|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
45-636 |
0e+00 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 719.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 45 TPWGRQFWRITRAYFVGPNSVRVWLMLGVLLLSVVLAVRLNVLFSYQGNDMYTALQKAFEGiasgdgtvkrsgvrGFWMS 124
Cdd:COG4178 1 RSLLRQFWRLARPYWRSEEKWKAWGLLALLLLLTLASVGLNVLLNFWNRDFYDALQARDAA--------------AFWQQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 125 IGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQDWLDGRAYYRDLFIDETIDNPDQRIQQDVDIFTagaggtpn 204
Cdd:COG4178 67 LGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFT-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 205 apsnGTASTLLFGAVQSIISVISFTAILWNLSG--TLNIFG--VSIPRAMFWTVLVYVFVATVISFIIGRPLIWLSFRNE 280
Cdd:COG4178 139 ----ETTLSLSLGLLSSVVTLISFIGILWSLSGslTFTLGGysITIPGYMVWAALIYAIIGTLLTHLIGRPLIRLNFEQQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 281 KLNAAFRYALVRLRDAAEAVGFYRGERVEGTQLQRRFTPVIDNYRRYVRRSIAFNGWNLSVSQTIVPLPWVIQAPRLFAG 360
Cdd:COG4178 215 RREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 361 QIDFGDVGQTATSFGNIHDSLSFFRNNYDAFASFRAAIIRLHGLVDANEKGRALPAVLTR--PSDDESVELNDIEVRTPA 438
Cdd:COG4178 295 EITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADALPEAASRieTSEDGALALEDLTLRTPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnETMFLSQLPYVPLGTLRDVVCYPNSAA 518
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVLFLPQRPYLPLGTLREALLYPATAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 519 AIPDATLRDTLTKVALAPLCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELP 598
Cdd:COG4178 454 AFSDAELREALEAVGLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP 533
|
570 580 590
....*....|....*....|....*....|....*...
gi 489997411 599 DCIVISVSHRPALERLHENQLELLGGGQWRLAPVEAAP 636
Cdd:COG4178 534 GTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
85-358 |
9.63e-86 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 269.09 E-value: 9.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 85 NVLFSYQGNDMYTALQkafegiasgdgtvkRSGVRGFWMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQD 164
Cdd:pfam06472 31 SVLVAQLDGQIVKALV--------------AKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRFRTRLTRHLHDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 165 WLDGRAYYRDLFIDETIDNPDQRIQQDVDIFTAgaggtpnapsngTASTLLFGAVQSIISVISFTAILWNLSGTLNIfgv 244
Cdd:pfam06472 97 YLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCS------------SLSDLYSNLLKPILDIILFTFRLWRLSGWRGP--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 245 sipramfWTVLVYVFVATVISFIIGRPLIWLSFRNEKLNAAFRYALVRLRDAAEAVGFYRGERVEGTQLQRRFTPVIDNY 324
Cdd:pfam06472 162 -------AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
|
250 260 270
....*....|....*....|....*....|....*
gi 489997411 325 RRYVRRSIAFNGWNLSV-SQTIVPLPWVIQAPRLF 358
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVlKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
427-627 |
1.68e-74 |
|
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: 235.90 E-value: 1.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENeTMFLSQLPYVPLGT 506
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGED-LLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPnsaaaipdatlrdtltkvalaplcdrldeerdWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLE 586
Cdd:cd03223 80 LREQLIYP--------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 587 FALYQLLRSELpdCIVISVSHRPALERLHENQLELLGGGQW 627
Cdd:cd03223 128 DRLYQLLKELG--ITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
106-629 |
4.20e-58 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 206.91 E-value: 4.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 106 IASGDGTVKRSGVRG----FWMSIGVFSVMAVLhVTRVMADI-YLTQRFIIAWRVWLTHHLTQDWLDGRAYYRDLFIDET 180
Cdd:TIGR00954 115 VATLDGQIESSIVRRsprnFAWILFKWFLIAPP-ASFINSAIkYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 181 IDNPDQRIQQDVDIFtagaggtpnapSNGTAStLLFGAVQSIISVISFTAILwnlsgtlnifGVSIPRAMFWTVLVYVFV 260
Cdd:TIGR00954 194 IQNPDQLLTQDVEKF-----------CDSVVE-LYSNLTKPILDVILYSFKL----------LTALGSVGPAGLFAYLFA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 261 ATVISFIIGRPLIWLSFRNEKLNAAFRYALVRLRDAAEAVGFYRGERVEGTQLQRRFTPVIDNYRR--YVRRSIAF---- 334
Cdd:TIGR00954 252 TGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLiiKFRFSYGFldni 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 335 --------NGWnLSVSQTIV--------------PLPWVIQAPRLFAGQIDFGdvGQTATSFGNIhDSLSFFRNNYDAFA 392
Cdd:TIGR00954 332 vakytwsaVGL-VAVSIPIFdkthpaflemseeeLMQEFYNNGRLLLKAADAL--GRLMLAGRDM-TRLAGFTARVDTLL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 393 SFRAAIIRLH-------GLVDANEKGRALPAVLTRPS---DDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRS 462
Cdd:TIGR00954 408 QVLDDVKSGNfkrprveEIESGREGGRNSNLVPGRGIveyQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPN 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 463 GAGKTTLLRSLAELWPYASGTLHRPGgENETMFLSQLPYVPLGTLRDVVCYPNSA-----AAIPDATLRDTLTKVALAPL 537
Cdd:TIGR00954 488 GCGKSSLFRILGELWPVYGGRLTKPA-KGKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQLTHI 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 538 CDR---LDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSElpDCIVISVSHRPALERL 614
Cdd:TIGR00954 567 LEReggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKY 644
|
570
....*....|....*
gi 489997411 615 HENQLELLGGGQWRL 629
Cdd:TIGR00954 645 HEYLLYMDGRGGYQF 659
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
122-610 |
8.30e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.59 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 122 WMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHL-TQDWldgrAYYRDLFIDETIdnpdQRIQQDVDIFTAgag 200
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLlRLPL----SFFDRRRTGDLL----SRLTNDVDAVEQ--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 201 gtpnapsngTASTLLFGAVQSIISVISFTAILWNLSgtlnifgvsipramfWTVLVYVFVATVISFIIgrpLIWLSFRNE 280
Cdd:COG1132 134 ---------FLAHGLPQLVRSVVTLIGALVVLFVID---------------WRLALIVLLVLPLLLLV---LRLFGRRLR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 281 KLNAAFRYALVRLrdAAEAVGFYRGERV------EGTQLqRRFTPVIDNYRRYVRRSIAFNGWNLSVSQTIVPLPWVI-- 352
Cdd:COG1132 187 KLFRRVQEALAEL--NGRLQESLSGIRVvkafgrEEREL-ERFREANEELRRANLRAARLSALFFPLMELLGNLGLALvl 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 353 --QAPRLFAGQIDFGDVGQTATSFGNIHDSLSFFRNNYDAFASFRAAIIRLHGLVDANEKGRALPAVLTRPSDDESVELN 430
Cdd:COG1132 264 lvGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 431 DIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-ETMFLSQLP----YVP-- 503
Cdd:COG1132 344 NVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDiRDLTLESLRrqigVVPqd 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 --L--GTLRDVVCYPNsaaaiPDAT---LRDTLTKVALAPLCDRLDE-------ERdwAKVLSPGEQQRVAFARILLTKP 569
Cdd:COG1132 423 tfLfsGTIRENIRYGR-----PDATdeeVEEAAKAAQAHEFIEALPDgydtvvgER--GVNLSGGQRQRIAIARALLKDP 495
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489997411 570 KAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPA 610
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLS 536
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
395-610 |
2.98e-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: 119.49 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 395 RAAIIRLHGLVDAnEKGRALPAVLTRPSDDESVELNDIEVRTPAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSL 473
Cdd:COG4987 303 RAAARRLNELLDA-PPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 474 AELWPYASGTLhRPGGEN----------ETM-FLSQLPYVPLGTLRDvvcypNSAAAIPDAT---LRDTLTKVALAPLCD 539
Cdd:COG4987 382 LRFLDPQSGSI-TLGGVDlrdldeddlrRRIaVVPQRPHLFDTTLRE-----NLRLARPDATdeeLWAALERVGLGDWLA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 540 RLDEERDwAKV------LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPA 610
Cdd:COG4987 456 ALPDGLD-TWLgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
428-624 |
7.05e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-----------ETMFL 496
Cdd:COG4619 2 ELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGKPlsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYVPLGTLRDVVCYPNSAAAIP--DATLRDTLTKVALAPlcDRLDEErdwAKVLSPGEQQRVAFARILLTKPKAVFL 574
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKfdRERALELLERLGLPP--DILDKP---VERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489997411 575 DESTSALDTGLEFALYQLLRSEL--PDCIVISVSHRPA-LERLHENQLELLGG 624
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEqIERVADRVLTLEAG 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
212-611 |
8.41e-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: 115.70 E-value: 8.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 212 STLLFGAVQSIISVISFTAILWNLSGTLnifgvsipramFWTVLVYVFVATVISFIIGRPLIWLSFRNEKLNAAFRYALV 291
Cdd:COG2274 270 TGSLLTALLDLLFVLIFLIVLFFYSPPL-----------ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLV 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 292 RLRDAAEAVGFYRGERVEGTQLQRRFTPVIDNYRRYVRRSIAFNGWNLSVSQ--TIVPLpwVIQAPRLFAGQIDFGD--- 366
Cdd:COG2274 339 ETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQlaTVALL--WLGAYLVIDGQLTLGQlia 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 367 ----VGQTATSFGNIHDSLSFFrnnYDAfasfRAAIIRLHGLVDANEKGRALPAVLTRPSDDESVELNDIEVR-TPAGDR 441
Cdd:COG2274 417 fnilSGRFLAPVAQLIGLLQRF---QDA----KIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRyPGDSPP 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 442 LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQLP---------YVP----L--GT 506
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-LIDGID----LRQIDpaslrrqigVVLqdvfLfsGT 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYpnSAAAIPDATLRDTLTKVALAPLCDRLDE-------ERdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:COG2274 565 IRENITL--GDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgEG--GSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
410 420 430
....*....|....*....|....*....|..
gi 489997411 580 ALDTGLEFALYQLLRSELPDCIVISVSHRPAL 611
Cdd:COG2274 641 ALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
396-611 |
1.88e-26 |
|
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: 114.08 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 396 AAIIRLHGLVDANEKGRALPAVLTRPSDDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAE 475
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 476 LWPYASGTLHRPGGENETM----------FLSQLPYVPLGTLRDvvcypNSAAAIPDAT---LRDTLTKVALAPLCDRLD 542
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLdpaswrrqiaWVPQNPYLFAGTIRE-----NLRLGRPDASdeeLEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 543 E-------ERdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPAL 611
Cdd:COG4988 461 DgldtplgEG--GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLAL 534
|
|
| PRK12369 |
PRK12369 |
putative transporter; Reviewed |
121-401 |
4.47e-26 |
|
putative transporter; Reviewed
Pssm-ID: 171443 [Multi-domain] Cd Length: 326 Bit Score: 109.39 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 121 FWMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQDWLDgrayyrdlfIDETIDNPDQRIQQDVDIFTAgag 200
Cdd:PRK12369 62 FWASILSFLAIAMPYVLIATVVDYFASHYAFRWREAMTFSYLKFWRN---------KRDNIEGSSQRIQEDTYRFAK--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 201 gtpnapsngTASTLLFGAVQSIISVISFTAILWNLSGTLNI-FGVSIPRAMFWTVLVYVFVATVISFIIGRPLIWLSFRN 279
Cdd:PRK12369 130 ---------IMESLGLSFLRAIMTLIAFIPILWGLSDGVSLpFLKDIPGSLVWIALLISLGGLVISWFVGIKLPGLEYNN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 280 EKLNAAFRYALVRLRDAAEavgfyRGERVEGtqLQRRFTPVIDNYRRYVRRSIAFNGWNLSVSQTIVPLPWVIQAPRLFA 359
Cdd:PRK12369 201 QKVEAAFRKELVYAEDDKK-----NYAKPET--LIELFTGLRFNYFRLFLHYGYFNIWLISFSQMMVIVPYLIMAPGLFA 273
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489997411 360 GQIDFGDVGQTATSFGNIHDSLSFFRNNYDAFASFRAAIIRL 401
Cdd:PRK12369 274 GVITLGVLMQISNAFSQVRSSFSVFIRNWTTITELRSIYKRL 315
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
427-614 |
6.90e-26 |
|
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: 104.39 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmflsqLPYVPLG 505
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGVD-------LRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 TLRDVVCYPNSAAAIPDATLRDTLtkvalaplcdrldeerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSGTIRENI---------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180
....*....|....*....|....*....
gi 489997411 586 EFALYQLLRSELPDCIVISVSHRPALERL 614
Cdd:cd03228 132 EALILEALRALAKGKTVIVIAHRLSTIRD 160
|
|
| SbmA_BacA |
pfam05992 |
SbmA/BacA-like family; The Rhizobium meliloti bacA gene encodes a function that is essential ... |
121-388 |
1.49e-25 |
|
SbmA/BacA-like family; The Rhizobium meliloti bacA gene encodes a function that is essential for bacterial differentiation into bacteroids within plant cells in the symbiosis between R. meliloti and alfalfa. An Escherichia coli homolog of BacA, SbmA, is implicated in the uptake of microcins and bleomycin. This family is likely to be a subfamily of the ABC transporter family.
