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 404 eamPYfqsigctpLIAMNPaEFLldlangNTTDVSVPSELDDKVHMENQNLQTNTKNDYKP 464
Cdd:PRK13631 260 ---PY--------EIFTDQ-HII------NSTSIQVPRVIQVINDLIKKDPKYKKLYQKQP 302
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
204-375 |
9.48e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSILGgRVAGPgdVEGCVSYNDEPY----CKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLR 279
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS-RLMTP--AHGHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDITVQELVARGRYPH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 280 LPR-TMTRQEKEERTIDIIYELGLercqdTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQ 358
Cdd:PRK10253 110 QPLfTRWRKEDEEAVTKAMQATGI-----THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170
....*....|....*...
gi 1002256437 359 LLHDI-AEDGKTVITTIH 375
Cdd:PRK10253 185 LLSELnREKGYTLAAVLH 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
188-426 |
1.05e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPreILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGcVSYNDEPYCKSLNRRIGFVTQD-DVLF 263
Cdd:PRK13644 14 GTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrpqKGKVLVSG-IDTGDFSKLQGIRKLVGIVFQNpETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAAL-LRLPRTMTRQekeeRTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK13644 91 VGRTVEEDLAFGPEnLCLPPIEIRK----RVDRALAEIGLEKYRHRS-----PKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYFGKASEAM--PYFQSIGCTPLIAM 420
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPSLI 239
|
....*.
gi 1002256437 421 NPAEFL 426
Cdd:PRK13644 240 ELAENL 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
191-404 |
1.45e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVA---GPGDVEGCVSYNDEPYCK----SLNRRIGFVTQDDVLF 263
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQidaiKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAallrlprTMTRQEKEERTIDIIYELGLERC------QDTMigGSFVRGVSGGERKRVCIGNEIIINPS 337
Cdd:PRK14246 103 PHLSIYDNIAYP-------LKSHGIKEKREIKKIVEECLRKVglwkevYDRL--NSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTiHQPsSRLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNP-QQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
175-404 |
1.51e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYKVAVKGTPReiLSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAGPGdvegcvsYNDEPY-C 246
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLDG-------HDLRDYtL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 247 KSLNRRIGFVTQDDVLFTHlTVKETLTYAAllrlPRTMTRQEKEE-----RTIDIIYEL--GLercqDTMIGGSFVRgVS 319
Cdd:PRK11176 413 ASLRNQVALVSQNVHLFND-TIANNIAYAR----TEQYSREQIEEaarmaYAMDFINKMdnGL----DTVIGENGVL-LS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 320 GGERKRVCIGNEIIINPSLLFLDEPTSGLDsTTALRIIQLLHDIAEDGKTVITTIHQPSSrlFHKFDKLILLGRGSLLYF 399
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALD-TESERAIQAALDELQKNRTSLVIAHRLST--IEKADEILVVEDGEIVER 559
|
....*
gi 1002256437 400 GKASE 404
Cdd:PRK11176 560 GTHAE 564
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
203-395 |
1.59e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.02 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRVagpgdvegcvsyndePYCKSlnrRIGFVTQDDVLFthLTVKetlTYaallrLPR 282
Cdd:cd03223 26 PGDRLLITGPSGTGKSSLFRALAGLW---------------PWGSG---RIGMPEGEDLLF--LPQR---PY-----LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 283 TMTRQEkeertidIIYELGLErcqdtmiggsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHd 362
Cdd:cd03223 78 GTLREQ-------LIYPWDDV--------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK- 135
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 363 iaEDGKTVITTIHQPSSRLFHKFdKLILLGRGS 395
Cdd:cd03223 136 --ELGITVISVGHRPSLWKFHDR-VLDLDGEGG 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
192-409 |
1.75e-12 |
|
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: 70.22 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDvEGCVSYN------------------------------ 241
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT-SGRIIYHvalcekcgyverpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 242 -------DEPYCKSLNRRIGFVTQ--------DDVLFTHLTVKETLTYAAllrlprtmtrQEKEERTIDIIYELGLERcQ 306
Cdd:TIGR03269 93 evdfwnlSDKLRRRIRKRIAIMLQrtfalygdDTVLDNVLEALEEIGYEG----------KEAVGRAVDLIEMVQLSH-R 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 307 DTMIGgsfvRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTAlriiQLLHD-----IAEDGKTVITTIHQPSSrL 381
Cdd:TIGR03269 162 ITHIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA----KLVHNaleeaVKASGISMVLTSHWPEV-I 232
|
250 260
....*....|....*....|....*...
gi 1002256437 382 FHKFDKLILLGRGSLLYFGKASEAMPYF 409
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
204-375 |
1.86e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEGCVSYNDEPYckslNRRIGFVTQDDVLFTHLTVKETLTYAALL-R 279
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGfeqPTAGQIMLDGVDLSHVPPY----QRPINMMFQSYALFPHMTVEQNIAFGLKQdK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 280 LPRTMTRQEKEERtidiiyeLGLERCQDtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQL 359
Cdd:PRK11607 121 LPKAEIASRVNEM-------LGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170
....*....|....*..
gi 1002256437 360 LHDIAED-GKTVITTIH 375
Cdd:PRK11607 192 VVDILERvGVTCVMVTH 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
187-459 |
2.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGD-------VEGcVSYNDEPYCkSLNRRIGFVTQD 259
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL-PDDnpnskitVDG-ITLTAKTVW-DIREKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 -DVLFTHLTVKETLTYAALlrlPRTMTRQEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSL 338
Cdd:PRK13640 93 pDNQFVGATVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYID-----SEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQPSSRlfHKFDKLILLGRGSLLYFGKASEAMP---YFQSIGC 414
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEIFSkveMLKEIGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002256437 415 -TPLIamnpAEFLLDLangNTTDVSVPSELDDKVHMENQNLQTNTK 459
Cdd:PRK13640 243 dIPFV----YKLKNKL---KEKGISVPQEINTEEKLVQYLCQLNSK 281
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
205-380 |
2.86e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 205 EVLALMGPSGSGKTTLLS--------ILGGRVagpgdvEGCVSYND-EPYCKSLN-----RRIGFVTQDDVLFTHlTVKE 270
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRcfnrlndlIPGFRV------EGKVTFHGkNLYAPDVDpvevrRRIGMVFQKPNPFPK-SIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TLTYAALLR---------LPRTMTRQEKEERTIDIIYELGLercqdtmiggsfvrGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:PRK14243 110 NIAYGARINgykgdmdelVERSLRQAALWDEVKDKLKQSGL--------------SLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTiH--QPSSR 380
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVT-HnmQQAAR 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
187-376 |
3.73e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.18 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLsilggR-VAG---PGdvEGCVSYNDEPYcKSLN--------RRIG 254
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI-----RcINLlerPT--SGSVLVDGVDL-TALSerelraarRKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 255 FVTQDDVLFTHLTVKETLTYAalLRLPRtMTRQEKEERTIDIIyEL-GLE-RcqdtmiGGSFVRGVSGGERKRVCIGNEI 332
Cdd:COG1135 86 MIFQHFNLLSSRTVAENVALP--LEIAG-VPKAEIRKRVAELL-ELvGLSdK------ADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002256437 333 IINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTV--ITtiHQ 376
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIvlIT--HE 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
191-375 |
4.85e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDVEGCVSYNDEPYCKS-----LNRRIGFVTQDDVLFTH 265
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAGKIWFSGHDITRLKNrevpfLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLTYAALLRLPRTMTRQEKEERTIDIIYELGLERcqdtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAK--------NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
194-371 |
6.71e-12 |
|
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: 63.99 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPyckslnrrigfvtqddVLFThltvketlt 273
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PD--SGEILVDGKE----------------VSFA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 yaallrlprtmTRQEKEERTIDIIYELglercqdtmiggsfvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:cd03216 68 -----------SPRDARRAGIAMVYQL------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170
....*....|....*...
