|
Name |
Accession |
Description |
Interval |
E-value |
| TyrR |
COG3283 |
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ... |
1-516 |
0e+00 |
|
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];
Pssm-ID: 442513 [Multi-domain] Cd Length: 514 Bit Score: 819.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 1 MRIKVHCQNRVGILRDILNLLVDYGINVNRGEVggDQGNAIYLLCPNMINLQLQSLRPKLEAVPGVFGVKRVGLMPSERR 80
Cdd:COG3283 1 MRLEVTCEDRLGITRELLDLLVERNIDLRGIEI--DPSGRIYLNFPELDFEQFQHLMPEIRRIPGVTDVRTVPFMPSERE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 81 HLELNALLAALDFPVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARINGLRVKVKGDVFL 160
Cdd:COG3283 79 HLELDALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLSELLKGFNFSRWLESNEPRPQSERVVINGQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 161 ADIAPLQSEHDESE-ALAGAVLTLHRADRVGERIYHVRKQELRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGT 239
Cdd:COG3283 159 ADILPIYLPDEEGKsILAGAVVTLKSAARLGEQLQALQVNDDSGFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 240 GKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFeGARPEGKLGLLELTAGGTLFLDGVGEMSPRLQAK 319
Cdd:COG3283 239 GKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAF-GNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 320 LLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASR 399
Cdd:COG3283 318 LLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 400 QIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHIRLPDYGAPQPLGDFSLEGDLDAIVGRFEKA 479
Cdd:COG3283 398 QLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPEDLQLPEYAASAGLLDDLLEGSLDEIVKRFERS 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 15596070 480 VLERLFREHPSSRQLGKRLGVSHTTAANKLRQHGVGQ 516
Cdd:COG3283 478 LLRRLYPSYPSTRKLAKRLGVSHTAIANKLREYGIGK 514
|
|
| PRK10820 |
PRK10820 |
transcriptional regulator TyrR; |
1-519 |
0e+00 |
|
transcriptional regulator TyrR;
Pssm-ID: 236769 [Multi-domain] Cd Length: 520 Bit Score: 518.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 1 MRIKVHCQNRVGILRDILNLLVDYGINVNRGEVggDQGNAIYLLCPNMINLQLQSLRPKLEAVPGVFGVKRVGLMPSERR 80
Cdd:PRK10820 1 MRLEVFCEDRLGLTRELLDLLVLRSIDLRGIEI--DPIGRIYLNFAELEFESFSSLMAEIRRIAGVTDVRTVPFMPSERE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 81 HLELNALLAALDFPVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARINGLRVKVKGDVFL 160
Cdd:PRK10820 79 HRALSALLEALPEPVLSIDMKGKVELANPASCQLFGQSEEKLRNHTAAQLINGFNFLRWLESEPQDSHNEHVVINGQDFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 161 ADIAPLQSEHDESE-ALAGAVLTLHRADRVGERIYHVRKQELRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGT 239
Cdd:PRK10820 159 MEITPVYLQDENDQhVLVGAVVMLRSTARMGRQLQNLAVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 240 GKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARpEGKLGLLELTAGGTLFLDGVGEMSPRLQAK 319
Cdd:PRK10820 239 GKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPNAL-EGKKGFFEQANGGSVLLDEIGEMSPRMQAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 320 LLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASR 399
Cdd:PRK10820 318 LLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFAD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 400 QIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHIRLPDYGAPQPLGDFSLEGDLDAIVGRFEKA 479
Cdd:PRK10820 398 EQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELRPQDILLPDYDAAVAVGEDAMEGSLDEITSRFERS 477
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15596070 480 VLERLFREHPSSRQLGKRLGVSHTTAANKLRQHGVGQSEG 519
Cdd:PRK10820 478 VLTRLYRNYPSTRKLAKRLGVSHTAIANKLREYGLSQKKG 517
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
94-513 |
2.35e-150 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 437.67 E-value: 2.35e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 94 PVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARING-LRVKVKGDVFLADIAPLQSEHDe 172
Cdd:COG3829 23 GIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPVTGViQKTGGKGKTVIVTAIPIFEDGE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 173 seaLAGAVLTLHRADRVGERIYHVRKQELR-------GFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLA 245
Cdd:COG3829 102 ---VIGAVETFRDITELKRLERKLREEELErglsakyTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 246 RACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQ 325
Cdd:COG3829 179 RAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKKGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 326 DGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGL 405
Cdd:COG3829 259 EKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 406 PKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHirLPDY-GAPQPLGDFSLEGDLDAIVGRFEKAVLERL 484
Cdd:COG3829 339 KGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVITPEH--LPEYlLEEAEAASAAEEGSLKEALEEVEKELIEEA 416
|
410 420 430
....*....|....*....|....*....|
gi 15596070 485 FREHPSSR-QLGKRLGVSHTTAANKLRQHG 513
Cdd:COG3829 417 LEKTGGNKsKAAKALGISRSTLYRKLKKYG 446
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
94-513 |
2.89e-115 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 353.82 E-value: 2.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 94 PVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRyVEDLDLPELVRANKARinglrvkvkgdvfLADIAPLqseHDES 173
Cdd:COG3284 228 GLLAFDEDGRIVAANRAARRLLGLADAALLGRPLEE-LFGLDLEALPDGARRA-------------PASPRPL---RLRD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 174 EALAGAVLTLHRADRVGERIyHVRKQELRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASP 253
Cdd:COG3284 291 GRRLGALLRLRPARRAARAA-PAGAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 254 RGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVG 333
Cdd:COG3284 370 RADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 334 SDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDgLAPLAEHFLDQASRqiGCGLPKLSAQAL 413
Cdd:COG3284 450 GTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRERED-LPALIEHLLRELAA--GRGPLRLSPEAL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 414 ERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHirLPDY-----GAPQPLGDFSLeGDLDAIvgrfEKAVLERLFREH 488
Cdd:COG3284 527 ALLAAYPWPGNVRELRNVLRTALALADGGVITVED--LPDElraelAAAAPAAAAPL-TSLEEA----ERDAILRALRAC 599
|
410 420
....*....|....*....|....*...