Pssm-ID: 461797 [Multi-domain] Cd Length: 314 Bit Score: 107.50 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 121 FWMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQDWLDGRayyrdlfideTIDNPDQRIQQDVDIFTAgag 200
Cdd:pfam05992 55 FYASLLVFLGIAFIYVTIAVLNLFFVSHYVFRWRTAMNDYYTSHWQQLR----------HIEGASQRVQEDTMRFAS--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 201 gtpnapsngTASTLLFGAVQSIISVISFTAILWNLSG---TLNIFGvSIPRAMFWTVLVYVFVATVISFIIGRPLIWLSF 277
Cdd:pfam05992 122 ---------IVEDLGVSLVRAIMTLIAFLPVLFGLSKhvpVLPIIG-DIPHSLVWAAVVWSLGGTVFLAVVGIKLPGLEF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 278 RNEKLNAAFRYALVRLRDAAeavgfyrgERVEGTQLQRRFTPVIDNYRRYVRRSIAFNGWNLSVSQTIVPLPWVIQAPRL 357
Cdd:pfam05992 192 NNQKVEAAYRKELVYGEDDA--------TRATPKTLKELFSDVRKNYFRLYFHYMYFNIARIFYLQLDNLFGYIFLAPSI 263
|
250 260 270
....*....|....*....|....*....|.
gi 489997411 358 FAGQIDFGDVGQTATSFGNIHDSLSFFRNNY 388
Cdd:pfam05992 264 VAGKITLGVMQQITNVFGKVRGSFQYLINSW 294
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
428-626 |
2.05e-23 |
|
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: 96.93 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGgenetmflSQLPYVPLGTL 507
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------KDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYpnsaaaIPDatlrdtltkvalaplcdrldeerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEF 587
Cdd:cd00267 72 RRRIGY------VPQ----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489997411 588 ALYQLLRSELPD-CIVISVSHRPALERLHENQLELLGGGQ 626
Cdd:cd00267 118 RLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
439-609 |
9.39e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 96.39 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGG---ENETMFLSQLPYVP--LG-----TL 507
Cdd:COG4133 13 GERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirDAREDYRRRLAYLGhaDGlkpelTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDvvcypN-------SAAAIPDATLRDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSA 580
Cdd:COG4133 93 RE-----NlrfwaalYGLRADREAIDEALEAVGLAGLADLP------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|.
gi 489997411 581 LDT-GLEfALYQLLRSELPD-CIVISVSHRP 609
Cdd:COG4133 162 LDAaGVA-LLAELIAAHLARgGAVLLTTHQP 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
427-610 |
1.41e-21 |
|
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: 93.35 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEvRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENET----------MFL 496
Cdd:cd03259 1 LELKGLS-KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTgvpperrnigMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYVPLGTLRDVVCYPNSAAAIPDATLRD----TLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAV 572
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRArvreLLELVGLEGLLNRYPHE------LSGGQQQRVALARALAREPSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 573 FLDESTSALDTGLEFALYQLLRS---ELpDCIVISVSHRPA 610
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElqrEL-GITTIYVTHDQE 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-609 |
1.55e-21 |
|
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: 98.59 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 395 RAAIIRLHGLVDANEKGRA--LPAVLTRPSDDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRS 472
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEgsAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 473 LAELWPYASGTLHRPGGENETM----------FLSQLPYVPLGTLRDvvcypNSAAAIPDAT---LRDTLTKVALAPLCD 539
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLdqdevrrrvsVCAQDAHLFDTTVRE-----NLRLARPDATdeeLWAALERVGLADWLR 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489997411 540 RLDEERDW-----AKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRP 609
Cdd:TIGR02868 456 ALPDGLDTvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
428-626 |
4.91e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 90.96 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENetmfLSQLPYVPLGTL 507
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-DGKD----LASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVcypnsaaaiPDAtlrdtLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEF 587
Cdd:cd03214 75 IAYV---------PQA-----LELLGLAHLADRPFNE------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 588 ALYQLLR--SELPDCIVISVSHRPALERLHENQLELLGGGQ 626
Cdd:cd03214 135 ELLELLRrlARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
428-611 |
6.25e-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: 87.27 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQlpyVPLGT 506
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-RLDGAD----ISQ---WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPNSAAAIPDATLRDTltkvalaplcdrldeerdwakVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLE 586
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAEN---------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180
....*....|....*....|....*.
gi 489997411 587 FALYQLLRS-ELPDCIVISVSHRPAL 611
Cdd:cd03246 133 RALNQAIAAlKAAGATRIVIAHRPET 158
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
427-594 |
2.11e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 87.94 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLD---VRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---RPGGENETM------ 494
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKdvsLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgRPVTRRRRKafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 -FLSQLPYV---PLGTLRDVVCYPNSAAAIPD--ATLRDTLTKVALAP-LCDRLDEErdwakvLSPGEQQRVAFARILLT 567
Cdd:COG1124 82 qMVFQDPYAslhPRHTVDRILAEPLRIHGLPDreERIAELLEQVGLPPsFLDRYPHQ------LSGGQRQRVAIARALIL 155
|
170 180
....*....|....*....|....*..
gi 489997411 568 KPKAVFLDESTSALDTGLEFALYQLLR 594
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLK 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
423-614 |
2.15e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.96 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 423 DDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENETMF------- 495
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVNGVPLADAdadswrd 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 ----LSQLPYVPLGTLRDvvcypNSAAAIPDAT---LRDTLTKVALAPLCDRLdeERDWAKV-------LSPGEQQRVAF 561
Cdd:TIGR02857 397 qiawVPQHPFLFAGTIAE-----NIRLARPDASdaeIREALERAGLDEFVAAL--PQGLDTPigeggagLSGGQAQRLAL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489997411 562 ARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPALERL 614
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
446-607 |
2.84e-19 |
|
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: 86.82 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGgENETMFLSQLPYVPL---------GTLRDVV---CY 513
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-KPLEKERKRIGYVPQrrsidrdfpISVRDVVlmgLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 514 P-------NSAAAIPDAtlRDTLTKVALAPLCDR-LDEerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:cd03235 97 GhkglfrrLSKADKAKV--DEALERVGLSELADRqIGE-------LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180
....*....|....*....|....
gi 489997411 586 EFALYQLLRsELPD--CIVISVSH 607
Cdd:cd03235 168 QEDIYELLR-ELRRegMTILVVTH 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
427-607 |
1.48e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.53 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRtpAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM-----FLSQLP 500
Cdd:COG1121 7 IELENLTVS--YGGRPVlEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 YVPLG---TLRDVV---CYPN-SAAAIPDATLRD----TLTKVALAPLCDR-LDEerdwakvLSPGEQQRVAFARILLTK 568
Cdd:COG1121 85 EVDWDfpiTVRDVVlmgRYGRrGLFRRPSRADREavdeALERVGLEDLADRpIGE-------LSGGQQQRVLLARALAQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 569 PKAVFLDESTSALDTGLEFALYQLLRsELPD--CIVISVSH 607
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLR-ELRRegKTILVVTH 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
458-608 |
2.30e-18 |
|
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: 84.47 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQL----------PYVPLGTLRDVVCyPNSAAaiPDATLRD 527
Cdd:cd03244 35 IVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrsrisiipqdPVLFSGTIRSNLD-PFGEY--SDEELWQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 528 TLTKVALAPLCDRLDEERDwAKV------LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCI 601
Cdd:cd03244 112 ALERVGLKEFVESLPGGLD-TVVeeggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT 190
|
....*..
gi 489997411 602 VISVSHR 608
Cdd:cd03244 191 VLTIAHR 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
427-607 |
7.25e-18 |
|
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: 83.55 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-ETM----------F 495
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-LLDGRDlASLsrrelarriaY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 LSQLPYVPLG-TLRDVV---CYP-NSAAAIPDATLR----DTLTKVALAPLCDR-LDEerdwakvLSPGEQQRVAFARIL 565
Cdd:COG1120 80 VPQEPPAPFGlTVRELValgRYPhLGLFGRPSAEDReaveEALERTGLEHLADRpVDE-------LSGGERQRVLIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489997411 566 LTKPKAVFLDESTSALDTGLEFALYQLLR--SELPDCIVISVSH 607
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLH 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
443-579 |
1.27e-17 |
|
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: 80.00 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLP----YV-------PLGTLRDVV 511
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigYVfqdpqlfPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 512 CYPNSAAAIPDATLRDTLTKV-ALAPLCDRLDEE-RDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEAlEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
427-594 |
1.28e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 82.17 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGD---RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM--------- 494
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 ----FLSQLPYV---PLGTLRDVVC------YPNSAAAIPDATLRDTLTKVALAPLC-DRLDEErdwakvLSPGEQQRVA 560
Cdd:cd03257 82 keiqMVFQDPMSslnPRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHE------LSGGQRQRVA 155
|
170 180 190
....*....|....*....|....*....|....
gi 489997411 561 FARILLTKPKAVFLDESTSALDTGLEFALYQLLR 594
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLK 189
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
427-624 |
1.41e-17 |
|
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: 81.77 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPL---DVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGE------------- 490
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-RVDGTdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 491 -NETM-FLSQ----LPYVplgTLRDVVCYPNSAAAIPDATLRD----TLTKVALAplcDRLDeerdwAKV--LSPGEQQR 558
Cdd:cd03255 80 rRRHIgFVFQsfnlLPDL---TALENVELPLLLAGVPKKERREraeeLLERVGLG---DRLN-----HYPseLSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 559 VAFARILLTKPKAVFLDESTSALD--TGLEFalYQLLRS--ELPDCIVISVSHRPALERLHENQLELLGG 624
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDseTGKEV--MELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
426-614 |
3.18e-17 |
|
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: 81.10 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVRTPAGDRL-IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM---------- 494
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 FLSQLPYVPLGTLRDvvcypNSAAAIPDATLRDTLTKVALAPL----------CDRLDEERDWAkvLSPGEQQRVAFARI 564
Cdd:cd03245 82 YVPQDVTLFYGTLRD-----NITLGAPLADDERILRAAELAGVtdfvnkhpngLDLQIGERGRG--LSGGQRQAVALARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489997411 565 LLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPALERL 614
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDL 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
428-594 |
8.77e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPYaSGTLH---RPggenetmfLSQLP--- 500
Cdd:COG4559 3 EAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgELTPS-SGEVRlngRP--------LAAWSpwe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 ----------YVPLG---TLRDVVC---YPNSAAAIPDATL-RDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFAR 563
Cdd:COG4559 73 larrravlpqHSSLAfpfTVEEVVAlgrAPHGSSAAQDRQIvREALALVGLAHLAGRSYQT------LSGGEQQRVQLAR 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 489997411 564 ILL-------TKPKAVFLDESTSALDTGLEFALYQLLR 594
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLAR 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
439-583 |
1.63e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENE-TMFLSQLPYV-------PLGTLRDV 510
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLghrnamkPALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489997411 511 VCYPNSAAAIPDATLRDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDT 583
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAVGLAPLAHLP------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
427-608 |
1.75e-16 |
|
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: 77.74 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmfLSQLPyvplG 505
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----VSDLE----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 TLRDVVCYPNSAAAIPDATLRDTLtkvalaplcdrldeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:cd03247 72 ALSSLISVLNQRPYLFDTTLRNNL------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180
....*....|....*....|...
gi 489997411 586 EFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03247 134 ERQLLSLIFEVLKDKTLIWITHH 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
443-607 |
2.15e-16 |
|
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: 79.13 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---RPGGENETMFLSQLPYVPLG-------TLRDVVC 512
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgEDVRKEPREARRQIGVLPDErglydrlTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 513 YPNSAAAIPDATLRDTLTKVAlaplcDR--LDEERD--WAKvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFA 588
Cdd:COG4555 97 YFAELYGLFDEELKKRIEELI-----ELlgLEEFLDrrVGE-LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
|
170 180
....*....|....*....|.
gi 489997411 589 LYQLLRS--ELPDCIVISvSH 607
Cdd:COG4555 171 LREILRAlkKEGKTVLFS-SH 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
424-608 |
2.20e-16 |
|
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: 78.22 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 424 DESVELNDIEVR-TPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETmflsqlpyV 502
Cdd:cd03369 4 HGEIEVENLSVRyAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST--------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 PLGTLRdvvcypNSAAAIP-DATLRDTLTKVALAPLcDRLDEERDWAKV--------LSPGEQQRVAFARILLTKPKAVF 573
Cdd:cd03369 76 PLEDLR------SSLTIIPqDPTLFSGTIRSNLDPF-DEYSDEEIYGALrvsegglnLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190
....*....|....*....|....*....|....*
gi 489997411 574 LDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHR 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
428-639 |
2.69e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPYaSGT---LHRPGGENETMFLSQ----L 499
Cdd:PRK13548 4 EARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPD-SGEvrlNGRPLADWSPAELARrravL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 P-YVPLG---TLRDVVC---YPNSAAAIPDATL-RDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILL----- 566
Cdd:PRK13548 82 PqHSSLSfpfTVEEVVAmgrAPHGLSRAEDDALvAAALAQVDLAHLAGRDYPQ------LSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 567 -TKPKAVFLDESTSALDTGLEFALYQLLRS---ELPDCiVISVSHRPALERLHENQLELLGGGqwRLApVEAAPAEV 639
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQlahERGLA-VIVVLHDLNLAARYADRIVLLHQG--RLV-ADGTPAEV 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
447-582 |
3.77e-16 |
|
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: 77.99 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTlhRPGGE----------NETMFLS---------QLPYVPLG 505
Cdd:cd03260 18 DISLDipKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA--PDEGEvlldgkdiydLDVDVLElrrrvgmvfQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 TLRDVVCYPNSAAAI-----PDATLRDTLTKVALAP-LCDRLDeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:cd03260 96 SIYDNVAYGLRLHGIklkeeLDERVEEALRKAALWDeVKDRLH-----ALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
...
gi 489997411 580 ALD 582
Cdd:cd03260 171 ALD 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
439-582 |
4.55e-16 |
|
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: 77.01 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENET---------MFLSQLPYV-PLGTLR 508
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdepheniLYLGHLPGLkPELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 509 DVVCYPNSAAAIPDATLRDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLP------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
421-616 |
5.28e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.43 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 421 PSDDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYaSGTLHRPGGE----NETMFL 496
Cdd:PRK11174 344 SNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIElrelDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQL------PYVPLGTLRDVVCYPNSAAAipDATLRDTLTKVALAPLCDRLD-----EERDWAKVLSPGEQQRVAFARIL 565
Cdd:PRK11174 423 KHLswvgqnPQLPHGTLRDNVLLGNPDAS--DEQLQQALENAWVSEFLPLLPqgldtPIGDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489997411 566 LTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRpaLERLHE 616
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQ--LEDLAQ 549
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
428-611 |
2.29e-15 |
|
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: 75.20 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmflsqLPYVPLGT 506
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD--------LTKLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVcypnsaaAI----PDATL-RDTLTK-VALAPLCDRLDEERDWAKV-------------------LSPGEQQRVAF 561
Cdd:cd03225 73 LRRKV-------GLvfqnPDDQFfGPTVEEeVAFGLENLGLPEEEIEERVeealelvgleglrdrspftLSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489997411 562 ARILLTKPKAVFLDESTSALDTGLEFALYQLLRsELPD---CIVIsVSHRPAL 611
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAegkTIII-VTHDLDL 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
427-608 |
3.52e-15 |
|
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: 75.34 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-----ETMFLSQLPY 501
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGQDirevtLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 502 VPL------GTLRDVVCYPNsaaaiPDATLRDTLTKVALAPLCDRLDEERDW--AKV------LSPGEQQRVAFARILLT 567
Cdd:cd03253 80 VPQdtvlfnDTIGYNIRYGR-----PDATDEEVIEAAKAAQIHDKIMRFPDGydTIVgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 568 KPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHR 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
427-595 |
3.56e-15 |
|
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: 74.75 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYV--PL 504
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 505 GT-------LRDVVCYPNSAAA--IPDATLRDTLTKVALA-PLCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFL 574
Cdd:cd03292 81 GVvfqdfrlLPDRNVYENVAFAleVTGVPPREIRKRVPAAlELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180
....*....|....*....|.