gi 1002256437 354 LRIIQLLHDIAEDGKTVI 371
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVI 136
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
194-362 |
9.32e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.68 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTT-------LLSILGGRVagpgDVEGC-VSYNDEPYCKSLNRRIGFVTQD--DVLF 263
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTlgrlllrLEEPTSGEI----LFDGQdITGLSGRELRPLRRRMQMVFQDpyASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGLERcqdtmiggSFVR----GVSGGERKRVCIGNEIIINPSLL 339
Cdd:COG4608 110 PRMTVGDII--AEPLRIHGLASKAERRERVAELLELVGLRP--------EHADryphEFSGGQRQRIGIARALALNPKLI 179
|
170 180
....*....|....*....|....
gi 1002256437 340 FLDEPTSGLD-STTAlRIIQLLHD 362
Cdd:COG4608 180 VCDEPVSALDvSIQA-QVLNLLED 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
175-412 |
9.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYKVAvKGTP--REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGP------GDVEgCVSYNDEPYC 246
Cdd:PRK13643 2 IKFEKVNYTYQ-PNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtvGDIV-VSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 247 KSLNRRIGFVTQ--DDVLFTHLTVKETltyaALLRLPRTMTRQEKEERTIDIIYELGLERcqDTMIGGSFvrGVSGGERK 324
Cdd:PRK13643 80 KPVRKKVGVVFQfpESQLFEETVLKDV----AFGPQNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPF--ELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 325 RVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKfDKLILLGRGSLLYFGKASE 404
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYA-DYVYLLEKGHIISCGTPSD 230
|
....*...
gi 1002256437 405 AmpyFQSI 412
Cdd:PRK13643 231 V---FQEV 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
204-379 |
1.10e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSILGG--RVAgpgdvEGCVSYNDEPYCKSLNRR-IGFVTQDD-------VLFTHLTVKETLT 273
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGfvRLA-----SGKISILGQPTRQALQKNlVAYVPQSEevdwsfpVLVEDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 YAALLRLPRTMTRQekeertidiIYELGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTA 353
Cdd:PRK15056 108 HMGWLRRAKKRDRQ---------IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|....*.
gi 1002256437 354 LRIIQLLHDIAEDGKTVITTIHQPSS 379
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
191-363 |
1.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILG--GRVAGPGDVEGCVSY-NDEPYCKSLN-----RRIGFVTQDDVL 262
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVRVEGRVEFfNQNIYERRVNlnrlrRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FThLTVKETLTYAAllrlpRTMTRQEKEErtIDIIYELGLERCQ-----DTMIGGSFVRgVSGGERKRVCIGNEIIINPS 337
Cdd:PRK14258 100 FP-MSVYDNVAYGV-----KIVGWRPKLE--IDDIVESALKDADlwdeiKHKIHKSALD-LSGGQQQRLCIARALAVKPK 170
|
170 180
....*....|....*....|....*.
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSL 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
176-404 |
1.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.40 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 176 KFAEVKYKVAVKGTPreILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGcVSYNDEPYcKSLNRR 252
Cdd:PRK13632 9 KVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkpqSGEIKIDG-ITISKENL-KEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 253 IGFVTQD-DVLFTHLTVKETLTYAallrlprTMTRQEKEERTIDIIYELGlercQDTMIGGSFVR---GVSGGERKRVCI 328
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDIAFG-------LENKKVPPKKMKDIIDDLA----KKVGMEDYLDKepqNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 329 GNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDG-KTVITTIHQPSSRLfhKFDKLILLGRGSLLYFGKASE 404
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKE 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
204-350 |
1.75e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSIlggrVAG---PgdVEGCVSYNDEPYCKS--LNRRIGFVTQDDVLFTHLTVKETLTYA-AL 277
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRL----VAGlekP--TEGQIFIDGEDVTHRsiQQRDICMVFQSYALFPHMSLGENVGYGlKM 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 278 LRLPRTmtrqEKEERTIDIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDS 350
Cdd:PRK11432 106 LGVPKE----ERKQRVKEALELVDLAGFED-----RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
203-366 |
1.78e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTT----LLSILGGRvagpgdvEGCVSYNDE-----PYCK--SLNRRIGFVTQDDvlFTHLTVKET 271
Cdd:PRK10261 349 PGETLSLVGESGSGKSTtgraLLRLVESQ-------GGEIIFNGQridtlSPGKlqALRRDIQFIFQDP--YASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 272 LTYAAL--LRLPRTMTRQEKEERTIDIIYELGLERCQDTMIGGSFvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:PRK10261 420 VGDSIMepLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170
....*....|....*..
gi 1002256437 350 STTALRIIQLLHDIAED 366
Cdd:PRK10261 496 VSIRGQIINLLLDLQRD 512
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
192-348 |
2.88e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEPYCK---SLNRRIG--FVTQDDVLFTHL 266
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARltpAKAHQLGiyLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLtyaaLLRLPRtmtRQEKEERTIDIIYELGLERCQDTMIGGSFVrgvsgGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:PRK15439 102 SVKENI----LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTA 169
|
..
gi 1002256437 347 GL 348
Cdd:PRK15439 170 SL 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
187-404 |
3.24e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTP--REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGCVSYNDEPYCKSLNRRIGFVTQ--D 259
Cdd:PRK13637 14 EGTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkptSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHlTVKETLTYAallrlPRTM--TRQEKEERTIDIIYELGLERcqDTMIGGS-FvrGVSGGERKRVCIGNEIIINP 336
Cdd:PRK13637 94 YQLFEE-TIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGLDY--EDYKDKSpF--ELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 337 SLLFLDEPTSGLDSTT---ALRIIQLLHDiaEDGKTVITTIHqpSSRLFHKF-DKLILLGRGSLLYFGKASE 404
Cdd:PRK13637 164 KILILDEPTAGLDPKGrdeILNKIKELHK--EYNMTIILVSH--SMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
194-371 |
4.27e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgDvEGCVSYNDEPYC-----KSLNRRIGFVTQDDVLFTHLTV 268
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-P-D-SGEILIDGKPVRirsprDAIALGIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLPRTMTRQEKEERTIDIIYELGLE-----RcqdtmiggsfVRGVSGGERKRVcignEII----INPSLL 339
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpdaK----------VEDLSVGEQQRV----EILkalyRGARIL 163
|
170 180 190
....*....|....*....|....*....|..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
146-375 |
5.20e-11 |
|
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: 66.58 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 146 PFSDDDNTMDIEagtpRKKLMTEPTLPIYLKFAEVKyKVaVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILG 225
Cdd:TIGR01257 1913 PIFDEDDDVAEE----RQRIISGGNKTDILRLNELT-KV-YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT 1986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 226 GRVA---GPGDVEGCVSYNDepyCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRlprTMTRQEKEERTIDIIYELGL 302
Cdd:TIGR01257 1987 GDTTvtsGDATVAGKSILTN---ISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR---GVPAEEIEKVANWSIQSLGL 2060
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 303 ERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:TIGR01257 2061 SLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
194-375 |
5.93e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGdvEGCVSYNDEPY-----CKSLNRRIGFVTQDDVLFTHLTV 268
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQ-PD--AGSILIDGQEMrfastTAALAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTyaaLLRLPRTM---TRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:PRK11288 97 AENLY---LGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTP-----LKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
162-397 |
9.16e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.15 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 162 RKKLMTEPTLPIY-LKFAEVKYKVavkGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSY 240
Cdd:TIGR01193 460 NKKKRTELNNLNGdIVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG-FFQAR--SGEILL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 241 NDEPYCK----SLNRRIGFVTQDDVLFTHlTVKETLTYAAllrlpRTMTRQEKEERTIDI------IYELGLERCQDTMI 310
Cdd:TIGR01193 534 NGFSLKDidrhTLRQFINYLPQEPYIFSG-SILENLLLGA-----KENVSQDEIWAACEIaeikddIENMPLGYQTELSE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 311 GGSfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdgKTVITTIHQPSsrLFHKFDKLIL 390
Cdd:TIGR01193 608 EGS---SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIV 680
|
....*..
gi 1002256437 391 LGRGSLL 397
Cdd:TIGR01193 681 LDHGKII 687
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
187-404 |
1.02e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.11 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGCVSynDEPYCKSLNRRIGFVTQD-DVL 262
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlpeAGTITVGGMVL--SEETVWDVRRQVGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAallrLP-RTMTRQEKEERTIDIIYELGLErcqdtmiggSFVR----GVSGGERKRVCIGNEIIINPS 337
Cdd:PRK13635 94 FVGATVQDDVAFG----LEnIGVPREEMVERVDQALRQVGME---------DFLNrephRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 338 LLFLDEPTSGLD---STTALRIIQLLHDiaEDGKTVITTIHQPSSRLfhKFDKLILLGRGSLLYFGKASE 404
Cdd:PRK13635 161 IIILDEATSMLDprgRREVLETVRQLKE--QKGITVLSITHDLDEAA--QADRVIVMNKGEILEEGTPEE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
191-375 |
1.38e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagpgDVEgcvsYNDEPYcKSLNRRIGFVTQDDVLFTHLTVKE 270
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKD----FNGEAR-PQPGIKVGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TL------TYAALLRL--------------PRTMTRQEKEERTIDII----YELGLE------RCQDtmiGGSFVRGVSG 320
Cdd:TIGR03719 88 NVeegvaeIKDALDRFneisakyaepdadfDKLAAEQAELQEIIDAAdawdLDSQLEiamdalRCPP---WDADVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAedgKTVITTIH 375
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTH 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
187-412 |
1.38e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTPREILSGISGSAAPGEVLALMGPSGSGKT-TLLSILGgRVAGPGDVEG-CVSYN--DEPYCKSLNRR------IGFV 256
Cdd:PRK11022 16 ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMG-LIDYPGRVMAeKLEFNgqDLQRISEKERRnlvgaeVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQDDVlfTHLTVKETLTYAAL--LRLPRTMTRQEKEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIII 334
Cdd:PRK11022 95 FQDPM--TSLNPCYTVGFQIMeaIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGKASEAM-----PYF 409
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFraprhPYT 250
|
...
gi 1002256437 410 QSI 412
Cdd:PRK11022 251 QAL 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
194-366 |
1.39e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTL--------------LSILGGRVAGPgdvegcvsynDEPYCKSLNRRIGFVTQD 259
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlltmietptggeLYYQGQDLLKA----------DPEAQKLLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DvlFTHL----TVKETLtyAALLRLPRTMTRQEKEERTIDIIYELGL--ERCQ--DTMIggsfvrgvSGGERKRVCIGNE 331
Cdd:PRK11308 101 P--YGSLnprkKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLrpEHYDryPHMF--------SGGQRQRIAIARA 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 332 IIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED 366
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
191-363 |
1.40e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.48 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPGDVEGCVSYNDEPyckSLNR--------RIGFVTQDDVL 262
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIA-PDHGEILFDGENIP---AMSRsrlytvrkRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAalLR----LPRTMTRQekeerTIDIIYE-LGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPS 337
Cdd:PRK11831 96 FTDMNVFDNVAYP--LRehtqLPAPLLHS-----TVMMKLEaVGLRGAAKLMPS-----ELSGGMARRAALARAIALEPD 163
|
170 180
....*....|....*....|....*.
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISEL 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
197-396 |
1.70e-10 |
|
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: 64.08 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 197 ISGSAAPGEVLALMGPSGSGKTTLLSILGGrvAGPGDVEGCVSYNDEPY-----CKSLNRRIGFVTQD---DVLFTHLTV 268
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPVdirnpAQAIRAGIAMVPEDrkrHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLP-RTMTRQEKEERTIDI-IYELGLERCQ-DTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:TIGR02633 357 GKNITLSVLKSFCfKMRIDAAAELQIIGSaIQRLKVKTASpFLPIGR-----LSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVITTihqpSSRLFHKF---DKLILLGRGSL 396
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEVLglsDRVLVIGEGKL 481
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
192-404 |
1.81e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPgdvEGCVSYNDEP--YCK----SLNRRIGFVTQD---DVL 262
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQGKPldYSKrgllALRQQVATVFQDpeqQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAALLRLPRTMTRQEKEERTIdiiyeLGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTL-----VDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpSSRLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
191-354 |
2.06e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgP--GDVEgcvsyndepycKSLNRRIGFVTQD-DVLFTHLT 267
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-PdsGTVK-----------LGETVKIGYFDQHqEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLTYAAllrlprtmtRQEKEERTIDIiyelgLER------CQDTmiggsFVRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:COG0488 396 VLDELRDGA---------PGGTEQEVRGY-----LGRflfsgdDAFK-----PVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170
....*....|....*
gi 1002256437 342 DEPTSGLD--STTAL 354
Cdd:COG0488 457 DEPTNHLDieTLEAL 471
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
194-375 |
2.33e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgDVEGCVSYNDEPYCK----SLNRRIGFVTQD-DVLFTHLTV 268
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGELLTAenvwNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAAllrLPRTMTRQEKEERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTSGL 348
Cdd:PRK13642 100 EDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKTREPA-----RLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180
....*....|....*....|....*...
gi 1002256437 349 DSTTALRIIQLLHDIAEDGK-TVITTIH 375
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQlTVLSITH 199
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
193-396 |
2.53e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.71 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSG-ISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgdVEGCVSYNDEPYcKSLN-----RRIGFVTQDDVLFtHL 266
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKINGIEL-RELDpeswrKHLSWVGQNPQLP-HG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAallrlprtmtrqeKEERTIDIIYELgLERCQ------------DTMIG-GSfvRGVSGGERKRVCIGNEII 333
Cdd:PRK11174 438 TLRDNVLLG-------------NPDASDEQLQQA-LENAWvseflpllpqglDTPIGdQA--AGLSVGQAQRLALARALL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIHQPSSrlFHKFDKLILLGRGSL 396
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLED--LAQWDQIWVMQDGQI 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
190-400 |
2.85e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.01 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLLSILG-------GRVAGPGDVEGCVSYNdepyckslnrrIGFvtQDDvl 262
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAgiyppdsGTVTVRGRVSSLLGLG-----------GGF--NPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 fthLTVKETLTYAALLrlpRTMTRQEKEERtIDIIYEL-GLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:cd03220 99 ---LTGRENIYLNGRL---LGLSRKEIDEK-IDEIIEFsELGDFIDLP-----VKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 342 DEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSrlFHKF-DKLILLGRGSLLYFG 400
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS--IKRLcDRALVLEKGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
205-376 |
3.24e-10 |
|
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: 63.88 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 205 EVLALMGPSGSGKTTLLSILGGRVAgPGDVEGCVSYND-EPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAALLRlprT 283
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLP-PTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK---G 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 284 MTRQEKEERTIDIIYELGLERCQDTMiggsfVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI 363
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDTGLHHKRNEE-----AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170
....*....|...