gi 489997411 575 DESTSALDTGLEFALYQLLRS 595
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKK 181
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
426-610 |
3.93e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAelwpyasGTLHRP---GGE---NETMfLSQL 499
Cdd:COG4136 1 MLSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA-------GTLSPAfsaSGEvllNGRR-LTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PYVP--LGTL-RDVVCYP------NSAAAIPDATLR--------DTLTKVALAPLcdrldEERDWAKvLSPGEQQRVAFA 562
Cdd:COG4136 72 PAEQrrIGILfQDDLLFPhlsvgeNLAFALPPTIGRaqrrarveQALEEAGLAGF-----ADRDPAT-LSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489997411 563 RILLTKPKAVFLDESTSALDTGL-----EFALYQLLRSELPdciVISVSHRPA 610
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALraqfrEFVFEQIRQRGIP---ALLVTHDEE 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
427-609 |
4.25e-15 |
|
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: 75.51 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTpaGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSL-AELWPYASGTLH----RPGGEN--E------ 492
Cdd:COG1119 4 LELRNVTVRR--GGKTIlDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRlfgeRRGGEDvwElrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 493 --TMFLsQLPYVPLGTLRDVVC---------YPN-SAAAIpdATLRDTLTKVALAPLCDRLdeerdWAKvLSPGEQQRVA 560
Cdd:COG1119 82 lvSPAL-QLRFPRDETVLDVVLsgffdsiglYREpTDEQR--ERARELLELLGLAHLADRP-----FGT-LSQGEQRRVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489997411 561 FARILLTKPKAVFLDESTSALDtglEFALYQLLRS-----ELPDCIVISVSHRP 609
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLD---LGARELLLALldklaAEGAPTLVLVTHHV 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
428-582 |
4.84e-15 |
|
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: 74.22 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-------ETM-FLSQL 499
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPikakerrKSIgYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PYVPLG--TLRDVVCYPNSAAAIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDES 577
Cdd:cd03226 80 VDYQLFtdSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS------LSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
....*
gi 489997411 578 TSALD 582
Cdd:cd03226 154 TSGLD 158
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
446-617 |
8.07e-15 |
|
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: 73.87 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLV-ITGRSGAGKTTLLRSLAELWPYASGTL---HRPGGENE-TMFLS-----------QLPYVPLGTLRD 509
Cdd:cd03297 15 LKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIvlnGTVLFDSRkKINLPpqqrkiglvfqQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 510 VVCYpnSAAAIPDATLRDTLTKV----ALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:cd03297 95 NLAF--GLKRKRNREDRISVDELldllGLDHLLNRYPAQ------LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 489997411 586 EFALYQLLRSELPD--CIVISVSHRPA-LERLHEN 617
Cdd:cd03297 167 RLQLLPELKQIKKNlnIPVIFVTHDLSeAEYLADR 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
443-595 |
9.13e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.36 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPG--------GENET-----MFLSQLPYVP-LGTLR 508
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLIrqeagMVFQQFYLFPhLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 509 DVVCYP----NSAAAIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTG 584
Cdd:PRK09493 97 NVMFGPlrvrGASKEEAEKQARELLAKVGLAERAHHYPSE------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170
....*....|.
gi 489997411 585 LEFALYQLLRS 595
Cdd:PRK09493 171 LRHEVLKVMQD 181
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
456-626 |
9.62e-15 |
|
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: 72.97 E-value: 9.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 456 LVITGRSGAGKTTLLRSLAelwpyasGTLHRPG--GEnetMFLSQLPyVPLGTLRDVVCY-PNSAAAIPDATLRDTLTKV 532
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALA-------GRRTGLGvsGE---VLINGRP-LDKRSFRKIIGYvPQDDILHPTLTVRETLMFA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 533 ALaplcdrldeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPD-CIVISVSHRPAL 611
Cdd:cd03213 107 AK-------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSS 173
|
170
....*....|....*.
gi 489997411 612 ERLHE-NQLELLGGGQ 626
Cdd:cd03213 174 EIFELfDKLLLLSQGR 189
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
446-582 |
1.02e-14 |
|
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: 73.33 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRldRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENET---------------------MF--LSQLPYV 502
Cdd:cd03262 21 LTVK--KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-IIDGLKLTddkkninelrqkvgmvfqqfnLFphLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 PLGtLRDVVCYPNSAAaipDATLRDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:cd03262 98 TLA-PIKVKGMSKAEA---EERALELLEKVGLA------DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
427-624 |
3.24e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.38 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPL---DVRLDRGGSLVITGRSGAGKTTLLRSLaelwpyasGTLHRP-GGE------------ 490
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGLDRPtSGEvlidgqdissls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 491 --------NETM-FLSQ----LPYVplgTLRDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSP 553
Cdd:COG1136 77 erelarlrRRHIgFVFQffnlLPEL---TALENVALPLLLAGVSRKERRerarELLERVGLGDRLDHRPSQ------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489997411 554 GEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPDCIVISVSHRPALERLHENQLELLGG 624
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
446-581 |
4.04e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 72.08 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENETMFLSQ------LPYVPLGtlRDVvcypnsaaa 519
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDITGLPPHeraragIGYVPEG--RRI--------- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 520 IPDATLRDTLTKVALAPLCDRLDEERDW---------------AKVLSPGEQQRVAFARILLTKPKAVFLDESTSAL 581
Cdd:cd03224 87 FPELTVEENLLLGAYARRRAKRKARLERvyelfprlkerrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
427-582 |
5.52e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.43 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVR--TPAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENET-------MFl 496
Cdd:COG1116 8 LELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGpgpdrgvVF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 sQ----LPYVplgTLRDVVCYPNSAAAIPDATLRDT----LTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTK 568
Cdd:COG1116 87 -QepalLPWL---TVLDNVALGLELRGVPKAERRERarelLELVGLA------GFEDAYPHQLSGGMRQRVAIARALAND 156
|
170
....*....|....
gi 489997411 569 PKAVFLDESTSALD 582
Cdd:COG1116 157 PEVLLMDEPFGALD 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
412-582 |
7.41e-14 |
|
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: 74.55 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 412 RALPAVLTRPSDDESVELNDI----EVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGT---- 483
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfd 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 484 ---LHRPGGENETMFLSQLPYV---------PLGTLRDVVCYP------NSAAAIPDATlRDTLTKVALAPLC-DRLDEE 544
Cdd:COG1123 326 gkdLTKLSRRSLRELRRRVQMVfqdpysslnPRMTVGDIIAEPlrlhglLSRAERRERV-AELLERVGLPPDLaDRYPHE 404
|
170 180 190
....*....|....*....|....*....|....*...
gi 489997411 545 rdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG1123 405 ------LSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
391-611 |
8.86e-14 |
|
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: 74.40 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 391 FASFRAAIIRLHGL---VDANEKGRALPavltRPSDDESVElnDIEVRTPAGDRLI-DPLDVRLDRGGSLVITGRSGAGK 466
Cdd:COG4618 298 FVSARQAYRRLNELlaaVPAEPERMPLP----RPKGRLSVE--NLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 467 TTLLRSLAELWPYASGTLhRPGGENetmfLSQLP---------YVP----L--GTLRD------------VVcypnsAAA 519
Cdd:COG4618 372 STLARLLVGVWPPTAGSV-RLDGAD----LSQWDreelgrhigYLPqdveLfdGTIAEniarfgdadpekVV-----AAA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 520 ----IPDATLR-----DTltkvalaplcdRLDEERdwaKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALY 590
Cdd:COG4618 442 klagVHEMILRlpdgyDT-----------RIGEGG---ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
250 260
....*....|....*....|...
gi 489997411 591 QLLRsELPD--CIVISVSHRPAL 611
Cdd:COG4618 508 AAIR-ALKArgATVVVITHRPSL 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
443-607 |
1.15e-13 |
|
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: 69.52 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENETMFLSQLPyvplgTLRDVVCYpnsaaAIPD 522
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-LIDGEDLTDLEDELP-----PLRRRIGM-----VFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 523 ATLRDTLT---KVALAplcdrldeerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS--EL 597
Cdd:cd03229 85 FALFPHLTvleNIALG---------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqAQ 149
|
170
....*....|
gi 489997411 598 PDCIVISVSH 607
Cdd:cd03229 150 LGITVVLVTH 159
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
432-609 |
1.25e-13 |
|
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: 70.21 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 432 IEVRTPAGDR----LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL---------HRPGGENETMFLSQ 498
Cdd:cd03231 1 LEADELTCERdgraLFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 499 LPYVPlGTLRDVVCYPNSAAAIPDATLRDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDEST 578
Cdd:cd03231 81 APGIK-TTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRP------VAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|..
gi 489997411 579 SALDTGLEFALYQLLRSELPD-CIVISVSHRP 609
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARgGMVVLTTHQD 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
434-638 |
2.08e-13 |
|
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: 70.16 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 434 VRTPAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH------RPGGENET----------MFL 496
Cdd:COG4181 18 VGTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlFALDEDARarlrarhvgfVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 S-QLpyvpLGTL--RDVVCYPNSAAAIPDATLR--DTLTKVALAplcDRLDEerdWAKVLSPGEQQRVAFARILLTKPKA 571
Cdd:COG4181 98 SfQL----LPTLtaLENVMLPLELAGRRDARARarALLERVGLG---HRLDH---YPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 572 VFLDESTSALD--TG-----LEFALYQLLRSELpdcivISVSHRPALERLHENQLELLGGgqwRLAPVEAAPAE 638
Cdd:COG4181 168 LFADEPTGNLDaaTGeqiidLLFELNRERGTTL-----VLVTHDPALAARCDRVLRLRAG---RLVEDTAATAA 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
439-583 |
2.15e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---RPGGENETMFLSQLPYvpLGtlrdvvcyp 514
Cdd:PRK13538 12 DERiLFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgEPIRRQRDEYHQDLLY--LG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 nSAAAI-PDATLRDTLTkvALAPLCDRLDEERDW---------------AKVLSPGEQQRVAFARILLTKPKAVFLDEST 578
Cdd:PRK13538 81 -HQPGIkTELTALENLR--FYQRLHGPGDDEALWealaqvglagfedvpVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....*
gi 489997411 579 SALDT 583
Cdd:PRK13538 158 TAIDK 162
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
426-585 |
2.47e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.67 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVR---TPAgdrlIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQLP-- 500
Cdd:COG3842 5 ALELENVSKRygdVTA----LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI-LLDGRD----VTGLPpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 -----YV-------PLGTLRDVVCYP-----NSAAAIpDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFAR 563
Cdd:COG3842 76 krnvgMVfqdyalfPHLTVAENVAFGlrmrgVPKAEI-RARVAELLELVGLEGLADRYPHQ------LSGGQQQRVALAR 148
|
170 180
....*....|....*....|..
gi 489997411 564 ILLTKPKAVFLDESTSALDTGL 585
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKL 170
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
427-593 |
2.70e-13 |
|
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: 69.42 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRL---IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGT-------LHRPGgeNETMFL 496
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvlvdgepVTGPG--PDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYV-PLGTLRDVVCYPNSAAAIPDATLRDT----LTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKA 571
Cdd:cd03293 79 FQQDALlPWLTVLDNVALGLELQGVPKAEARERaeelLELVGLS------GFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180
....*....|....*....|..
gi 489997411 572 VFLDESTSALDTGLEFALYQLL 593
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEEL 174
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
443-598 |
3.46e-13 |
|
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: 68.82 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---------RPGGENETMFLSQLPYVPLGTLRDVVCY 513
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQNYALYPHMTVYDNIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 514 PNSAAAIPDATLRDTLTKVA----LAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFAl 589
Cdd:cd03301 96 GLKLRKVPKDEIDERVREVAellqIEHLLDRK------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ- 168
|
....*....
gi 489997411 590 yqlLRSELP 598
Cdd:cd03301 169 ---MRAELK 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
415-625 |
5.58e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 415 PAVLTRPSDDES----VELNDIEVRtpAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPYaSGTLHRpg 488
Cdd:COG0488 300 TVEIRFPPPERLgkkvLELEGLSKS--YGDKtLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAgELEPD-SGTVKL-- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 489 GENETM-FLSQLpyvpLGTLRdvvcypnsaaaiPDATLRDTL-------TKVALAPLCDRL----DEERDWAKVLSPGEQ 556
Cdd:COG0488 375 GETVKIgYFDQH----QEELD------------PDKTVLDELrdgapggTEQEVRGYLGRFlfsgDDAFKPVGVLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 557 QRVAFARILLTKPKAVFLDESTSALD----TGLEFALyqllrSELPDCIVIsVSH-RPALERLHENQLELLGGG 625
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDietlEALEEAL-----DDFPGTVLL-VSHdRYFLDRVATRILEFEDGG 506
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
427-607 |
6.67e-13 |
|
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: 67.04 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVR---TPAgdrlIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPG---GENETMFLSQLP 500
Cdd:cd03230 1 IEVRNLSKRygkKTA----LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdiKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 YVPlgtlrdvvcypNSAAAIPDATLRDTLTkvalaplcdrldeerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSA 580
Cdd:cd03230 77 YLP-----------EEPSLYENLTVRENLK--------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180
....*....|....*....|....*....
gi 489997411 581 LDTGLEFALYQLLRsELPD--CIVISVSH 607
Cdd:cd03230 126 LDPESRREFWELLR-ELKKegKTILLSSH 153
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
427-582 |
6.81e-13 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 68.76 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPL-DVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYV- 502
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALkDVSLSvpKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 -PLG------------TLRDVVCYPNSAAAIPDATL----RDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARIL 565
Cdd:cd03258 82 rRIGmifqhfnllssrTVFENVALPLEIAGVPKAEIeervLELLELVGLE------DKADAYPAQLSGGQKQRVGIARAL 155
|
170
....*....|....*..
gi 489997411 566 LTKPKAVFLDESTSALD 582
Cdd:cd03258 156 ANNPKVLLCDEATSALD 172
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
439-585 |
8.97e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.03 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL-------------HRPGGeneTMFLSqlpYV--P 503
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkditnlpphKRPVN---TVFQN---YAlfP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 LGTLRDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEIKervaEALDLVQLEGYANRKPSQ------LSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
....*.
gi 489997411 580 ALDTGL 585
Cdd:cd03300 160 ALDLKL 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
441-607 |
1.01e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 441 RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQL---PYVPLGTLRDVVCYPNsa 517
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldTTLPLTVNRFLRLRPG-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 aaIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQL---LR 594
Cdd:PRK09544 96 --TKKEDILPALKRVQAGHLIDAPMQK------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLidqLR 167
|
170
....*....|...
gi 489997411 595 SELpDCIVISVSH 607
Cdd:PRK09544 168 REL-DCAVLMVSH 179
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
427-621 |
1.03e-12 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 67.66 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSL-AELWPYASgtLHRPGGEN-ETMFLSQLPY--- 501
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLyGALTPSRG--QVRIAGEDvNRLRGRQLPLlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 502 -----------VPLGTLRDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILL 566
Cdd:TIGR02673 80 rigvvfqdfrlLPDRTVYENVALPLEVRGKKEREIQrrvgAALRQVGLEHKADAFPEQ------LSGGEQQRVAIARAIV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 567 TKPKAVFLDESTSALDTGLEFALYQLL-RSELPDCIVISVSHRPAL-ERLHENQLEL 621
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLkRLNKRGTTVIVATHDLSLvDRVAHRVIIL 210
|
|
| PRK11098 |
PRK11098 |
peptide antibiotic transporter SbmA; |
96-388 |
1.04e-12 |
|
peptide antibiotic transporter SbmA;
Pssm-ID: 182960 Cd Length: 409 Bit Score: 70.41 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 96 YTALQKAFegiaSGDGTVKrsgVRGFWMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQDWLDGRAyyrdl 175
Cdd:PRK11098 119 YDLIQTAL----SSPGKVT---IGQFYSEVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMAHWQKLRH----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 176 fidetIDNPDQRIQQDVDIFTAgaggtpnapsngTASTLLFGAVQSIISVISFTAILWNLSG---TLNIFGvSIPRAMFW 252
Cdd:PRK11098 187 -----IEGAAQRVQEDTMRFAS------------TLENLGVSFINAIMTLIAFLPVLVTLSAhvpELPIVG-HIPYGLVI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 253 TVLVYVFVATVISFIIGRPLIWLSFRNEKLNAAFRYALVRLRDAAeavgfyrgERVEGTQLQRRFTPVIDNYRRYVRRSI 332
Cdd:PRK11098 249 AAIVWSLFGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDA--------DRATPPTVRELFSNVRKNYFRLYFHYM 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 333 AFNGWNLSVSQTIVPLPWVIQAPRLFAGQIDFGDVGQTATSFGNIHDSLSFFRNNY 388
Cdd:PRK11098 321 YFNIARILYLQVDNVFGLFLLFPSIVAGTITLGLMTQITNVFGQVRGSFQYLINSW 376
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
426-597 |
1.07e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 69.72 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVR---TPAgdrlIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENetmfLSQLP-- 500
Cdd:COG3839 3 SLELENVSKSyggVEA----LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRD----VTDLPpk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 ----------YV--PLGTLRDVVCYPNSAAAIPDATLRDTLTKVA----LAPLCDRLdeerdwAKVLSPGEQQRVAFARI 564
Cdd:COG3839 74 drniamvfqsYAlyPHMTVYENIAFPLKLRKVPKAEIDRRVREAAellgLEDLLDRK------PKQLSGGQRQRVALGRA 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 489997411 565 LLTKPKAVFLDESTSALDtglefalYQL---LRSEL 597
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD-------AKLrveMRAEI 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
426-626 |
1.29e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVRTP-AGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN----------ETM 494
Cdd:PRK11160 338 SLTLNNVSFTYPdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQPiadyseaalrQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 -FLSQLPYVPLGTLRDvvcypNSAAAIPDAT---LRDTLTKVALAPLCDRLDEERDW----AKVLSPGEQQRVAFARILL 566
Cdd:PRK11160 417 sVVSQRVHLFSATLRD-----NLLLAAPNASdeaLIEVLQQVGLEKLLEDDKGLNAWlgegGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489997411 567 TKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR-PALERLheNQLELLGGGQ 626
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRlTGLEQF--DRICVMDNGQ 550
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
443-607 |
1.36e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 67.78 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL----HRPGGENETM-----FLSQLPYVPLG-TLRDVV- 511
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgEDVARDPAEVrrrigYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 512 ----CYPNSAAAIpDATLRDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEF 587
Cdd:COG1131 96 ffarLYGLPRKEA-RERIDELLELFGLTDAADRK------VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180
....*....|....*....|...