gi 1002256437 364 aEDGKTVITTIHQ 376
Cdd:TIGR01257 1108 -RSGRTIIMSTHH 1119
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
204-406 |
3.97e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.36 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLLSILGgRVAGPG------DVEGCVSYNDEPYCKSLNRRIGFVTQDDVLFTHLTVKETLTYAAL 277
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLN-RLIEPTrgqvliDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 LRlprTMTRQEKEERTIDIIYELGLERcqdtmIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRII 357
Cdd:PRK10070 133 LA---GINAEERREKALDALRQVGLEN-----YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002256437 358 QLLHDIAEDGKTVITTIHQPSSRLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
191-362 |
5.45e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 58.23 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGR-VAGPGDVEgcvsyndepycKSLNRRIGFVTQddvlfthltvk 269
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElEPDEGIVT-----------WGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 etltyaallrlprtmtrqekeertidiiyelglercqdtmiggsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170
....*....|...
gi 1002256437 350 STTALRIIQLLHD 362
Cdd:cd03221 103 LESIEALEEALKE 115
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
191-397 |
5.71e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGR-----VAGPGDVEGCVSYNDEPYCKSLNRRigfvtqDDVlfth 265
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkgtpVAGCVDVPDNQFGREASLIDAIGRK------GDF---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 266 LTVKETLTYAAL------LRLPRTMtrqekeertidiiyelglercqdtmiggsfvrgvSGGERKRVCIGNEIIINPSLL 339
Cdd:COG2401 113 KDAVELLNAVGLsdavlwLRRFKEL----------------------------------STGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIA-EDGKTVITTIHQPSSRLFHKFDKLILLGRGSLL 397
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVP 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
192-379 |
1.12e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGgRVAGPgdVEGCVSYNDEPYCKSLN-----RRIGFVTQDDVLFTHl 266
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIE-RLYDP--TEGDIIINDSHNLKDINlkwwrSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYA-------------------------------------ALLRLPRTMTRQE-----KEERTID--------- 295
Cdd:PTZ00265 475 SIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMSNTTDSNEliemrKNYQTIKdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 296 --IIYEL--GLERCQDTMIGgSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTV 370
Cdd:PTZ00265 555 kvLIHDFvsALPDKYETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT 633
|
....*....
gi 1002256437 371 ITTIHQPSS 379
Cdd:PTZ00265 634 IIIAHRLST 642
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
191-391 |
1.22e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILG-------GRVAGPGdvEGCVSYNDEPYckslNRRIGFVTQDDVLF 263
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAslisptsGTLLFEG--EDISTLKPEIY----RQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THlTVKETLTYAALLRlprtmTRQEKEERTIDIIYELGLErcqDTMIGGSfVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:PRK10247 94 GD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALP---DTILTKN-IAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKfDKLILL 391
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHA-DKVITL 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
202-375 |
2.38e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 202 APGEVLALMGPSGSGKTTLLSILGGRVagpgdVEGCVSYNDEP-YCKSLNRRIGFVTQDdvLFTHL---TVKETLTYAAL 277
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKL-----KPNLGKFDDPPdWDEILDEFRGSELQN--YFTKLlegDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 278 LRLPRT--------MTRQEKEERTIDIIYELGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:cd03236 97 DLIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*.
gi 1002256437 350 STTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
194-376 |
2.72e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.73 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLL-SILGGRVAGPGDVEGCVSYNDEPYCKSLNRR----IGFVTQDDVLFtHLTV 268
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLPR--TMTRQEKEERTIDIiyelgLERCQDTMIGGsfvRGV--SGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:cd03290 96 EENITFGSPFNKQRykAVTDACSLQPDIDL-----LPFGDQTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 345 TSGLDSTTALRIIQ--LLHDIAEDGKTVITTIHQ 376
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
173-375 |
2.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.59 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 173 IYLKFAEVKYKvavKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGD--VEGCVSYNDEPYckSL 249
Cdd:PRK13650 5 IEVKNLTFKYK---EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGlLEAESGQiiIDGDLLTEENVW--DI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 250 NRRIGFVTQD-DVLFTHLTVKETLTYAAllrLPRTMTRQEKEERTIDIIYELGLERCQDTmiggSFVRgVSGGERKRVCI 328
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKER----EPAR-LSGGQKQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002256437 329 GNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVITTIH 375
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
194-371 |
3.12e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSG-----ISGSAAPGEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEGCVSYNDEPYcKSLNRRIGFVTQD---DVL 262
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGalpRTSGYVTLDGHEVVTRSPQ-DGLANGIVYISEDrkrDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAALLRLPRTMTR-QEKEERTI--DIIYELGLER-CQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSL 338
Cdd:PRK10762 342 VLGMSVKENMSLTALRYFSRAGGSlKHADEQQAvsDFIRLFNIKTpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
197-371 |
3.89e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 197 ISGSAAPGEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEGCVSYNDEPYcKSLNRRIGFVTQ---DDVLFTHLTVKE 270
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkRAGGEIRLNGKDISPRSPL-DAVKKGMAYITEsrrDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TLTYAALLRLPR-----TMTRQEKEERTIDIIYELGLERCQDTmigGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:PRK09700 361 NMAISRSLKDGGykgamGLFHEVDEQRTAENQRELLALKCHSV---NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180
....*....|....*....|....*.
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
189-366 |
4.07e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 189 TPREILSGISGSAAPGEVLALMGPSGSGKT-TLLSILGGRVAGPGDVEGCVSYNDEPY--CKSLNRRIGFVTQ------D 259
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRQTAGRVLLDGKPVapCALRGRKIATIMQnprsafN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 260 DVLFTHLTVKETLtyaallrlpRTMTRQEKEERTIDIIYELGLErcQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLL 339
Cdd:PRK10418 94 PLHTMHTHARETC---------LALGKPADDATLTAALEAVGLE--NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180
....*....|....*....|....*..
gi 1002256437 340 FLDEPTSGLDSTTALRIIQLLHDIAED 366
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQK 189
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
183-376 |
4.21e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 183 KVAVKGTprEILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGR-----VAGPGDVEGCVSYNDEPYCKSlNRRIGFVT 257
Cdd:PRK09580 8 HVSVEDK--AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevTGGTVEFKGKDLLELSPEDRA-GEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 258 QDDVLFTHLTVKETLTYAalLRLPRTMTRQEKEER--TIDIIYE-LGLERCQDTMIGGSFVRGVSGGERKRVCIGNEIII 334
Cdd:PRK09580 85 QYPVEIPGVSNQFFLQTA--LNAVRSYRGQEPLDRfdFQDLMEEkIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002256437 335 NPSLLFLDEPTSGLDsTTALRIIQLLHDIAEDGKT--VITTIHQ 376
Cdd:PRK09580 163 EPELCILDESDSGLD-IDALKIVADGVNSLRDGKRsfIIVTHYQ 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
175-376 |
4.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 175 LKFAEVKYkVAVKGTP--REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgPgdVEGCVSYND--------EP 244
Cdd:PRK13634 3 ITFQKVEH-RYQYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ-P--TSGTVTIGErvitagkkNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 245 YCKSLNRRIGFVTQ--DDVLFTHlTVKETLTYAallrlPRT--MTRQEKEERTIDIIYELGLErcQDTMIGGSFvrGVSG 320
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFG-----PMNfgVSEEDAKQKAREMIELVGLP--EELLARSPF--ELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQL---LHDiaEDGKTVITTIHQ 376
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMfykLHK--EKGLTTVLVTHS 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
194-364 |
1.51e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDVEGCVSYNDEPYcKSLNRR------IGFVTQDDVLFTHLT 267
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGTYEGEIIFEGEEL-QASNIRdteragIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKET------LTYAALLRLPRTMTRQEK--EERTIDI-----IYELGlercqdtmiggsfvrgvsGGERKRVCIGNEIII 334
Cdd:PRK13549 99 VLENiflgneITPGGIMDYDAMYLRAQKllAQLKLDInpatpVGNLG------------------LGQQQLVEIAKALNK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 335 NPSLLFLDEPTSGL-DSTTA--LRIIQLL--HDIA 364
Cdd:PRK13549 161 QARLLILDEPTASLtESETAvlLDIIRDLkaHGIA 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
194-404 |
1.55e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTllSILGGRVAGPGdvEGCVSYNDEPYC---KSLNRRIGFvtqddvlftHLTVK- 269
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPD--AGRRPWRF*TWCanrRALRRTIG*---------HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ---ETLTYAALLRL---PRTMTRQEKEERTIDIiyelgLERCQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:NF000106 96 grrESFSGRENLYMigr*LDLSRKDARARADEL-----LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIH--QPSSRLFHkfdKLILLGRGSLLYFGKASE 404
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQymEEAEQLAH---ELTVIDRGRVIADGKVDE 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
203-375 |
1.75e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRVAgP--GDvegcvsYNDEPyckslnrrigfvTQDDV--------LFTHL------ 266
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELK-PnlGD------YDEEP------------SWDEVlkrfrgteLQDYFkklang 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 --------------------TVKETLTYAallrlprtmtrqekEERTI--DIIYELGLERCQDTMIggsfvRGVSGGERK 324
Cdd:COG1245 159 eikvahkpqyvdlipkvfkgTVRELLEKV--------------DERGKldELAEKLGLENILDRDI-----SELSGGELQ 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 325 RVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
191-371 |
1.77e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrvAGPGDVEGCVSYNDEPY----C-KSLNRRIGFVTQD---DVL 262
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWEGEIFIDGKPVkirnPqQAIAQGIAMVPEDrkrDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLTVKETLTYAALLRLP-RTMTRQEKEERTID-IIYELGLeRCQDTMIGgsfVRGVSGGERKRVCIGNEIIINPSLLF 340
Cdd:PRK13549 353 VPVMGVGKNITLAALDRFTgGSRIDDAAELKTILeSIQRLKV-KTASPELA---IARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190
....*....|....*....|....*....|.
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAII 459
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
193-411 |
1.77e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGP--GDVEgcvsyndepycksLNRRI--------GFVTQddvl 262
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-ILEPtsGRVE-------------VNGRVsallelgaGFHPE---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 fthLTVKE-TLTYAALLRlprtMTRQEKEERTIDIIY--ELglercqdtmigGSF----VRGVSGGERKRVCIGNEIIIN 335
Cdd:COG1134 103 ---LTGREnIYLNGRLLG----LSRKEIDEKFDEIVEfaEL-----------GDFidqpVKTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256437 336 PSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPSS--RLfhkFDKLILLGRGSLLYFGKASEAMPYFQS 411
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAvrRL---CDRAIWLEKGRLVMDGDPEEVIAAYEA 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
188-375 |
1.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPRE--ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDVE------GCVSYNDEpyCKSLNRRIGFVTQ 258
Cdd:PRK13649 15 GTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlHVPTQGSVRvddtliTSTSKNKD--IKQIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 259 --DDVLFTHlTVKETLTYAallrlPRTM-TRQEKEERtidiiyelgLERCQDTMIGGS---FVRG---VSGGERKRVCIG 329
Cdd:PRK13649 93 fpESQLFEE-TVLKDVAFG-----PQNFgVSQEEAEA---------LAREKLALVGISeslFEKNpfeLSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002256437 330 NEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
190-376 |
2.55e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPgdVEGCVSYNDEPYCK-----SLNRRIGFVTQDDVLFT 264
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG-IHEP--TKGTITINNINYNKldhklAAQLGIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 HLTVKETLTYAallRLPrtmTRQ----------EKEERTIDIIYELGLERCQDTmiggsFVRGVSGGERKRVCIGNEIII 334
Cdd:PRK09700 94 ELTVLENLYIG---RHL---TKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDE-----KVANLSISHKQMLEIAKTLML 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002256437 335 NPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
191-375 |
3.10e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRvagpgDVEgcvsYNDEPYcKSLNRRIGFVTQDDVLFTHLTVKE 270
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKE----FEGEAR-PAPGIKVGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TL------TYAALLRL---------P-----RTMTRQEKEERTIDII--YELG--LE------RCQDtmiGGSFVRGVSG 320
Cdd:PRK11819 90 NVeegvaeVKAALDRFneiyaayaePdadfdALAAEQGELQEIIDAAdaWDLDsqLEiamdalRCPP---WDAKVTKLSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002256437 321 GERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAedGkTVITTIH 375
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP--G-TVVAVTH 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
193-376 |
5.31e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 193 ILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVE-GCVSYNDEPYCKsLNRRIGFVTQDDVLFTHLTVKET 271
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQiDGVSWNSVPLQK-WRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 272 LTYAallrlprtmtrQEKEERTIDIIYELGLERCQD--------TMIGGSFVrgVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:cd03289 98 DPYG-----------KWSDEEIWKVAEEVGLKSVIEqfpgqldfVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1002256437 344 PTSGLDSTTaLRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:cd03289 165 PSAHLDPIT-YQVIRKTLKQAFADCTVILSEHR 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
194-404 |
5.62e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGdvEGCVSYNDEPYC----KSLNRRIGFVTQD-DVLFTHLTV 268
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVK--SGEIFYNNQAITddnfEKLRKHIGIVFQNpDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KetltYAALLRLPRTMTRQEKEERTI-DIIYELGLERCQDtmiggSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:PRK13648 102 K----YDVAFGLENHAVPYDEMHRRVsEALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 348 LDSTTALRIIQLLHDIAEDGKTVITTIHQPSSRLFHKfDKLILLGRGSLLYFGKASE 404
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTE 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
194-368 |
6.23e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGrVAGPGDVEGCVSYNDEPYCKSLNRR-----IGFVTQDDVLFTHLTV 268
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGTWDGEIYWSGSPLKASNIRDteragIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRLP-RTMTRQEKEERTIDIIYELGLERCQDTMIGGSFvrgvSGGERKRVCIGNEIIINPSLLFLDEPTSG 347
Cdd:TIGR02633 96 AENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180
....*....|....*....|.
gi 1002256437 348 LDSTTalriIQLLHDIAEDGK 368
Cdd:TIGR02633 172 LTEKE----TEILLDIIRDLK 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
192-400 |
6.31e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.57 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTL-LSILggRVAGPgdVEGCVSYNDEPYCK----SLNRRIGFVTQDDVLFTHl 266
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALF--RFLEA--EEGKIEIDGIDISTipleDLRSSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLtyaallrlprtmtrQEKEERTIDIIYElGLERCQdtmiGGSfvrGVSGGERKRVCIGNEIIINPSLLFLDEPTS 346
Cdd:cd03369 97 TIRSNL--------------DPFDEYSDEEIYG-ALRVSE----GGL---NLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 347 GLDSTTALRIIQLLHDIAEDGkTVITTIHQPSSRLfhKFDKLILLGRGSLLYFG 400
Cdd:cd03369 155 SIDYATDALIQKTIREEFTNS-TILTIAHRLRTII--DYDKILVMDAGEVKEYD 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
141-371 |
2.27e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 141 SAELHPFSDDDNtmdIEAGTPRKK---LMTEPTLPIYLKFAEvkyKVAVKGTPR---EILSG-----ISGSAAPGEVLAL 209
Cdd:PRK15439 221 SGKTADLSTDDI---IQAITPAAReksLSASQKLWLELPGNR---RQQAAGAPVltvEDLTGegfrnISLEVRAGEILGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 210 MGPSGSGKTTLLSILGG-RVAGPGDV--EGCvsynDEPYCKSLNR-RIGFV-----TQDDVLFthLTVKETLTYAALLRL 280
Cdd:PRK15439 295 AGVVGAGRTELAETLYGlRPARGGRImlNGK----EINALSTAQRlARGLVylpedRQSSGLY--LDAPLAWNVCALTHN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 281 PRTMTRQEKEERTIdiiyelgLERCQDTMiGGSF------VRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTAL 354
Cdd:PRK15439 369 RRGFWIKPARENAV-------LERYRRAL-NIKFnhaeqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
250
....*....|....*..