gi 489997411 588 ALYQLLRsELPD---CIVISvSH 607
Cdd:COG1131 169 ELWELLR-ELAAegkTVLLS-TH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
427-611 |
1.37e-12 |
|
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: 70.32 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYA---SGTLHRPGGENETM-------- 494
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 -------FLSQLpyVPLgTLRDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFAR 563
Cdd:COG1123 85 igmvfqdPMTQL--NPV-TVGDQIAEALENLGLSRAEARarvlELLEAVGLERRLDRYPHQ------LSGGQRQRVAIAM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489997411 564 ILLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPDCIVISVSHRPAL 611
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGV 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
427-607 |
1.79e-12 |
|
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: 65.16 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENetmflsqLPYVPLgt 506
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-------IGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 lrdvvcypnsaaaipdatlrdtltkvalaplcdrldeerdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALD-TGL 585
Cdd:cd03221 71 --------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDlESI 106
|
170 180
....*....|....*....|..
gi 489997411 586 EfALYQLLRSElpDCIVISVSH 607
Cdd:cd03221 107 E-ALEEALKEY--PGTVILVSH 125
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
439-607 |
2.98e-12 |
|
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: 66.59 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmfLSQLPyvPlgTLRDVVCYPNSAA 518
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKD-----ITNLP--P--EKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 519 AIPDATLRDTLT---KVALAPLCDRLDEERDWAKV-------------LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:cd03299 82 LFPHMTVYKNIAyglKKRKVDKKEIERKVLEIAEMlgidhllnrkpetLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180
....*....|....*....|....*..
gi 489997411 583 TGLEFALYQLLRS--ELPDCIVISVSH 607
Cdd:cd03299 162 VRTKEKLREELKKirKEFGVTVLHVTH 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
447-614 |
5.18e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLP-------------YV---PLGTLR 508
Cdd:PRK11701 24 DVSFDlyPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewgFVhqhPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 509 DVVcypnSAAA-IPD----------ATLRDT----LTKVALAPlcDRLDeerDWAKVLSPGEQQRVAFARILLTKPKAVF 573
Cdd:PRK11701 104 MQV----SAGGnIGErlmavgarhyGDIRATagdwLERVEIDA--ARID---DLPTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489997411 574 LDESTSALDTGLEFALYQLLR---SELpDCIVISVSHRPALERL 614
Cdd:PRK11701 175 MDEPTGGLDVSVQARLLDLLRglvREL-GLAVVIVTHDLAVARL 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
427-608 |
5.50e-12 |
|
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: 66.10 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVR-TPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGE----------NETMF 495
Cdd:cd03251 1 VEFKNVTFRyPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlaslrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 LSQLPYVPLGTLRDvvcypNSAAAIPDATLRDTL--TKVALA-PLCDRLDEERDwAKV------LSPGEQQRVAFARILL 566
Cdd:cd03251 81 VSQDVFLFNDTVAE-----NIAYGRPGATREEVEeaARAANAhEFIMELPEGYD-TVIgergvkLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489997411 567 TKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHR 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
443-582 |
6.17e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.79 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDpLDVRldRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENETMFLSQLPYV--------------PLGTLR 508
Cdd:COG1126 20 IS-LDVE--KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLTDSKKDINKLrrkvgmvfqqfnlfPHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 509 DVVCYP-------NSAAAIPDAtlRDTLTKVALAplcDRLDEerdWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSAL 581
Cdd:COG1126 96 ENVTLApikvkkmSKAEAEERA--MELLERVGLA---DKADA---YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
.
gi 489997411 582 D 582
Cdd:COG1126 168 D 168
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
437-608 |
8.00e-12 |
|
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: 65.59 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 437 PAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL----HRPGGENETMFLSQLPYVPL------GT 506
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdgHDLALADPAWLRRQVGVVLQenvlfnRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDvvcypNSAAAIPDATLRDTLTKVALAPLCDRLDEERDWAKV--------LSPGEQQRVAFARILLTKPKAVFLDEST 578
Cdd:cd03252 92 IRD-----NIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190
....*....|....*....|....*....|
gi 489997411 579 SALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHR 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
427-607 |
8.39e-12 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 65.22 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTpaGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENETMfLSQLPYVPLG 505
Cdd:cd03261 1 IELRGLTKSF--GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-LIDGEDISG-LSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 ----------------TLRDVVCYP-NSAAAIPDATLRD----TLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARI 564
Cdd:cd03261 77 rrmgmlfqsgalfdslTVFENVAFPlREHTRLSEEEIREivleKLEAVGLRGAEDLYPAE------LSGGMKKRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489997411 565 LLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPDCIVISVSH 607
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTH 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
447-582 |
9.65e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH----------RPGG-------ENETMFLSQLPYVP-LGT 506
Cdd:PRK11124 20 DITLDcpQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfskTPSDkairelrRNVGMVFQQYNLWPhLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYP------NSAAAIPDAtlRDTLTKVALAPLCDRldeerdWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSA 580
Cdd:PRK11124 100 QQNLIEAPcrvlglSKDQALARA--EKLLERLRLKPYADR------FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
..
gi 489997411 581 LD 582
Cdd:PRK11124 172 LD 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
439-585 |
1.08e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---------RPGGENETM---FLSQLPYV---- 502
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtaRSLSQQKGLirqLRQHVGFVfqnf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 ---PLGT-LRDVVCYPNSAAAIP----DATLRDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFL 574
Cdd:PRK11264 95 nlfPHRTvLENIIEGPVIVKGEPkeeaTARARELLAKVGLA------GKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170
....*....|.
gi 489997411 575 DESTSALDTGL 585
Cdd:PRK11264 169 DEPTSALDPEL 179
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
427-607 |
1.22e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.52 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGdRLIDPLDVRLDRGgSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPG---GENETMFLSQLPYVP 503
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 lgtlRDVVCYPN---------SAAA--IPD----ATLRDTLTKVALAplcDRLDEErdwAKVLSPGEQQRVAFARILLTK 568
Cdd:cd03264 79 ----QEFGVYPNftvrefldyIAWLkgIPSkevkARVDEVLELVNLG---DRAKKK---IGSLSGGMRRRVGIAQALVGD 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 489997411 569 PKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSH 607
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
452-610 |
1.68e-11 |
|
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: 64.55 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 452 RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQL----------PYVPLGTLRDVVCYPNSAAaiP 521
Cdd:cd03254 28 PGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrsmigvvlqdTFLFSGTIMENIRLGRPNA--T 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 522 DATLRDTLTKVALAPLCDRL----DEE-RDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSE 596
Cdd:cd03254 106 DEEVIEAAKEAGAHDFIMKLpngyDTVlGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL 185
|
170
....*....|....
gi 489997411 597 LPDCIVISVSHRPA 610
Cdd:cd03254 186 MKGRTSIIIAHRLS 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
446-614 |
2.10e-11 |
|
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: 65.89 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEneTMFLSQ----LP-------YVP--------- 503
Cdd:COG4148 16 LDVDFTlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGE--VLQDSArgifLPphrrrigYVFqearlfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 --LGTLRDVvcYPNSAAAIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSAL 581
Cdd:COG4148 93 svRGNLLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPAT------LSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 489997411 582 DTGLEFALYQLLRS-----ELPdciVISVSHRPA-LERL 614
Cdd:COG4148 165 DLARKAEILPYLERlrdelDIP---ILYVSHSLDeVARL 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
446-576 |
2.69e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 63.85 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQLP----------YVPLGtlRDVvcYPN 515
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI-RFDGED----ITGLPphriarlgigYVPEG--RRI--FPS 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489997411 516 ---------SAAAIPD-ATLRDTLTKV-ALAPlcdRLDEERD-WAKVLSPGEQQRVAFARILLTKPKAVFLDE 576
Cdd:COG0410 93 ltveenlllGAYARRDrAEVRADLERVyELFP---RLKERRRqRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
428-582 |
2.77e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.50 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDR---LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHR-------PGGENETMF-- 495
Cdd:COG4525 5 TVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgPGADRGVVFqk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 ------LSQLPYVPLG-TLRDVvcypnsAAAIPDATLRDTLTKVALAPLCDRldeeRDWAkvLSPGEQQRVAFARILLTK 568
Cdd:COG4525 85 dallpwLNVLDNVAFGlRLRGV------PKAERRARAEELLALVGLADFARR----RIWQ--LSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 489997411 569 PKAVFLDESTSALD 582
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
427-611 |
3.08e-11 |
|
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: 63.51 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGEN--------------- 491
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKDitkknlrelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 492 -----ETMFLSQlpyvplgTLRDVVCY-P-N---SAAAIpDATLRDTLTKVALAPLcdrldEERDWAKvLSPGEQQRVAF 561
Cdd:COG1122 80 vfqnpDDQLFAP-------TVEEDVAFgPeNlglPREEI-RERVEEALELVGLEHL-----ADRPPHE-LSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489997411 562 ARILLTKPKAVFLDESTSALD-TGLEfALYQLLRsELPD--CIVISVSHRPAL 611
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDpRGRR-ELLELLK-RLNKegKTVIIVTHDLDL 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
441-609 |
3.24e-11 |
|
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: 63.44 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 441 RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLaelwpyaSGTLHRPGGENETMFLSQLPYVPlGTLRDVVCY-PNSAAA 519
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGTTSGQILFNGQPRKP-DQFQKCVAYvRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 520 IPDATLRDTLTKVALAPLCDRLDEERDWAKV--------------------LSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVedvllrdlaltriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|..
gi 489997411 580 ALDTGLEFALYQLLRsELP--DCIVISVSHRP 609
Cdd:cd03234 173 GLDSFTALNLVSTLS-QLArrNRIVILTIHQP 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
255-608 |
3.35e-11 |
|
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: 66.89 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 255 LVYVFVATVISFIIGRPLIWLSFRNEKLNAAFRYALVRLRDAAEA-VGFYRGERVEGTQL------QRRF-----TPVID 322
Cdd:TIGR00957 1097 LIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSpVYSHFNETLLGVSVirafeeQERFihqsdLKVDE 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 323 NYRRYVRrSIAFNGWnLSVSqtivpLPWVIQAPRLFAGQidFGDVGQTATSFGNIHDSLSF-----FRNNY--DAFASFR 395
Cdd:TIGR00957 1177 NQKAYYP-SIVANRW-LAVR-----LECVGNCIVLFAAL--FAVISRHSLSAGLVGLSVSYslqvtFYLNWlvRMSSEME 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 396 AAIIRLHGLVDANEKGRALPAVL--TRPSDD----ESVELNDIEVR-TPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTT 468
Cdd:TIGR00957 1248 TNIVAVERLKEYSETEKEAPWQIqeTAPPSGwpprGRVEFRNYCLRyREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 469 LLRSLAELWPYASGTLHRPG------GENETMF-LSQLPYVPL---GTLRdVVCYPNSAAAIPDA--TLRDTLTKVALAP 536
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIDGlniakiGLHDLRFkITIIPQDPVlfsGSLR-MNLDPFSQYSDEEVwwALELAHLKTFVSA 1406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489997411 537 LCDRLDEE-RDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:TIGR00957 1407 LPDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHR 1479
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
450-582 |
3.74e-11 |
|
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: 63.22 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 450 LDRGGSLVITGRSGAGKTTLLRSLaelwpYA-----SGT--LHRPGGE---------------NETM-----FLSQLPYV 502
Cdd:COG4778 34 VAAGECVALTGPSGAGKSTLLKCI-----YGnylpdSGSilVRHDGGWvdlaqaspreilalrRRTIgyvsqFLRVIPRV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 PlgTLrDVVCYPNSAAAIPDATLRDTltkvALApLCDRLD-EERDWAkvLSP-----GEQQRVAFARILLTKPKAVFLDE 576
Cdd:COG4778 109 S--AL-DVVAEPLLERGVDREEARAR----ARE-LLARLNlPERLWD--LPPatfsgGEQQRVNIARGFIADPPLLLLDE 178
|
....*.
gi 489997411 577 STSALD 582
Cdd:COG4778 179 PTASLD 184
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
429-602 |
4.06e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 429 LNDIEVRTPAGDrlidpldvrldrggSLVITGRSGAGKTTLLRSLAELWPYASGT-------LHRPGGENETMFL-SQLp 500
Cdd:PRK11247 28 LNQLDLHIPAGQ--------------FVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtapLAEAREDTRLMFQdARL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 yVPLGTLRDVVCYPNSAAAIPDAtlRDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSA 580
Cdd:PRK11247 93 -LPWKKVIDNVGLGLKGQWRDAA--LQALAAVGLA------DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180
....*....|....*....|..
gi 489997411 581 LDTglefalyqLLRSELPDCIV 602
Cdd:PRK11247 164 LDA--------LTRIEMQDLIE 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
458-626 |
4.15e-11 |
|
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: 63.26 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTL---HRPGGENETMFL-------SQLPYVPLGTLRDvvcypNSAAAIPDATLrD 527
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQGGQVlldGKPISQYEHKYLhskvslvGQEPVLFARSLQD-----NIAYGLQSCSF-E 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 528 TLTKVA--------LAPLCDRLDEERDWA-KVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELP 598
Cdd:cd03248 119 CVKEAAqkahahsfISELASGYDTEVGEKgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE 198
|
170 180
....*....|....*....|....*....