gi 1002256437 355 RIIQLLHDIAEDGKTVI 371
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVL 457
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
247-391 |
3.91e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 247 KSLNRRIGFVTQDDVLFtHLTVKETLTYAAllrlpRTMTRQEKEE----RTIDIIYElGLERCQDTMIGgSFVRGVSGGE 322
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLF-NMSIYENIKFGK-----EDATREDVKRackfAAIDEFIE-SLPNKYDTNVG-PYGKSLSGGQ 1363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 323 RKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDG-KTVITTIHQPSSrlFHKFDKLILL 391
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS--IKRSDKIVVF 1431
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
192-406 |
5.33e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 192 EILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGdveGCVSYNDEPYC----KSLNRRIGFVTQDDVlfTHLT 267
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS---GELLIDDHPLHfgdySYRSQRIRMIFQDPS--TSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETL--TYAALLRLPRTMTRQEKEERTIDIIYELGLERCQdtmiGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPT 345
Cdd:PRK15112 102 PRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 346 SGLDSTTALRIIQLLHDIAEdgKTVITTIH--QPSSRLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQE--KQGISYIYvtQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
203-349 |
1.12e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGG--RVAGpgdveGCVSYNDEP---YCKSLNRRIGFVT--QDDVLFTHLTVKETL--- 272
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGfyKPTG-----GTILLRGQHiegLPGHQIARMGVVRtfQHVRLFREMTVIENLlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 273 --------TYAALLRLPRtMTRQEKE--ERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK11300 105 qhqqlktgLFSGLLKTPA-FRRAESEalDRAATWLERVGLLEHANRQAG-----NLAYGQQRRLEIARCMVTQPEILMLD 178
|
....*..
gi 1002256437 343 EPTSGLD 349
Cdd:PRK11300 179 EPAAGLN 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
188-414 |
1.24e-06 |
|
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: 52.22 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 188 GTPreILSGISGSAAPGEVLALMGPSGSGKTTLLS-ILGGRVAGPGDVE--GCVSYndepyCKSLNRRIGFVTQDDVLFT 264
Cdd:TIGR01271 438 VTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKhsGRISF-----SPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 265 hltvketLTYAALLRlpRTMTRQEKEERTIDIIYElglercQDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEP 344
Cdd:TIGR01271 511 -------LSYDEYRY--TSVIKACQLEEDIALFPE------KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 345 TSGLDSTTALRIIQ--LLHDIAEDGKTVITtihqpsSRLFH--KFDKLILLGRGSLLYFGKASEAM---PYFQS--IGC 414
Cdd:TIGR01271 576 FTHLDVVTEKEIFEscLCKLMSNKTRILVT------SKLEHlkKADKILLLHEGVCYFYGTFSELQakrPDFSSllLGL 648
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
194-458 |
2.01e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEGCVSY--------NDepyckSLnrrigfvtQDDVL 262
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdKVEGHVHMKGSVAYvpqqawiqND-----SL--------RENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 263 FTHLT----VKETLTYAALLRLPRTMTRQEKEErtidiIYELGLErcqdtmiggsfvrgVSGGERKRVCIGNEIIINPSL 338
Cdd:TIGR00957 721 FGKALnekyYQQVLEACALLPDLEILPSGDRTE-----IGEKGVN--------------LSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 339 LFLDEPTSGLDSTTALRIIQllHDIAEDG----KTVITTIHQPSsrLFHKFDKLILLGRgsllyfGKASEAMPY------ 408
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFE--HVIGPEGvlknKTRILVTHGIS--YLPQVDVIIVMSG------GKISEMGSYqellqr 851
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 409 ---FQSIGCTpliaMNPAEFLLDLANGNTTDVSVPSEldDKVHMENQNLQTNT 458
Cdd:TIGR00957 852 dgaFAEFLRT----YAPDEQQGHLEDSWTALVSGEGK--EAKLIENGMLVTDV 898
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
203-375 |
2.06e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRVAgP--GDvegcvsYNDEPyckslnrrigfvTQDDVLfTHLTVKETLTYAALLR- 279
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELI-PnlGD------YEEEP------------SWDEVL-KRFRGTELQNYFKKLYn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 280 --------------LPRTM---TRQ--EK-EERTI--DIIYELGLERCQDTMIggsfvRGVSGGERKRVCIGNEIIINPS 337
Cdd:PRK13409 158 geikvvhkpqyvdlIPKVFkgkVREllKKvDERGKldEVVERLGLENILDRDI-----SELSGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002256437 338 LLFLDEPTSGLDSTTALRIIQLLHDIAEdGKTVITTIH 375
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
189-394 |
2.27e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 189 TPREILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAgpgdvegcvsyNDEPYCKSLNRRIGFVTQDDVLFtHLTV 268
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSSVVIRGSVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 269 KETLTYAALLRlprtmtrQEKEERTIDII---YELGLERCQD-TMIGGsfvRGV--SGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PLN03232 696 RENILFGSDFE-------SERYWRAIDVTalqHDLDLLPGRDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 343 EPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpsSRLFHKFDKLILLGRG 394
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
180-404 |
2.61e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 180 VKYKVAvKGTPREI--LSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGP------GDVEGCVSYNDEPYCKSLNR 251
Cdd:PRK13645 12 VSYTYA-KKTPFEFkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 252 RIGFVTQ--DDVLFTHlTVKETLTYAALlrlPRTMTRQEKEERTIDIIYELGLERcqDTMIGGSFvrGVSGGERKRVCIG 329
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPE--DYVKRSPF--ELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 330 NEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQpSSRLFHKFDKLILLGRGSLLYFGKASE 404
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
204-349 |
2.82e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTT-------LLSI------LGGRVAGPGDVEgcvsyndepycksLNRRIGFVTQDDVLFTHLTVKE 270
Cdd:NF033858 292 GEIFGFLGSNGCGKSTtmkmltgLLPAsegeawLFGQPVDAGDIA-------------TRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 271 TLT-YAALLRLPRTmtrqEKEERTIDIIYELGLERCQDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:NF033858 359 NLElHARLFHLPAA----EIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
191-376 |
4.38e-06 |
|
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: 50.29 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDVE-GCVSYNDEPYcKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQiDGVSWNSVTL-QTWRKAFGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTYAallrlprtmtrQEKEERTIDIIYELGL----ERCQD----TMIGGSFVrgVSGGERKRVCIGNEIIINPSLLFL 341
Cdd:TIGR01271 1311 NLDPYE-----------QWSDEEIWKVAEEVGLksviEQFPDkldfVLVDGGYV--LSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....*
gi 1002256437 342 DEPTSGLDSTTaLRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:TIGR01271 1378 DEPSAHLDPVT-LQIIRKTLKQSFSNCTVILSEHR 1411
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
306-371 |
4.90e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 4.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256437 306 QDTMIGGsfvrgVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:PRK10982 385 HRTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
203-373 |
5.12e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRV---AGPGDVEGCVSYNDEPyckslNRRIGFVTQDDVLFTHLTVKETLTYAALL- 278
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLhveSGQIQIDGKTATRGDR-----SRFMAYLGHLPGLKADLSTLENLHFLCGLh 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 279 -RLPRTMTRQekeerTIDIIyelGLERCQDTMiggsfVRGVSGGERKRVCIGnEIIINPS-LLFLDEPTSGLD--STTAL 354
Cdd:PRK13543 111 gRRAKQMPGS-----ALAIV---GLAGYEDTL-----VRQLSAGQKKRLALA-RLWLSPApLWLLDEPYANLDleGITLV 176
|
170
....*....|....*....