gi 489997411 599 DCIVISVSHR-PALERLHenQLELLGGGQ 626
Cdd:cd03248 199 RRTVLVIAHRlSTVERAD--QILVLDGGR 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
426-594 |
8.34e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.01 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVRTPaGDRLIDplDVRLD-RGGSLV-ITGRSGAGKTTLLRSLAEL-WPYaSGTL---------HRPGGENET 493
Cdd:COG1118 2 SIEVRNISKRFG-SFTLLD--DVSLEiASGELVaLLGPSGSGKTTLLRIIAGLeTPD-SGRIvlngrdlftNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 494 MFLSQ----LPYVplgTLRDVVCY-----PNSAAAIpDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARI 564
Cdd:COG1118 78 GFVFQhyalFPHM---TVAENIAFglrvrPPSKAEI-RARVEELLELVQLEGLADRYPSQ------LSGGQRQRVALARA 147
|
170 180 190
....*....|....*....|....*....|
gi 489997411 565 LLTKPKAVFLDESTSALDTGLEFALYQLLR 594
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLR 177
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
427-582 |
8.86e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.99 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSL-AELWPYaSGTLhRPGGENetmfLSQLPY--VP 503
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPT-SGQV-LVNGQD----LSRLKRreIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 LgtLR-------------------DVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVA 560
Cdd:COG2884 76 Y--LRrrigvvfqdfrllpdrtvyENVALPLRVTGKSRKEIRrrvrEVLDLVGLSDKAKALPHE------LSGGEQQRVA 147
|
170 180
....*....|....*....|..
gi 489997411 561 FARILLTKPKAVFLDESTSALD 582
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLD 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
443-597 |
9.28e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL-------------HRPggeNETMFLSqlpYV--PLGTL 507
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaeNRH---VNTVFQS---YAlfPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDt 583
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEITprvmEALRMVQLEEFAQRKPHQ------LSGGQQQRVAIARAVVNKPKVLLLDESLSALD- 176
|
170
....*....|....
gi 489997411 584 gleFALYQLLRSEL 597
Cdd:PRK09452 177 ---YKLRKQMQNEL 187
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
427-608 |
9.65e-11 |
|
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: 62.17 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPA--GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM----FLSQLP 500
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnlrwLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 YVP------LGTLRDVVCYpnsaaAIPDATL--RDTLTKVALA-----PLCDRLDEE-RDWAKVLSPGEQQRVAFARILL 566
Cdd:cd03249 81 LVSqepvlfDGTIAENIRY-----GKPDATDeeVEEAAKKANIhdfimSLPDGYDTLvGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489997411 567 TKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHR 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
428-582 |
9.68e-11 |
|
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: 62.20 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENET-------------- 493
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalrqlrrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 494 MFLSQLPYVP-LGTLRDVVC-------------YPNSAAAIPDAtlRDTLTKVALAPLC-DRLDEerdwakvLSPGEQQR 558
Cdd:cd03256 82 MIFQQFNLIErLSVLENVLSgrlgrrstwrslfGLFPKEEKQRA--LAALERVGLLDKAyQRADQ-------LSGGQQQR 152
|
170 180
....*....|....*....|....
gi 489997411 559 VAFARILLTKPKAVFLDESTSALD 582
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLD 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
422-585 |
9.86e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 422 SDDESVELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHrPGGENET-------- 493
Cdd:PRK11432 2 TQKNFVVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-IDGEDVThrsiqqrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 494 ---MFLSQ--LPYVPLGtlrDVVCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARI 564
Cdd:PRK11432 80 icmVFQSYalFPHMSLG---ENVGYGLKMLGVPKEERKqrvkEALELVDLAGFEDRYVDQ------ISGGQQQRVALARA 150
|
170 180
....*....|....*....|.
gi 489997411 565 LLTKPKAVFLDESTSALDTGL 585
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANL 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
447-609 |
1.74e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.31 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENetmFLSQLPYV-PLGTL---------RDVvcYPNS 516
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQD---LTALPPAErPVSMLfqennlfphLTV--AQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 517 AAAI-PD--------ATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEF 587
Cdd:COG3840 93 GLGLrPGlkltaeqrAQVEQALERVGLAGLLDRLPGQ------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180
....*....|....*....|....*
gi 489997411 588 ALYQLLRsELPD---CIVISVSHRP 609
Cdd:COG3840 167 EMLDLVD-ELCRergLTVLMVTHDP 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
438-582 |
1.77e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 438 AGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHR-------PGGENETMFLSQ--LPYvplgtlR 508
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegPGAERGVVFQNEglLPW------R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 509 DV---VCYPNSAAAIP----DATLRDTLTKVALAplcdRLDEERDWAkvLSPGEQQRVAFARILLTKPKAVFLDESTSAL 581
Cdd:PRK11248 86 NVqdnVAFGLQLAGVEkmqrLEIAHQMLKKVGLE----GAEKRYIWQ--LSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
.
gi 489997411 582 D 582
Cdd:PRK11248 160 D 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
429-582 |
1.88e-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: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 429 LNDIEVRtpAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGenETM-FLSQ-LPYVPLG 505
Cdd:COG0488 1 LENLSKS--FGGRpLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--LRIgYLPQePPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 TLRDVVCYPNSAAAIPDATLRDTLTKVA--------LAPLCDRLDEERDWA-----------------------KVLSPG 554
Cdd:COG0488 77 TVLDTVLDGDAELRALEAELEELEAKLAepdedlerLAELQEEFEALGGWEaearaeeilsglgfpeedldrpvSELSGG 156
|
170 180
....*....|....*....|....*...
gi 489997411 555 EQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
445-582 |
3.02e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 445 PLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENET-------MFLSQLPYVP--LGTLRDVVCYPN 515
Cdd:PRK13543 29 PLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgdrsrfmAYLGHLPGLKadLSTLENLHFLCG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 516 SAAAIPDATLRDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK13543 109 LHGRRAKQMPGSALAIVGLA------GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
447-623 |
3.24e-10 |
|
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: 60.82 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLD-RGGSLV-ITGRSGAGKTTLLRSLAELWPYASGTL--------HRPGGENETMFLSQ-LPYVPLGTLRDVVCY-- 513
Cdd:cd03296 20 DVSLDiPSGELVaLLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERNVGFVFQhYALFRHMTVFDNVAFgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 514 -------PNSAAAIpDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLE 586
Cdd:cd03296 100 rvkprseRPPEAEI-RAKVHELLKLVQLDWLADRYPAQ------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489997411 587 FALYQLLRsELPDCIVIS---VSH--RPALER------LHENQLELLG 623
Cdd:cd03296 173 KELRRWLR-RLHDELHVTtvfVTHdqEEALEVadrvvvMNKGRIEQVG 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
447-593 |
3.51e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYVPLGTLRDVVCYPNSAAAI-----P 521
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIglglnP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 522 D--------ATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLL 593
Cdd:PRK10771 99 GlklnaaqrEKLHAIARQMGIEDLLARLPGQ------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
421-607 |
4.14e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 421 PSDDESVELNDIEVRTPaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL---HRP-GGENETMFL 496
Cdd:PRK10575 6 NHSDTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPlESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYVPLG-------TLRDVVC---YPNSAA-----AIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAF 561
Cdd:PRK10575 85 RKVAYLPQQlpaaegmTVRELVAigrYPWHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDS------LSGGERQRAWI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489997411 562 ARILLTKPKAVFLDESTSALDTGLE---FALYQLLrSELPDCIVISVSH 607
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRL-SQERGLTVIAVLH 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
428-582 |
4.85e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTpAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM----------FLS 497
Cdd:PRK10247 9 QLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiyrqqvsYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 498 QLPYVPLGTLRDVVCYP---NSAAAIPDATLRDtLTKVALAP--LCDRLDEerdwakvLSPGEQQRVAFARILLTKPKAV 572
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDD-LERFALPDtiLTKNIAE-------LSGGEKQRISLIRNLQFMPKVL 159
|
170
....*....|
gi 489997411 573 FLDESTSALD 582
Cdd:PRK10247 160 LLDEITSALD 169
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
446-582 |
9.42e-10 |
|
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: 59.96 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRldRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYV---------------PLGTLRDV 510
Cdd:cd03294 45 LDVR--EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkismvfqsfallPHRTVLEN 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 511 VCYPNSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:cd03294 123 VAFGLEVQGVPRAEREeraaEALELVGLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
460-582 |
1.00e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSL---AELWP---------YASGTLHRPggENET--------MFLSQLPYVPLGTLRDVVcYPNSAAA 519
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtitgsivYNGHNIYSP--RTDTvdlrkeigMVFQQPNPFPMSIYENVV-YGLRLKG 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 520 IPDATLRDTLTKVAL--APLCDRL-DEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK14239 115 IKDKQVLDEAVEKSLkgASIWDEVkDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
439-593 |
1.83e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.35 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYV--PLGT-------LRD 509
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMifqdhhlLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 510 VVCYPNSAAA--IPDATLRDTLTKVALAplCDR---LDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTG 584
Cdd:PRK10908 94 RTVYDNVAIPliIAGASGDDIRRRVSAA--LDKvglLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
....*....
gi 489997411 585 LEFALYQLL 593
Cdd:PRK10908 172 LSEGILRLF 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
446-611 |
2.27e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPYaSGTLHRPGGeneTMFLSQLPYVPLGTLRDVVCYpnsAAAIPDAT 524
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLgELEKL-SGSVSVPGS---IAYVSQEPWIQNGTIRENILF---GKPFDEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 525 LRDTLTKVALAPLCDRLdEERDWAKV------LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQ-LLRSEL 597
Cdd:cd03250 97 YEKVIKACALEPDLEIL-PDGDLTEIgekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLL 175
|
170
....*....|....*
gi 489997411 598 PDC-IVISVSHRPAL 611
Cdd:cd03250 176 LNNkTRILVTHQLQL 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
404-582 |
3.94e-09 |
|
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: 59.31 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 404 LVDANEKGRALPAvltRPSDDESVELNDIEV----------RTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSL 473
Cdd:COG4172 256 LLAAEPRGDPRPV---PPDAPPLLEARDLKVwfpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 474 AELWPyASGTL----HRPGGENETMFLS---------QLPY--------V------PLGTLRDvvcyPNSAAAIpDATLR 526
Cdd:COG4172 333 LRLIP-SEGEIrfdgQDLDGLSRRALRPlrrrmqvvfQDPFgslsprmtVgqiiaeGLRVHGP----GLSAAER-RARVA 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 527 DTLTKVALAPLC-DRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG4172 407 EALEEVGLDPAArHRYPHE------FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
427-582 |
3.94e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEvrtpagDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELwpyasgtlhrpggenetmfLSQLPYVPLGT 506
Cdd:COG2401 36 VELRVVE------RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------------------LKGTPVAGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPNsaAAIPDATLR--DTLTKVAL--------APLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDE 576
Cdd:COG2401 91 VPDNQFGRE--ASLIDAIGRkgDFKDAVELlnavglsdAVLWLRRFKE------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
....*.
gi 489997411 577 STSALD 582
Cdd:COG2401 163 FCSHLD 168
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
422-607 |
5.74e-09 |
|
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: 56.91 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 422 SDDESVELNDieVRTPAGDRLI-DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGEN-ETMFLSQL 499
Cdd:COG1127 1 MSEPMIEVRN--LTKSFGDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI-LVDGQDiTGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PYVPLG--------------TLRDVVCYP---NSaaAIPDATLRD----TLTKVALAPLCDRLDEErdwakvLSPGEQQR 558
Cdd:COG1127 78 YELRRRigmlfqggalfdslTVFENVAFPlreHT--DLSEAEIRElvleKLELVGLPGAADKMPSE------LSGGMRKR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489997411 559 VAFARILLTKPKAVFLDESTSALD--TGLEFAlyQL---LRSELpDCIVISVSH 607
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpiTSAVID--ELireLRDEL-GLTSVVVTH 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
458-609 |
6.75e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTLHRPGG-----------------ENETMFLSQLPYVPLGTLRDVVCYPNSAAAI 520
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqidaiklrKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 521 PDA-----TLRDTLTKVAL-APLCDRLDEErdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLR 594
Cdd:PRK14246 121 KEKreikkIVEECLRKVGLwKEVYDRLNSP---ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170
....*....|....*
gi 489997411 595 SELPDCIVISVSHRP 609
Cdd:PRK14246 198 ELKNEIAIVIVSHNP 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
404-595 |
8.66e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 404 LVDANEKGRALPAvltrPSDDESV-ELNDIEV----------RTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTT---- 468
Cdd:PRK15134 256 LLNSEPSGDPVPL----PEPASPLlDVEQLQVafpirkgilkRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtgla 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 469 ---LLRSLAELWpYASGTLHRPGGENETMFLSQL------PYVPLGTLRDV---------VCYPNSAAAIPDATLRDTLT 530
Cdd:PRK15134 332 llrLINSQGEIW-FDGQPLHNLNRRQLLPVRHRIqvvfqdPNSSLNPRLNVlqiieeglrVHQPTLSAAQREQQVIAVME 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489997411 531 KVALAPlcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS 595
Cdd:PRK15134 411 EVGLDP-----ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
427-582 |
1.12e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.12 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLI---DPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHrPGGENetmfLSQLPYVP 503
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-VDGQD----LTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 504 LGTLR-------------------DVVCYPNSAAAIPDATLRdtlTKVAlaPLCDR--LDEERD-WAKVLSPGEQQRVAF 561
Cdd:PRK11153 77 LRKARrqigmifqhfnllssrtvfDNVALPLELAGTPKAEIK---ARVT--ELLELvgLSDKADrYPAQLSGGQKQRVAI 151
|
170 180
....*....|....*....|.
gi 489997411 562 ARILLTKPKAVFLDESTSALD 582
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALD 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
443-614 |
1.76e-08 |
|
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: 54.98 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYVP-----------------LG 505
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPeerglypkmkvidqlvyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 506 TLRDVvcyPNSAAAipdATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTG- 584
Cdd:cd03269 96 QLKGL---KKEEAR---RRIDEWLERLELSEYANKRVEE------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVn 163
|
170 180 190
....*....|....*....|....*....|....
gi 489997411 585 ---LEFALYQLLRSELPdciVISVSHRPAL-ERL 614
Cdd:cd03269 164 velLKDVIRELARAGKT---VILSTHQMELvEEL 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
447-594 |
2.53e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 447 DVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTL----------------------------HRPGGENETMFL 496
Cdd:PRK10851 20 DISLDipSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrlhardrkvgfvfqhyalfrHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYvplgtlRDvvcYPNSAAAipDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDE 576
Cdd:PRK10851 100 TVLPR------RE---RPNAAAI--KAKVTQLLEMVQLAHLADRYPAQ------LSGGQKQRVALARALAVEPQILLLDE 162
|
170
....*....|....*...
gi 489997411 577 STSALDTGLEFALYQLLR 594
Cdd:PRK10851 163 PFGALDAQVRKELRRWLR 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
439-585 |
3.11e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.00 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmfLSQLPyvPLgtLRDVVCYPNSAA 518
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-----LSHVP--PY--QRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 519 AIPDATLRDTLT------KVALAPLCDRLDEE------RDWAK----VLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK11607 102 LFPHMTVEQNIAfglkqdKLPKAEIASRVNEMlglvhmQEFAKrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
...
gi 489997411 583 TGL 585
Cdd:PRK11607 182 KKL 184
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
428-626 |
3.27e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVrtpaGDRLiDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYaSGTLH---RPggenetmfLSQLPYVPL 504
Cdd:COG4138 2 QLNDVAV----AGRL-GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILlngRP--------LSDWSAAEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 505 GTLRDVVCYPNSA-AAIP---------DATLRDTLTKVALAPLCDRLDEE----RDWAKvLSPGEQQRVAFARILLT--- 567
Cdd:COG4138 68 ARHRAYLSQQQSPpFAMPvfqylalhqPAGASSEAVEQLLAQLAEALGLEdklsRPLTQ-LSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489997411 568 ----KPKAVFLDESTSALDTGLEFALYQLLR--SELPDCIVISvSHRPALERLHENQLELLGGGQ 626
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLDVAQQAALDRLLRelCQQGITVVMS-SHDLNHTLRHADRVWLLKQGK 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-593 |
4.83e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 437 PAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPyASGTLHRPGGENETMFlSQ-------LPYVPLgtLR 508
Cdd:PLN03073 519 PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISgELQP-SSGTVFRSAKVRMAVF-SQhhvdgldLSSNPL--LY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 509 DVVCYPnsaaAIPDATLRDTLT------KVALAPLcdrldeerdwaKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PLN03073 595 MMRCFP----GVPEQKLRAHLGsfgvtgNLALQPM-----------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170
....*....|.
gi 489997411 583 TGLEFALYQLL 593
Cdd:PLN03073 660 LDAVEALIQGL 670
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
452-630 |
4.88e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 452 RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmfLSQLPYVPLGTLR--DVVCYPNSAAAIPdaTLrDTL 529
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-----LHQMDEEARAKLRakHVGFVFQSFMLIP--TL-NAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 530 TKVALAPLC--DRLDEERDWAKVL-----------------SPGEQQRVAFARILLTKPKAVFLDESTSALD--TGLEFA 588
Cdd:PRK10584 107 ENVELPALLrgESSRQSRNGAKALleqlglgkrldhlpaqlSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489997411 589 --LYQLLRSElpDCIVISVSHRPALERLHENQLELLGGGQWRLA 630
Cdd:PRK10584 187 dlLFSLNREH--GTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
443-607 |
5.02e-08 |
|
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: 54.01 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH-------RPGGENETMF--LSQLPYVplgTLRDvvcy 513
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqitEPGPDRMVVFqnYSLLPWL---TVRE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 514 pNSAAAI----PD-------ATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:TIGR01184 74 -NIALAVdrvlPDlskserrAIVEEHIALVGLTEAADKRPGQ------LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190
....*....|....*....|....*....|....*
gi 489997411 583 TglefalyqLLRSELPD----------CIVISVSH 607
Cdd:TIGR01184 147 A--------LTRGNLQEelmqiweehrVTVLMVTH 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
460-607 |
5.43e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSL---AELWPYA--SGTLH------------------RPGgenetM-FlsQLPyVPL-GTLRDVVCYP 514
Cdd:COG1117 44 GPSGCGKSTLLRCLnrmNDLIPGArvEGEILldgediydpdvdvvelrrRVG-----MvF--QKP-NPFpKSIYDNVAYG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 ------NSAAAIpDATLRDTLTKVALAP-LCDRLDEErdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD---TG 584
Cdd:COG1117 116 lrlhgiKSKSEL-DEIVEESLRKAALWDeVKDRLKKS---ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTA 191
|
170 180
....*....|....*....|....
gi 489997411 585 -LEfALYQLLRSELpdCIVIsVSH 607
Cdd:COG1117 192 kIE-ELILELKKDY--TIVI-VTH 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
446-609 |
5.62e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 53.65 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 446 LDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPY------------------VPLGTL 507
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVsmlfqennlfahltveqnVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYPNSAAAIPDAtlrdtLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEF 587
Cdd:cd03298 97 PGLKLTAEDRQAIEVA-----LARVGLAGLEKRLPGE------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180
....*....|....*....|....*
gi 489997411 588 ALYQL---LRSElPDCIVISVSHRP 609
Cdd:cd03298 166 EMLDLvldLHAE-TKMTVLMVTHQP 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
440-607 |
6.03e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 440 DRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRpGGENETM-----------FLSQLPYVPLG-TL 507
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-GDKPISMlssrqlarrlaLLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYPNSaaaiPDATLRDTLT------------KVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLD 575
Cdd:PRK11231 94 RELVAYGRS----PWLSLWGRLSaednarvnqameQTRINHLADRRLTD------LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190
....*....|....*....|....*....|....
gi 489997411 576 ESTSALDTGLEFALYQLLRsELPDC--IVISVSH 607
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMR-ELNTQgkTVVTVLH 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
427-607 |
6.15e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRL-IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL---HRPGGEnETMF------- 495
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvgGMVLSE-ETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 -LSQLP---YVPlGTLRDVVCYPNSAAAIPdatlRDTLTK-----VALAPLCDRLDEErdwAKVLSPGEQQRVAFARILL 566
Cdd:PRK13635 85 mVFQNPdnqFVG-ATVQDDVAFGLENIGVP----REEMVErvdqaLRQVGMEDFLNRE---PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489997411 567 TKPKAVFLDESTSALD-TGLEFAL--YQLLRSELpDCIVISVSH 607
Cdd:PRK13635 157 LQPDIIILDEATSMLDpRGRREVLetVRQLKEQK-GITVLSITH 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
427-582 |
6.83e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.23 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVrTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPyvplgt 506
Cdd:PRK09536 4 IDVSDLSV-EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 lRDVVCYPNSAAAIPDATLRDT--------LTKVALAPLCDRLDEERDWAKV------------LSPGEQQRVAFARILL 566
Cdd:PRK09536 77 -RRVASVPQDTSLSFEFDVRQVvemgrtphRSRFDTWTETDRAAVERAMERTgvaqfadrpvtsLSGGERQRVLLARALA 155
|
170
....*....|....*.
gi 489997411 567 TKPKAVFLDESTSALD 582
Cdd:PRK09536 156 QATPVLLLDEPTASLD 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
429-582 |
6.94e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 429 LNDIEVRTPAGDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGtlhrpggenETMFLSQLPYVPLGTL 507
Cdd:PRK13540 2 LDVIELDFDYHDQpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG---------EILFERQSIKKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYPNSAAAI-PDATLRD--------TLTKVALAPLCD--RLDEERDW-AKVLSPGEQQRVAFARILLTKPKAVFLD 575
Cdd:PRK13540 73 QKQLCFVGHRSGInPYLTLREnclydihfSPGAVGITELCRlfSLEHLIDYpCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
....*..
gi 489997411 576 ESTSALD 582
Cdd:PRK13540 153 EPLVALD 159
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
443-595 |
7.89e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGE-------------NETMFLSQLPYVPLG---T 506
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgmkddewravrSDIQMIFQDPLASLNprmT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVC------YPNSAAAIPDATLRDTLTKVALAP-LCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:PRK15079 117 IGEIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHE------FSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170
....*....|....*.
gi 489997411 580 ALDTGLEFALYQLLRS 595
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQ 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
460-608 |
9.76e-08 |
|
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: 53.14 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSLAelwpyasgTLHRPGGENETMFLSQLPYVPLGTLRDVVCYPNSAAAIPDATLRDTLT--------- 530
Cdd:cd03266 38 GPNGAGKTTTLRMLA--------GLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEyfaglyglk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 531 ----KVALAPLCDRLD-----EERdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPD 599
Cdd:cd03266 110 gdelTARLEELADRLGmeellDRR--VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlrALGK 187
|
....*....
gi 489997411 600 CIVISvSHR 608
Cdd:cd03266 188 CILFS-THI 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
458-608 |
1.02e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTL-------HRPGGENETMFLSQLPYVPL---GTLR---DVVCYPNsaaaipDAT 524
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRImiddcdvAKFGLTDLRRVLSIIPQSPVlfsGTVRfniDPFSEHN------DAD 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 525 LRDTLTKVALAPLCDR----LDEE-RDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPD 599
Cdd:PLN03232 1341 LWEALERAHIKDVIDRnpfgLDAEvSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
....*....
gi 489997411 600 CIVISVSHR 608
Cdd:PLN03232 1421 CTMLVIAHR 1429
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
434-594 |
1.05e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 434 VRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGT-------LHRPGGENETMFLSQLPYV---- 502
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgepLAKLNRAQRKAFRRDIQMVfqds 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 503 -----PLGTLRDVVCYP-----NSAAAIPDATLRDTLTKVALAP-LCDRLDEErdwakvLSPGEQQRVAFARILLTKPKA 571
Cdd:PRK10419 99 isavnPRKTVREIIREPlrhllSLDKAERLARASEMLRAVDLDDsVLDKRPPQ------LSGGQLQRVCLARALAVEPKL 172
|
170 180
....*....|....*....|...
gi 489997411 572 VFLDESTSALDTGLEFALYQLLR 594
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLK 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
551-616 |
1.14e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 1.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSElpDCIVISVSHR-PALERLHE 616
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRlSTVERADQ 682
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
439-607 |
1.27e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPlDVRLD--RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---------RPGGENETM-FLSQLPYvPLGT 506
Cdd:PRK11000 14 GDVVISK-DINLDihEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrmndvPPAERGVGMvFQSYALY-PHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPNSAAAIPDATLRDTLTKVA----LAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRVNQVAevlqLAHLLDRK------PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|..
gi 489997411 583 TGL------EFA-LYQLLRselpdCIVISVSH 607
Cdd:PRK11000 166 AALrvqmriEISrLHKRLG-----RTMIYVTH 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
551-608 |
1.36e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 54.44 E-value: 1.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR 552
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
441-625 |
1.39e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 441 RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPyASGtlhRPGGENET-------MFLSQLPYVPLGTLRDVV-- 511
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT-GGG---APRGARVTgdvtlngEPLAAIDAPRLARLRAVLpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 512 -----------------CYPNS----AAAIPDATLRDTLTKVALAPLCDRLDeerdwAKVLSPGEQQRVAFARIL----- 565
Cdd:PRK13547 91 aaqpafafsareivllgRYPHArragALTHRDGEIAWQALALAGATALVGRD-----VTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 566 ----LTKPKAVFLDESTSALDTGLEFALYQLLRSELPD--CIVISVSHRPALERLHENQLELLGGG 625
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
427-616 |
1.48e-07 |
|
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: 51.28 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGdRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLaelwpyaSGTLHRPGGEnetMFLSQLPYVPLGt 506
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKIL-------SGLYKPDSGE---ILVDGKEVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 lrdvvcyPNSAAAIPDATlrdtltkvalaplcdrldeerdwakV--LSPGEQQRVAFARILLTKPKAVFLDESTSALdTG 584
Cdd:cd03216 69 -------PRDARRAGIAM-------------------------VyqLSVGERQMVEIARALARNARLLILDEPTAAL-TP 115
|
170 180 190
....*....|....*....|....*....|....*.
gi 489997411 585 LE----FALYQLLRSElpDCIVISVSHrpaleRLHE 616
Cdd:cd03216 116 AEverlFKVIRRLRAQ--GVAVIFISH-----RLDE 144
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
427-607 |
1.52e-07 |
|
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: 52.69 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQLPYVplgT 506
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGED----IREQDPV---E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYP-NSAAAIPDATLRDTltkVALAPLCDRLDEERDWAKV---------------------LSPGEQQRVAFARI 564
Cdd:cd03295 73 LRRKIGYViQQIGLFPHMTVEEN---IALVPKLLKWPKEKIRERAdellalvgldpaefadrypheLSGGQQQRVGVARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489997411 565 LLTKPKAVFLDESTSALDTGLEFALYQL---LRSELPDCIVIsVSH 607
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVF-VTH 194
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-638 |
2.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 438 AGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGtlHRPGGE----NETMF--------------LSQL 499
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG--YRYSGDvllgGRSIFnyrdvlefrrrvgmLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PY-VPLGTLRDVVCYPNSAAAIPDATLRDT----LTKVAL-APLCDRLDeerDWAKVLSPGEQQRVAFARILLTKPKAVF 573
Cdd:PRK14271 110 PNpFPMSIMDNVLAGVRAHKLVPRKEFRGVaqarLTEVGLwDAVKDRLS---DSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489997411 574 LDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPALERLHENQLELLGGGQWrlapVEAAPAE 638
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL----VEEGPTE 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
457-626 |
2.62e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 457 VITGRSGAGKTTLLR---SLAELWPYA--SGTLHRPGGENETMFLSQL------------PYVPLGTLRDVVCYP----- 514
Cdd:PRK14247 33 ALMGPSGSGKSTLLRvfnRLIELYPEArvSGEVYLDGQDIFKMDVIELrrrvqmvfqipnPIPNLSIFENVALGLklnrl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 -NSAAAIpDATLRDTLTKVAL-APLCDRLDEErdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQL 592
Cdd:PRK14247 113 vKSKKEL-QERVRWALEKAQLwDEVKDRLDAP---AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL 188
|
170 180 190
....*....|....*....|....*....|....
gi 489997411 593 LRSELPDCIVISVSHRPALERLHENQLELLGGGQ 626
Cdd:PRK14247 189 FLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
443-593 |
3.25e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL---HRPGGENETMFLSQL-------------PYVPLGT 506
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELlidDHPLHFGDYSYRSQRirmifqdpstslnPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPNSAAAIPDATLR--DTLTKVALAPlcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTG 584
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQiiETLRQVGLLP-----DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
....*....
gi 489997411 585 LEFALYQLL 593
Cdd:PRK15112 184 MRSQLINLM 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
411-608 |
3.43e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 411 GRALPAVL---TRPSDDESVELNDIEVRTPAGDrlIDpLDVRldRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRP 487
Cdd:COG1129 238 GRELEDLFpkrAAAPGEVVLEVEGLSVGGVVRD--VS-FSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 488 GGEnetmflsqlpyVPLGTLRDVVcypnsaAA--------------IPDATLRDTLTKVALAPLCDR--LD--EERDWA- 548
Cdd:COG1129 313 GKP-----------VRIRSPRDAI------RAgiayvpedrkgeglVLDLSIRENITLASLDRLSRGglLDrrRERALAe 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 549 -----------------KVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLR-------------SELP 598
Cdd:COG1129 376 eyikrlriktpspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRelaaegkavivisSELP 455
|
250
....*....|
gi 489997411 599 DciVISVSHR 608
Cdd:COG1129 456 E--LLGLSDR 463
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
428-594 |
4.02e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTpagdRLIdPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYaSGTLHRpGGENetmfLSQLPYVPLGTL 507
Cdd:PRK03695 2 QLNDVAVST----RLG-PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQF-AGQP----LEAWSAAELARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 508 RDVVCYPNSAAAI-----------PD----ATLRDTLTKVA-LAPLCDRLdeERDwAKVLSPGEQQRVAFARILL----- 566
Cdd:PRK03695 71 RAYLSQQQTPPFAmpvfqyltlhqPDktrtEAVASALNEVAeALGLDDKL--GRS-VNQLSGGEWQRVRLAAVVLqvwpd 147
|
170 180 190
....*....|....*....|....*....|
gi 489997411 567 TKP--KAVFLDESTSALDTGLEFALYQLLR 594
Cdd:PRK03695 148 INPagQLLLLDEPMNSLDVAQQAALDRLLS 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
458-582 |
4.40e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.39 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTLhRPGGENetmfLSQLPYVPLGTLR-------------------DVVCYPNSAA 518
Cdd:COG1135 36 IIGYSGAGKSTLIRCINLLERPTSGSV-LVDGVD----LTALSERELRAARrkigmifqhfnllssrtvaENVALPLEIA 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 519 AIPDATLRDtltKVAlaPLCDRLD-EERDWAKV--LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG1135 111 GVPKAEIRK---RVA--ELLELVGlSDKADAYPsqLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
438-582 |
4.68e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.27 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 438 AGDRLIDPLD---VRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH-------RPGGENET--------MFlsQL 499
Cdd:PRK11308 23 KPERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllKADPEAQKllrqkiqiVF--QN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PYVPLG---TLRDVVCYP-----NSAAAIPDATLRDTLTKVALAP-LCDRldeerdWAKVLSPGEQQRVAFARILLTKPK 570
Cdd:PRK11308 101 PYGSLNprkKVGQILEEPllintSLSAAERREKALAMMAKVGLRPeHYDR------YPHMFSGGQRQRIAIARALMLDPD 174
|
170
....*....|..