gi 1002256437 355 RIIQLLHdIAEDGKTVITT 373
Cdd:PRK13543 177 NRMISAH-LRGGGAALVTT 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
185-376 |
5.66e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 185 AVKGTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSIL-------GGRVAgpgdVEGC-VSYNDEPYCKSLNRRIGFV 256
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVL----VDGQdLTALSEKELRKARRQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 257 TQDDVLFTHLTVKETltyAAL-LRLPRTmTRQEKEERTIDIIYELGLERCQDTmiggsFVRGVSGGERKRVCIGNEIIIN 335
Cdd:PRK11153 88 FQHFNLLSSRTVFDN---VALpLELAGT-PKAEIKARVTELLELVGLSDKADR-----YPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002256437 336 PSLLFLDEPTSGLDSTTALRIIQLLHDIAED-GKTVITTIHQ 376
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
197-366 |
8.67e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 197 ISGSAAPGEVLALMGPSGSGKT-TLLSILGGRVAGPGDVEgcvsyNDEPYCKSLNRR-IGFVTQDDVLFTH-------LT 267
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQ-----CDKMLLRRRSRQvIELSEQSAAQMRHvrgadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 268 VKETLT-----------YAALLRLPRTMTRQE---KEERTIDIIyelgleRCQDT-MIGGSFVRGVSGGERKRVCIGNEI 332
Cdd:PRK10261 110 FQEPMTslnpvftvgeqIAESIRLHQGASREEamvEAKRMLDQV------RIPEAqTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190
....*....|....*....|....*....|....
gi 1002256437 333 IINPSLLFLDEPTSGLDSTTALRIIQLLHDIAED 366
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
191-410 |
9.06e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRVAGPGD----VEGCVSYndepyckslnrrigfVTQDDVLFtHL 266
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvIRGTVAY---------------VPQVSWIF-NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 267 TVKETLTYAALLrlprtmtRQEKEERTIDIIyelGLERCQDTMIGGSFV----RGV--SGGERKRVCIGNEIIINPSLLF 340
Cdd:PLN03130 694 TVRDNILFGSPF-------DPERYERAIDVT---ALQHDLDLLPGGDLTeigeRGVniSGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 341 LDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpsSRLFHKFDKLILLGRGSLLYFGKASEAM---PYFQ 410
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQ--LHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQ 834
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
319-401 |
1.00e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 319 SGGERKRVCIGNEIIINP--SLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQPssRLFHKFDKLILLGRGSL 396
Cdd:cd03238 89 SGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSG 166
|
....*
gi 1002256437 397 LYFGK 401
Cdd:cd03238 167 KSGGK 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
204-375 |
1.02e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 204 GEVLALMGPSGSGKTTLL-SILG------GRVAGPG-DVEGcvsYNDEPYcKSLNRRIGFVTQDDV--LFTHLTVKETLt 273
Cdd:PRK15079 47 GETLGVVGESGCGKSTFArAIIGlvkatdGEVAWLGkDLLG---MKDDEW-RAVRSDIQMIFQDPLasLNPRMTIGEII- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 274 yAALLRL--PRtMTRQEKEERTIDIIYELGLercQDTMIGgSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDST 351
Cdd:PRK15079 122 -AEPLRTyhPK-LSRQEVKDRVKAMMLKVGL---LPNLIN-RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180
....*....|....*....|....*
gi 1002256437 352 TALRIIQLLHDI-AEDGKTVITTIH 375
Cdd:PRK15079 196 IQAQVVNLLQQLqREMGLSLIFIAH 220
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
200-393 |
2.14e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 200 SAAPGEVLALMGPSGSGKTTLLsilggrvagpgdvegcvsyndepyckslnrrigfvtqddvlfthltvkETLTYAALLR 279
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTIL------------------------------------------------DAIGLALGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 280 LPRTMTRQEKEErtidiiyelGLERCQDTMIGGSFVRGVSGGERKRVCI----GNEIIINPSLLFLDEPTSGLDSTTALR 355
Cdd:cd03227 49 QSATRRRSGVKA---------GCIVAAVSAELIFTRLQLSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002256437 356 IIQLLHDIAEDGKTVITTIHQPssRLFHKFDKLILLGR 393
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
187-378 |
2.22e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.59 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 187 KGTP------------REILSGISGSAAPGEVLALMGPSGSGKTTLLSILGG-RVAGPGDV-EGCVSYNDepyckslnrr 252
Cdd:PRK11247 9 QGTPlllnavskrygeRTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGELlAGTAPLAE---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 253 igfvTQDDvlfTHLTVKEtltyAALLRLPRTMT------RQEKEERTIDIIYELGL-ERCQDtmiggsFVRGVSGGERKR 325
Cdd:PRK11247 79 ----ARED---TRLMFQD----ARLLPWKKVIDnvglglKGQWRDAALQALAAVGLaDRANE------WPAALSGGQKQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002256437 326 VCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIHQPS 378
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVS 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
289-407 |
2.93e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 289 KEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGK 368
Cdd:PRK15093 132 RKRRAIELLHRVGIKDHKDAM--RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNN 209
|
90 100 110
....*....|....*....|....*....|....*....