gi 489997411 571 AVFLDESTSALD 582
Cdd:PRK11308 175 VVVADEPVSALD 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
513-610 |
6.03e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 513 YPNSAAAIPDATLRDTLTKVALAPL---CDRLDEERD-----WAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTG 584
Cdd:PTZ00265 1313 YENIKFGKEDATREDVKRACKFAAIdefIESLPNKYDtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
90 100
....*....|....*....|....*...
gi 489997411 585 LEFALYQLLR--SELPDCIVISVSHRPA 610
Cdd:PTZ00265 1393 SEKLIEKTIVdiKDKADKTIITIAHRIA 1420
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
442-588 |
6.23e-07 |
|
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: 50.34 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 442 LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPYAS--GTLHRPG---GENETMFLSQLPYVPLGTLRdvvcypn 515
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnRTEGNVSveGDIHYNGipyKEFAEKYPGEIIYVSEEDVH------- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489997411 516 saaaIPDATLRDTLTKVALAplcdRLDEerdWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD--TGLEFA 588
Cdd:cd03233 95 ----FPTLTVRETLDFALRC----KGNE---FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDssTALEIL 158
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
423-608 |
6.38e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 423 DDESVeLNDIEVRTPAGdrlidpldvrldrgGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM-------- 494
Cdd:PRK10790 352 DDNLV-LQNINLSVPSR--------------GFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshsvlrqg 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 --FLSQLPYVPLGTLRDVVCYPNSaaaIPDATLRDTLTKVALAPLC--------DRLDEErdwAKVLSPGEQQRVAFARI 564
Cdd:PRK10790 417 vaMVQQDPVVLADTFLANVTLGRD---ISEEQVWQALETVQLAELArslpdglyTPLGEQ---GNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489997411 565 LLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHR 534
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
452-609 |
6.72e-07 |
|
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: 49.29 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 452 RGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHrpggenetmflsqlpYVPLGTLRDVvcypnsaaaipdatlrdtltk 531
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------YIDGEDILEE--------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 532 valAPLCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSEL-------PDCIVIS 604
Cdd:smart00382 45 ---VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTVIL 121
|
....*
gi 489997411 605 VSHRP 609
Cdd:smart00382 122 TTNDE 126
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
456-636 |
6.95e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 456 LVITGRSGAGKTTLLRSLAELWPYA---SGTLHRPGGENETMFLSQLP--------YVPLGTLRDVVCYP-------NSA 517
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISayvqqddlFIPTLTVREHLMFQahlrmprRVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 AAIPDATLRDTLTKVALAPLCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRsEL 597
Cdd:TIGR00955 134 KKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK-GL 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489997411 598 PD--CIVISVSHRPALErLHE--NQLELLGGGQ--WRLAPVEAAP 636
Cdd:TIGR00955 213 AQkgKTIICTIHQPSSE-LFElfDKIILMAEGRvaYLGSPDQAVP 256
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
427-582 |
8.08e-07 |
|
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: 51.21 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVR--TPAGD-RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWP---YASGT--------LHRPGGENE 492
Cdd:COG0444 2 LEVRNLKVYfpTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEilfdgedlLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 493 TMFLSQLPYV---------PLGTLRDVVCYP-------NSAAAipDATLRDTLTKVALAPLCDRLDE---ErdwakvLSP 553
Cdd:COG0444 82 KIRGREIQMIfqdpmtslnPVMTVGDQIAEPlrihgglSKAEA--RERAIELLERVGLPDPERRLDRyphE------LSG 153
|
170 180
....*....|....*....|....*....
gi 489997411 554 GEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
551-607 |
8.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 8.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPD--CIVISVSH 607
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITH 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
429-618 |
9.46e-07 |
|
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: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 429 LNDIEVR-TPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPyASGTLHRPGGENETMFLSQ-------LP 500
Cdd:TIGR01271 1220 VQGLTAKyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwrkafgvIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 ---YVPLGTLRDVVcypNSAAAIPDATLRDTLTKVALAPLC----DRLD-EERDWAKVLSPGEQQRVAFARILLTKPKAV 572
Cdd:TIGR01271 1299 qkvFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIeqfpDKLDfVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489997411 573 FLDESTSALDTglefALYQLLRSEL----PDCIVISVSHRpaLERLHENQ 618
Cdd:TIGR01271 1376 LLDEPSAHLDP----VTLQIIRKTLkqsfSNCTVILSEHR--VEALLECQ 1419
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
551-608 |
1.14e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLR-------------SELPDciVISVSHR 608
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINqfkaeglsiilvsSEMPE--VLGMSDR 464
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
441-594 |
1.17e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 441 RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWP-----YASG---------------TLHRPGGENETMFLsQLP 500
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGdirfhgesllhaseqTLRGVRGNKIAMIF-QEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 501 YV---PLGT----LRDVVC----YPNSAAAipdATLRDTLTKVALAPLCDRLdeeRDWAKVLSPGEQQRVAFARILLTKP 569
Cdd:PRK15134 102 MVslnPLHTlekqLYEVLSlhrgMRREAAR---GEILNCLDRVGIRQAAKRL---TDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180
....*....|....*....|....*
gi 489997411 570 KAVFLDESTSALDTGLEFALYQLLR 594
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLR 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
460-607 |
1.51e-06 |
|
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: 49.52 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSLAELWPYASG--TLHRPGGENETMFLSQLpyvplGTLRDV-VCYPNSAA-----------AIPDATL 525
Cdd:cd03268 33 GPNGAGKTTTMKIILGLIKPDSGeiTFDGKSYQKNIEALRRI-----GALIEApGFYPNLTArenlrllarllGIRKKRI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 526 RDTLTKVALAplcdrlDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSeLPD---CIV 602
Cdd:cd03268 108 DEVLDVVGLK------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS-LRDqgiTVL 180
|
....*
gi 489997411 603 ISvSH 607
Cdd:cd03268 181 IS-SH 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-610 |
1.55e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 440 DRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRS---LAELWPYA--SGTLhRPGGEN-------------ETMFLSQLPY 501
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEV-RLFGRNiyspdvdpievrrEVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 502 vPLGTLrdvVCYPNSAAAIP-----------DATLRDTLTKVAL-APLCDRLdeeRDWAKVLSPGEQQRVAFARILLTKP 569
Cdd:PRK14267 96 -PFPHL---TIYDNVAIGVKlnglvkskkelDERVEWALKKAALwDEVKDRL---NDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489997411 570 KAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPA 610
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPA 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
443-620 |
1.65e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPyasgtlhrpGGENETMFLSQLPY---VPLGTLRDVVCY-PNSA- 517
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---------GKFEGNVFINGKPVdirNPAQAIRAGIAMvPEDRk 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 --AAIPDATLRDTLTKVALAPLC--DRLDEERDWAKV--------------------LSPGEQQRVAFARILLTKPKAVF 573
Cdd:TIGR02633 347 rhGIVPILGVGKNITLSVLKSFCfkMRIDAAAELQIIgsaiqrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 574 LDESTSALDTGLEFALYQLL-------------RSELPDciVISVSHRPALerLHENQLE 620
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLInqlaqegvaiivvSSELAE--VLGLSDRVLV--IGEGKLK 482
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
427-618 |
1.86e-06 |
|
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: 49.85 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVR-TPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWpYASGTLHRPGGENETMFLSQ------- 498
Cdd:cd03289 3 MTVKDLTAKyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwrkafgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 499 LP---YVPLGTLRDVVcYPNSAAAipDATLRDTLTKVALAPLCDRLDEERDW-----AKVLSPGEQQRVAFARILLTKPK 570
Cdd:cd03289 82 IPqkvFIFSGTFRKNL-DPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFvlvdgGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489997411 571 AVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRpaLERLHENQ 618
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHR--IEAMLECQ 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
439-628 |
2.41e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.70 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGgenETMflsQLPYVplGTLRDVVcYPNSA 517
Cdd:TIGR03719 333 GDKlLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIG---ETV---KLAYV--DQSRDAL-DPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 A--AIPDATlrDTLT----KVALAPLCDRL-----DEERDwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDT--- 583
Cdd:TIGR03719 403 VweEISGGL--DIIKlgkrEIPSRAYVGRFnfkgsDQQKK-VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVetl 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489997411 584 -GLEFALyqllrSELPDCIVIsVSH-RPALERLHENQLELLGGGQWR 628
Cdd:TIGR03719 480 rALEEAL-----LNFAGCAVV-ISHdRWFLDRIATHILAFEGDSHVE 520
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
442-614 |
2.59e-06 |
|
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: 47.74 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 442 LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENEtmflsqlpyvplgtlRDVVCYpnsaaaiP 521
Cdd:cd03227 10 YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKA---------------GCIVAA-------V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 522 DATLRDTLTKvalaplcdrldeerdwakvLSPGEQQRVAFARIL---LTKPKA-VFLDESTSALDTGLEFAL-YQLLRSE 596
Cdd:cd03227 68 SAELIFTRLQ-------------------LSGGEKELSALALILalaSLKPRPlYILDEIDRGLDPRDGQALaEAILEHL 128
|
170
....*....|....*...
gi 489997411 597 LPDCIVISVSHRPALERL 614
Cdd:cd03227 129 VKGAQVIVITHLPELAEL 146
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
450-624 |
2.67e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 450 LDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM--------------FLSQLPYV-PLGTLRDVVCYP 514
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnqklgFIYQFHHLlPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 ----NSAAAIPDATLRDTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALY 590
Cdd:PRK11629 112 lligKKKPAEINSRALEMLAAVGLEHRANHRPSE------LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 489997411 591 QLLrSEL---PDCIVISVSHRPALERLHENQLELLGG 624
Cdd:PRK11629 186 QLL-GELnrlQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
458-616 |
2.68e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTlhRPGGENEtmFLSQLPY---VPLGTLRDVV-------------CYPNSAAAI- 520
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLNRMNELESEV--RVEGRVE--FFNQNIYerrVNLNRLRRQVsmvhpkpnlfpmsVYDNVAYGVk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 521 -----PDATLRDTL-TKVALAPLCDRLDEE-RDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQL- 592
Cdd:PRK14258 114 ivgwrPKLEIDDIVeSALKDADLWDEIKHKiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLi 193
|
170 180
....*....|....*....|....*...
gi 489997411 593 ----LRSELpdCIVISVSHRPALERLHE 616
Cdd:PRK14258 194 qslrLRSEL--TMVIVSHNLHQVSRLSD 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
428-624 |
3.49e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.11 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGDRLIDPLD---VRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM---------- 494
Cdd:PRK10535 6 ELKDIRRSYPSGEEQVEVLKgisLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaqlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 495 ----FLSQ----LPYvpLGTLRDV---VCYPNSAAAIPDATLRDTLTKVALAplcDRLDEErdwAKVLSPGEQQRVAFAR 563
Cdd:PRK10535 86 ehfgFIFQryhlLSH--LTAAQNVevpAVYAGLERKQRLLRAQELLQRLGLE---DRVEYQ---PSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 564 ILLTKPKAVFLDESTSALD--TGLE-FALYQLLRSElpDCIVISVSHRPALERLHENQLELLGG 624
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDshSGEEvMAILHQLRDR--GHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
551-611 |
3.52e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLrSELPD---CIVISVSHRPAL 611
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLI-AELAKkdkGIIIISSEMPEL 454
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
443-582 |
3.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.93 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 443 IDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTlhrpggenetMFLSQLPYVPLGTLRDVvcyPNSAAAI-- 520
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK----------VYVDGLDTSDEENLWDI---RNKAGMVfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 521 -PDATLRDTLTK--VALAP---------LCDRLDEE---------RDWA-KVLSPGEQQRVAFARILLTKPKAVFLDEST 578
Cdd:PRK13633 93 nPDNQIVATIVEedVAFGPenlgippeeIRERVDESlkkvgmyeyRRHApHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
....
gi 489997411 579 SALD 582
Cdd:PRK13633 173 AMLD 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
458-607 |
4.77e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLA--------ELWPyasgtlhRPG---GenetmFLSQLPYV-PLGTLRDVV---CYP-------- 514
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAgvdkdfngEARP-------QPGikvG-----YLPQEPQLdPTKTVRENVeegVAEikdaldrf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 ---NSAAAIPDATLRDTLTKvaLAPLCDRLDEERDW-------------------AKV--LSPGEQQRVAFARILLTKPK 570
Cdd:TIGR03719 104 neiSAKYAEPDADFDKLAAE--QAELQEIIDAADAWdldsqleiamdalrcppwdADVtkLSGGERRRVALCRLLLSKPD 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 489997411 571 AVFLDESTSALDTGLEFALYQLLRsELPDCiVISVSH 607
Cdd:TIGR03719 182 MLLLDEPTNHLDAESVAWLERHLQ-EYPGT-VVAVTH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
551-619 |
6.07e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLL-------------RSELPDciVISVSHRPALerLHEN 617
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInqlvqqgvaiiviSSELPE--VLGLSDRVLV--MHEG 481
|
..
gi 489997411 618 QL 619
Cdd:PRK13549 482 KL 483
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
427-626 |
6.43e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.15 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 427 VELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmflsqLPYVPLGT 506
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP--------IKYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 L--RDVV--CYPNSAAAIPDATLRDtltKVALAPLCDRLDEERDWAKV-------------------LSPGEQQRVAFAR 563
Cdd:PRK13639 74 LevRKTVgiVFQNPDDQLFAPTVEE---DVAFGPLNLGLSKEEVEKRVkealkavgmegfenkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 564 ILLTKPKAVFLDESTSALDTGLEFALYQLLrSELPD---CIVISvSHRPALERLHENQLELLGGGQ 626
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKegiTIIIS-THDVDLVPVYADKVYVMSDGK 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
452-607 |
6.62e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 452 RGGSLVITGRSGAGKTTLLRSLA-ELWP----------------YASGTlhrpggENETMF--LSQlpyvplGTLRdVVC 512
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSgELIPnlgdyeeepswdevlkRFRGT------ELQNYFkkLYN------GEIK-VVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 513 YPNSAAAIPDA---TLRDTLTKV----ALAPLCDRLDEE----RDwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSAL 581
Cdd:PRK13409 165 KPQYVDLIPKVfkgKVRELLKKVdergKLDEVVERLGLEnildRD-ISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*.
gi 489997411 582 DTGLEFALYQLLRSELPDCIVISVSH 607
Cdd:PRK13409 244 DIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
551-608 |
8.90e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 8.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHR 608
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
426-585 |
1.12e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 426 SVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLH---------RPGGENETMFL 496
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvnelEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 497 SQLPYVPLGTLRDVVCYPNSAAAIPDATLRDTLTKVA----LAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPkAV 572
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAArileLEPLLDRKPRE------LSGGQRQRVAMGRAIVREP-AV 155
|
170
....*....|....
gi 489997411 573 FL-DESTSALDTGL 585
Cdd:PRK11650 156 FLfDEPLSNLDAKL 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
453-593 |
1.62e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 453 GGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETM-------------FLSQLPYVPLGTlRDVVCY------ 513
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgklqalrrdiqFIFQDPYASLDP-RQTVGDsimepl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 514 ------PNSAAAIPDATLrdtLTKVALAPlcdrldeERDW--AKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:PRK10261 429 rvhgllPGKAAAARVAWL---LERVGLLP-------EHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
....*...
gi 489997411 586 EFALYQLL 593
Cdd:PRK10261 499 RGQIINLL 506
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
450-602 |
1.62e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.72 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 450 LDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPG---------------GENETMFLSQLPYVPLGTLRDVVCYP 514
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 515 NSAAAIPDATLR----DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTglefaly 590
Cdd:PRK10070 131 MELAGINAEERRekalDALRQVGLENYAHSYPDE------LSGGMRQRVGLARALAINPDILLMDEAFSALDP------- 197
|
170
....*....|..
gi 489997411 591 qLLRSELPDCIV 602
Cdd:PRK10070 198 -LIRTEMQDELV 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
424-607 |
2.30e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.67 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 424 DESVELNDIEVRTPAGDRLidpldvrldrggslVITGRSGAGKTTLLRSLAELWPYASGTL----HRPGGEN-------- 491
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWT--------------SIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNfeklrkhi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 492 -------ETMFL-SQLPY-VPLGTLRDVVCYPNSAAAIPDAtlrdtLTKValaplcDRLDEERDWAKVLSPGEQQRVAFA 562
Cdd:PRK13648 86 givfqnpDNQFVgSIVKYdVAFGLENHAVPYDEMHRRVSEA-----LKQV------DMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489997411 563 RILLTKPKAVFLDESTSALDTGLEFALYQLLR--SELPDCIVISVSH 607
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITH 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
442-607 |
2.55e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 442 LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLA-ELWPyASGTLHrpGGENetmflSQLPYVPLGTLRDvvcYPNsaaai 520
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVgELEP-DSGTVK--WSEN-----ANIGYYAQDHAYD---FEN----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 521 pDATLRDTLTK--------VALAPLCDRL----DEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDT----G 584
Cdd:PRK15064 398 -DLTLFDWMSQwrqegddeQAVRGTLGRLlfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMesieS 476
|
170 180
....*....|....*....|...
gi 489997411 585 LEFALyqllrsELPDCIVISVSH 607
Cdd:PRK15064 477 LNMAL------EKYEGTLIFVSH 493
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
460-608 |
2.92e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSLAELWPYASGTLHRpgGENETMFLS--------------QLPYVP---------LGTLrdvvcyPNS 516
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILI--DGQEMRFASttaalaagvaiiyqELHLVPemtvaenlyLGQL------PHK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 517 AAAIPDATLRDTlTKVALAPLCDRLDEErdwAKV--LSPGEQQRVAFARILLTKPKAVFLDESTSAL---DTGLEFALYQ 591
Cdd:PRK11288 109 GGIVNRRLLNYE-AREQLEHLGVDIDPD---TPLkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIR 184
|
170
....*....|....*..
gi 489997411 592 LLRSElpDCIVISVSHR 608
Cdd:PRK11288 185 ELRAE--GRVILYVSHR 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
458-582 |
3.25e-05 |
|
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: 46.72 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTLH-RPGGENETM----FLSQ---LPYvpLGTL-RDVVCYPNSaaaipdaTLRDT 528
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMtkpgPDGRgraKRY--IGILhQEYDLYPHR-------TVLDN 385
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 529 LTKVALAPLCDRL--------------DEER------DWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:TIGR03269 386 LTEAIGLELPDELarmkavitlkmvgfDEEKaeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
453-607 |
3.38e-05 |
|
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: 45.82 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 453 GGSLVITGRSGAGKTTLLRSLA-ELWPYAsGTLHRPGGENETM----------FLSQLpyvpLGTLRDVVCYPNSAAAIP 521
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgKLKPNL-GKFDDPPDWDEILdefrgselqnYFTKL----LEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 522 ---DATLRDTLTKV----ALAPLCDRLD----EERDWAKvLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALY 590
Cdd:cd03236 101 kavKGKVGELLKKKdergKLDELVDQLElrhvLDRNIDQ-LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170
....*....|....*...
gi 489997411 591 QLLRSEL-PDCIVISVSH 607
Cdd:cd03236 180 RLIRELAeDDNYVLVVEH 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
460-582 |
3.60e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 460 GRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYVP-----------------LGTLRDVvcypnSAAAIPD 522
Cdd:COG4152 34 GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPeerglypkmkvgeqlvyLARLKGL-----SKAEAKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489997411 523 ATLRdtltkvalapLCDRLD-EERDWAKV--LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:COG4152 109 RADE----------WLERLGlGDRANKKVeeLSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
458-608 |
3.93e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 458 ITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQL-------PYVPL---GTLR---DVVCYPNSA---AAIP 521
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLrkvlgiiPQAPVlfsGTVRfnlDPFNEHNDAdlwESLE 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 522 DATLRDTLTKVALAplcdrLDEERDWA-KVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDC 600
Cdd:PLN03130 1350 RAHLKDVIRRNSLG-----LDAEVSEAgENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSC 1424
|
....*...
gi 489997411 601 IVISVSHR 608
Cdd:PLN03130 1425 TMLIIAHR 1432
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
428-585 |
5.51e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.35 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 428 ELNDIEVRTPAGD-RLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGE---------------- 490
Cdd:PRK10619 5 KLNVIDLHKRYGEhEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 491 --------NETMFLSQLP-YVPLGTLRDVVCYPNSAAAIPDATLRDT----LTKVALaplcdrldEERDWAKV---LSPG 554
Cdd:PRK10619 85 nqlrllrtRLTMVFQHFNlWSHMTVLENVMEAPIQVLGLSKQEARERavkyLAKVGI--------DERAQGKYpvhLSGG 156
|
170 180 190
....*....|....*....|....*....|.
gi 489997411 555 EQQRVAFARILLTKPKAVFLDESTSALDTGL 585
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPEL 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
551-582 |
7.14e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 7.14e-05
10 20 30
....*....|....*....|....*....|..
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
450-639 |
7.16e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 450 LDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTL----HRPGGEN------ETMFLSQLPYVPL--GTLRDVVCYPNSA 517
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgELLTAENvwnlrrKIGMVFQNPDNQFvgATVEDDVAFGMEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 AAIPDATLRDTLTKVALAplCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRsEL 597
Cdd:PRK13642 110 QGIPREEMIKRVDEALLA--VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH-EI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489997411 598 PD---CIVISVSHRPAlERLHENQLELLGGGQwrlAPVEAAPAEV 639
Cdd:PRK13642 187 KEkyqLTVLSITHDLD-EAASSDRILVMKAGE---IIKEAAPSEL 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
551-607 |
8.27e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 44.72 E-value: 8.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPDCIVISVSH 607
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirDDYQMTVISITH 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
551-607 |
9.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.60 E-value: 9.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS--ELPDCIVISVSH 607
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITH 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
537-608 |
1.08e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489997411 537 LCDRLDEERD-WAKV--LSPGEQQRVAFARILLTKPKAVFLDESTSALdTGLEFA-LYQLLRsELPD---CIVIsVSHR 608
Cdd:COG1129 124 LLARLGLDIDpDTPVgdLSVAQQQLVEIARALSRDARVLILDEPTASL-TEREVErLFRIIR-RLKAqgvAIIY-ISHR 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
540-595 |
1.67e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489997411 540 RLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS 595
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS 448
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
450-626 |
1.77e-04 |
|
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: 43.29 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 450 LDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGenetmflsqlpyvplgtlrdVVCYPNSAAAI-PDATLRDT 528
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------------------VSSLLGLGGGFnPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 529 LTKVAL------APLCDRLDEERDWA----------KVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTglEFAL--Y 590
Cdd:cd03220 105 IYLNGRllglsrKEIDEKIDEIIEFSelgdfidlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA--AFQEkcQ 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 489997411 591 QLLRSELPDC-IVISVSHRPALERLHENQLELLGGGQ 626
Cdd:cd03220 183 RRLRELLKQGkTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
551-582 |
1.88e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|..
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
548-608 |
2.14e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 548 AKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFaLYQLLRSELP---DCIVISVSHR 608
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKgneNRITIIIAHR 639
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
440-582 |
3.67e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.69 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 440 DRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWP----------YASGTLHRPG----------GENETMF---- 495
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGrlardirksrANTGYIFqqfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 496 ----LSQLPYVPLGTLRDV----VCYPNSAAAIPDATLRdTLTKVALAplcdRLDEERdwAKVLSPGEQQRVAFARILLT 567
Cdd:PRK09984 97 lvnrLSVLENVLIGALGSTpfwrTCFSWFTREQKQRALQ-ALTRVGMV----HFAHQR--VSTLSGGQQQRVAIARALMQ 169
|
170
....*....|....*
gi 489997411 568 KPKAVFLDESTSALD 582
Cdd:PRK09984 170 QAKVILADEPIASLD 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
439-582 |
5.38e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 42.19 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGEnetmfLSQLP----------YVP--LGT 506
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED-----ISLLPlhararrgigYLPqeASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 507 LRDVVCYPNSAAAIpdaTLRDTLTKVALAPLCDRLDEE------RD-WAKVLSPGEQQRVAFARILLTKPKAVFLDESTS 579
Cdd:PRK10895 90 FRRLSVYDNLMAVL---QIRDDLSAEQREDRANELMEEfhiehlRDsMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 489997411 580 ALD 582
Cdd:PRK10895 167 GVD 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
527-607 |
6.63e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 527 DTLTKVAL--APLCDRL-DEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVI 603
Cdd:PRK14243 125 DELVERSLrqAALWDEVkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTII 204
|
....
gi 489997411 604 SVSH 607
Cdd:PRK14243 205 IVTH 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
425-591 |
6.91e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 425 ESVELNDIEVRTPAGD---------RLIDP----LDVRLDRGGSLVITGRSGAGKTTLLRS-LAELWPyASGTLHRPGge 490
Cdd:TIGR01271 411 EKIKQNNKARKQPNGDdglffsnfsLYVTPvlknISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEP-SEGKIKHSG-- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 491 nETMFLSQLPYVPLGTLRDVVCYPNS------AAAIPDATLRDTLTKVAlaplcdrldeERDWAKV------LSPGEQQR 558
Cdd:TIGR01271 488 -RISFSPQTSWIMPGTIKDNIIFGLSydeyryTSVIKACQLEEDIALFP----------EKDKTVLgeggitLSGGQRAR 556
|
170 180 190
....*....|....*....|....*....|...
gi 489997411 559 VAFARILLTKPKAVFLDESTSALDTGLEFALYQ 591
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
526-595 |
7.75e-04 |
|
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: 41.65 E-value: 7.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 526 RDTLTKVALAPLCDRLdeerdwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRS 595
Cdd:cd03219 125 EELLERVGLADLADRP------AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRE 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
549-582 |
8.38e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 8.38e-04
10 20 30
....*....|....*....|....*....|....
gi 489997411 549 KVLSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
551-607 |
1.16e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 41.19 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALD-TGLE--FALYQLLRSELpDCIVISVSH 607
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDeiLNKIKELHKEY-NMTIILVSH 203
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
451-475 |
1.18e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.18e-03
10 20
....*....|....*....|....*
gi 489997411 451 DRGGSLVITGRSGAGKTTLLRSLAE 475
Cdd:COG3267 41 QGGGFVVLTGEVGTGKTTLLRRLLE 65
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
456-582 |
1.20e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 40.85 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 456 LVITGRSGAGKTTLLRSLAelwpyasGTLHRPGGENETmFLSQLPYVPL-------GTLRDVVcypnsAAAIPDATLR-- 526
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLA-------GVLKPDEGDIEI-ELDTVSYKPQyikadyeGTVRDLL-----SSITKDFYTHpy 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 527 ---DTLTKVALAPLCDRLDEErdwakvLSPGEQQRVAFArILLTKPKAVFL-DESTSALD 582
Cdd:cd03237 95 fktEIAKPLQIEQILDREVPE------LSGGELQRVAIA-ACLSKDADIYLlDEPSAYLD 147
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
439-627 |
1.32e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 439 GDR-LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLhRPGgenETMflsQLPYVplgtlrDvvcypNSA 517
Cdd:PRK11819 335 GDRlLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-KIG---ETV---KLAYV------D-----QSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 518 AAI-PDATL-------RDTLT----KVALAPLCDRL-----DEERDwAKVLSPGEQQRVAFARILLTKPKAVFLDESTSA 580
Cdd:PRK11819 397 DALdPNKTVweeisggLDIIKvgnrEIPSRAYVGRFnfkggDQQKK-VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTND 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489997411 581 LDT----GLEFALyqllrSELPDCIVIsVSH-RPALERLHENQLELLGGGQW 627
Cdd:PRK11819 476 LDVetlrALEEAL-----LEFPGCAVV-ISHdRWFLDRIATHILAFEGDSQV 521
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
551-608 |
1.63e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSAL-DTGLEfALYQLLRsELPD--CIVISVSHR 608
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIR-ELKSqgRGIVYISHR 200
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
445-476 |
1.78e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 39.93 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|..
gi 489997411 445 PLDVRLDRGGSLVITGRSGAGKTTLLRSLAEL 476
Cdd:cd03243 21 PNDINLGSGRLLLITGPNMGGKSTYLRSIGLA 52
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
421-586 |
2.00e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.61 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 421 PSDDESVELNDIEVRtpaGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRS-LAELWPyASGTLHRPGgenETMFLSQL 499
Cdd:cd03291 34 SSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLiLGELEP-SEGKIKHSG---RISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 500 PYVPLGTLRDVVCYPNS------AAAIPDATLRDTLTKVAlaplcdrldeERDWAKV------LSPGEQQRVAFARILLT 567
Cdd:cd03291 107 SWIMPGTIKENIIFGVSydeyryKSVVKACQLEEDITKFP----------EKDNTVLgeggitLSGGQRARISLARAVYK 176
|
170
....*....|....*....
gi 489997411 568 KPKAVFLDESTSALDTGLE 586
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTE 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
442-582 |
2.04e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 442 LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGtlhRPGGENETMFLSQLPYVPLGTLRDVVCY--PNSAAA 519
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG---RVWAERSIAYVPQQAWIMNATVRGNILFfdEEDAAR 751
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 520 IPDAtLRDTLTKVALAPLCDRLDEERDWAKV-LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PTZ00243 752 LADA-VRVSQLEADLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
449-476 |
3.08e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 3.08e-03
10 20
....*....|....*....|....*...
gi 489997411 449 RLDRGGSLVITGRSGAGKTTLLRSLAEL 476
Cdd:pfam13401 1 IRFGAGILVLTGESGTGKTTLLRRLLEQ 28
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
447-476 |
4.98e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|
gi 489997411 447 DVRLDRGGSLVITGRSGAGKTTLLRSLAEL 476
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
551-582 |
6.64e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.91 E-value: 6.64e-03
10 20 30
....*....|....*....|....*....|..
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALD 582
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
551-623 |
7.77e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 7.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489997411 551 LSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRsELPD----CIVISvSHRPalerlhenqlELLG 623
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIIN-ELAAegkgVIVIS-SELP----------ELLG 469
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
417-560 |
9.21e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.40 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997411 417 VLTRPSDDESVELNDIEVRTPAGDR--LIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPyasgtlhrpggENETM 494
Cdd:COG5635 142 ILLLDADGLLVSLDDLYVPLNLLERieSLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELA-----------ERYLD 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997411 495 FLSQLP-YVPLGTLRD-------VVCYPNSAAAIPDATLRDTLTKVALAPLCDRLDEerdwakVLSPGEQQRVA 560
Cdd:COG5635 211 AEDPIPiLIELRDLAEeasledlLAEALEKRGGEPEDALERLLRNGRLLLLLDGLDE------VPDEADRDEVL 278
|
|
| |