gi 1002256437 369 TVITTIHQPSSRLFHKFDKLillgrgSLLYFGKASEAMP 407
Cdd:PRK15093 210 TTILLISHDLQMLSQWADKI------NVLYCGQTVETAP 242
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
375-636 |
3.66e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.82 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 375 HQPSSRLFHKFDKLILLGRGSL-LYFGKASEAMPYFQSIGCTPLIAMNPAEFLLDLANG-----NTTDVS---------- 438
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLtVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEGivkpsTSSGVDykqlpvrwml 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 439 -----VPSEL---DDKVHMENQNLQTNTKNDYKPS-----AQDVHEYLVDAYENRvaykaKKQLLDPLPISDDMkttitS 505
Cdd:pfam19055 81 hngypVPPDMlqnADGIAASSGENSSNGTNPGVGSeeqsfAGELWQDVKSNVELK-----RDHIRHNFLKSKDL-----S 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 506 SKREWGTswWQQYSILFCRGIKERrhdyLSWMRItQVI------ATSVILGLLwwhSDPStpkglqDQA----------- 568
Cdd:pfam19055 151 NRRTPGV--FRQYRYFLGRVGKQR----LREARI-QAVdylillLAGACLGTL---AKVS------DETfgalgytytii 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 569 --GLLFFIAvfwgffpvftAIFTFPQERAMLNKERAADMYKLsAYFLARTTSDLPLDLFLPVIFMVIVYF 636
Cdd:pfam19055 215 avSLLCKIA----------ALRSFSLDKLQYWRESASGMSSL-AYFLAKDTIDHFNTVIKPLVYLSMFYF 273
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
203-394 |
3.99e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 203 PGEVLALMGPSGSGKTTLLSILGGRVAGPGdvEGCVSYNDEpyckslnrrigfvtqddvlfthltvkETLTYAALLRLPR 282
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGE--------------------------DILEEVLDQLLLI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 283 TMTRQEKEERTIDIIYELgLERCQDTmiggsfvrgvsggerkrvcigneiiiNPSLLFLDEPTSGLDSTTALRIIQLLHD 362
Cdd:smart00382 53 IVGGKKASGSGELRLRLA-LALARKL--------------------------KPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002256437 363 ------IAEDGKTVITTIHQP----SSRLFHKFDKLILLGRG 394
Cdd:smart00382 106 rlllllKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
191-371 |
7.33e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 191 REILSGISGSAAPGEVLALMGPSGSGKTTL-LSILG---GRvagpgDVEGCVSYNDEPY-CKSLNRRIG----FVTQD-D 260
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsyGR-----NISGTVFKDGKEVdVSTVSDAIDaglaYVTEDrK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 261 VLFTHL--TVKETLTYAALLRLPRTMTRQEKEERTIdiiyelgLERCQDTM-IGGSFVRGV----SGGERKRVCIGNEII 333
Cdd:NF040905 348 GYGLNLidDIKRNITLANLGKVSRRGVIDENEEIKV-------AEEYRKKMnIKTPSVFQKvgnlSGGNQQKVVLSKWLF 420
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002256437 334 INPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVI 371
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
190-406 |
7.72e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 190 PREILSGISGSAAPGEVLALMGPSGSGKTTLL-SILGGRVAGPGDV--EGCVSY-NDEPYCKSLNRR--IGFVTQDDVLF 263
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEISEGRVwaERSIAYvPQQAWIMNATVRgnILFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 264 THLTVKETLTYAALLRLPRtmtrqekeertidiiyelGLErcqdTMIGGSFVRgVSGGERKRVCIGNEIIINPSLLFLDE 343
Cdd:PTZ00243 752 LADAVRVSQLEADLAQLGG------------------GLE----TEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256437 344 PTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQpsSRLFHKFDKLILLGRGSLLYFGKASEAM 406
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
181-375 |
1.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.92 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 181 KYKVAVKGTPREILSGISGSAAPGEVLALMGPSGSGKTT-------LLSILGGRVAgpgdVEGcVSYNDEPYCKSLNRRI 253
Cdd:PRK13633 13 KYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVY----VDG-LDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 254 GFVTQD-DVLFTHLTVKETLTYAallrlPRTMTRQEKEERtidiiyelglERCQDTM--IGGSFVRG-----VSGGERKR 325
Cdd:PRK13633 88 GMVFQNpDNQIVATIVEEDVAFG-----PENLGIPPEEIR----------ERVDESLkkVGMYEYRRhaphlLSGGQKQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 326 VCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDI-AEDGKTVITTIH 375
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH 203
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
180-403 |
1.92e-04 |
|
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: 43.74 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 180 VKYKVAVKgtprEILSGISGSAAPGEVLALMGPSGSGKTTL-------LSILGGRVAGPGdvegcVSYNDEPYcKSLNRR 252
Cdd:cd03288 27 VRYENNLK----PVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDG-----IDISKLPL-HTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 253 IGFVTQDDVLFThltvketltyaALLRLPRTMTRQEKEERTIDIIYELGLERCQDTMIGGSFVRGVSGGE------RKRV 326
Cdd:cd03288 97 LSIILQDPILFS-----------GSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEnfsvgqRQLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256437 327 CIGNEIIINPSLLFLDEPTSGLDSTTAlRIIQLLHDIAEDGKTVITTIHQPSSRLfhKFDKLILLGRGSLLYFGKAS 403
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVSTIL--DADLVLVLSRGILVECDTPE 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
179-366 |
3.11e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 179 EVKYKVAVKgtprEILSGISGSAAPGEVLALMGPSGSGKTTLLSILGGRV-AGPGDVegcvsyndepyckslnrRIGfvt 257
Cdd:PRK11147 324 NVNYQIDGK----QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRI-----------------HCG--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 258 qddvlfTHLTVKETLTYAALLRLPRTmtrqekeertidIIYELGlERCQDTMIGG----------SF----------VRG 317
Cdd:PRK11147 380 ------TKLEVAYFDQHRAELDPEKT------------VMDNLA-EGKQEVMVNGrprhvlgylqDFlfhpkramtpVKA 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002256437 318 VSGGERKRVCIGnEIIINPS-LLFLDEPTSGLDSTTalriIQLLHDIAED 366
Cdd:PRK11147 441 LSGGERNRLLLA-RLFLKPSnLLILDEPTNDLDVET----LELLEELLDS 485
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
286-441 |
5.97e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.59 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 286 RQEKEERTIDIIYELGLERCQDTMigGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAE 365
Cdd:COG4170 129 FKWRKKRAIELLHRVGIKDHKDIM--NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 366 DGKTVITTIHQPSSRLFHKFDKLillgrgSLLYFGKASEAMPYfQSIGCTP-------LIAMNPaEFLLDLANG---NTT 435
Cdd:COG4170 207 LQGTSILLISHDLESISQWADTI------TVLYCGQTVESGPT-EQILKSPhhpytkaLLRSMP-DFRQPLPHKsrlNTL 278
|
....*.
gi 1002256437 436 DVSVPS 441
Cdd:COG4170 279 PGSIPP 284
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
169-349 |
1.17e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 169 PTLP-----IYLKFAEVKYkvavkgTPREILSGISGSAAPGEVLALMGPSGSGKTTLLSI--------------LGGRVA 229
Cdd:PRK10938 252 HALPaneprIVLNNGVVSY------NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLFGRRR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 230 GPG----DVEgcvsyndepyckslnRRIGFVTQDdvlfTHL------TVKETL---------TYAALLRLPRTMTRQeke 290
Cdd:PRK10938 326 GSGetiwDIK---------------KHIGYVSSS----LHLdyrvstSVRNVIlsgffdsigIYQAVSDRQQKLAQQ--- 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 291 erTIDIiyeLGLercqDTMIGGSFVRGVSGGERKRVCIGNEIIINPSLLFLDEPTSGLD 349
Cdd:PRK10938 384 --WLDI---LGI----DKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
194-353 |
1.65e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 194 LSGISGSAAPGEVLALMGPSGSGKTTLLSILGG---RVAGPGDVEG-CVSYNDEPycKSLNRRIGFVTQDDVLFTHLTVK 269
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiytRDAGSILYLGkEVTFNGPK--SSQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256437 270 ETLTyaallrLPRTMTR-------QEKEERTIDIIYELGLERCQDTMIGgsfvrGVSGGERKRVCIGNEIIINPSLLFLD 342
Cdd:PRK10762 98 ENIF------LGREFVNrfgridwKKMYAEADKLLARLNLRFSSDKLVG-----ELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170
....*....|..
gi 1002256437 343 EPTSGL-DSTTA 353
Cdd:PRK10762 167 EPTDALtDTETE 178
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
319-376 |
5.72e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 5.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256437 319 SGGERKRVCIGNEIIiNPS----LLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIHQ 376
Cdd:cd03271 171 SGGEAQRIKLAKELS-KRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
318-375 |
6.16e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 6.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256437 318 VSGGERKRVCIGNEIII---NPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDGKTVITTIH 375
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
318-375 |
7.88e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.94 E-value: 7.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256437 318 VSGGERKRVCIGNEIIINPSLLFLDEPTSGLDSTTALRIIQLLHDIAEDG-KTVITTIH 375
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEH 130
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
201-234 |
9.33e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 37.86 E-value: 9.33e-03
10 20 30
....*....|....*....|....*....|....
gi 1002256437 201 AAPGEVLALMGPSGSGKTTLLSILGGRVAGPGDV 234
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAADPRL 35
|
|
| |