gi 15596070 489 ---PSsrQLGKRLGVSHTTAANKLRQHG 513
Cdd:COG3284 600 ggnVS--AAARALGISRSTLYRKLKRYG 625
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
197-513 |
7.20e-109 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 330.39 E-value: 7.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 197 RKQELRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETEL 276
Cdd:COG2204 123 LRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 277 FGYGPGAFEGARpEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELC 356
Cdd:COG2204 203 FGHEKGAFTGAV-ARRIGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 357 AKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGlPKLSAQALERLERYHWPGNVRQLENVLFQAV 436
Cdd:COG2204 282 EEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAV 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596070 437 SLCEGGTVKAEHirLPDYgapqplgdfslegdldaiVGRFEKAVLERLFREHPSSR-QLGKRLGVSHTTAANKLRQHG 513
Cdd:COG2204 361 ILADGEVITAED--LPEA------------------LEEVERELIERALEETGGNVsRAAELLGISRRTLYRKLKKYG 418
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
207-375 |
8.64e-87 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 264.65 E-value: 8.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 207 IFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEG 286
Cdd:pfam00158 1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 287 ARPEGKlGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLY 366
Cdd:pfam00158 81 ADSDRK-GLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLY 159
|
....*....
gi 15596070 367 HRLNVLSLH 375
Cdd:pfam00158 160 YRLNVIPIE 168
|
|
| PRK05022 |
PRK05022 |
nitric oxide reductase transcriptional regulator NorR; |
175-502 |
5.06e-82 |
|
nitric oxide reductase transcriptional regulator NorR;
Pssm-ID: 235331 [Multi-domain] Cd Length: 509 Bit Score: 263.96 E-value: 5.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 175 ALAGAVLTL--------HRADRVGERIYHVRKQELRGFDSIFQSSrVMAAVVREARRMAPLDAPLLIEGETGTGKELLAR 246
Cdd:PRK05022 150 ALAAATLRNallieqleSQAELPQDVAEFLRQEALKEGEMIGQSP-AMQQLKKEIEVVAASDLNVLILGETGVGKELVAR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 247 ACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGA---RPeGKLgllELTAGGTLFLDGVGEMSPRLQAKLLRF 323
Cdd:PRK05022 229 AIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAisnRS-GKF---ELADGGTLFLDEIGELPLALQAKLLRV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 324 LQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGC 403
Cdd:PRK05022 305 LQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 404 GLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGG------TVKAEHIRLPDYGA-----PQPLGDFSLEGDLDAI 472
Cdd:PRK05022 385 RSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLARARgagrivTLEAQHLDLPAEVAlpppeAAAAPAAVVSQNLREA 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15596070 473 VGRFEKAVLERLFREHPSS-----RQLG----------KRLGVSH 502
Cdd:PRK05022 465 TEAFQRQLIRQALAQHQGNwaaaaRALEldranlhrlaKRLGLKD 509
|
|
| PEP_resp_reg |
TIGR02915 |
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ... |
182-514 |
1.41e-76 |
|
PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]
Pssm-ID: 274348 [Multi-domain] Cd Length: 445 Bit Score: 247.74 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 182 TLHRADRVGERIYHvrKQELRGFdsiFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMA 261
Cdd:TIGR02915 121 TLETENRRLQSALG--GTALRGL---ITSSPGMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 262 LNCAGLPESMAETELFGYGPGAFEGARPEgKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLD 341
Cdd:TIGR02915 196 INCAAIPENLLESELFGYEKGAFTGAVKQ-TLGKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 342 VRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHW 421
Cdd:TIGR02915 275 VRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAW 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 422 PGNVRQLENVLFQAVSLCEGGTVKAEHIRLPDY-GAPQPlgdfsLEGDLDAIVGRFEK-AVLERLFREHPSSRQLGKRLG 499
Cdd:TIGR02915 355 PGNVRELENKVKRAVIMAEGNQITAEDLGLDAReRAETP-----LEVNLREVRERAEReAVRKAIARVDGNIARAAELLG 429
|
330
....*....|....*
gi 15596070 500 VSHTTAANKLRQHGV 514
Cdd:TIGR02915 430 ITRPTLYDLMKKHGI 444
|
|
| ntrC |
TIGR01818 |
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ... |
214-483 |
2.10e-74 |
|
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]
Pssm-ID: 273818 [Multi-domain] Cd Length: 463 Bit Score: 242.72 E-value: 2.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 214 MAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEgKL 293
Cdd:TIGR01818 143 MQEVFRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTR-RQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 294 GLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLS 373
Cdd:TIGR01818 222 GRFEQADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 374 LHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHI--RL 451
Cdd:TIGR01818 302 IHLPPLRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLpaEL 381
|
250 260 270
....*....|....*....|....*....|..
gi 15596070 452 PDYGAPQPLGDFSLEGDLDAIVGRFEKAVLER 483
Cdd:TIGR01818 382 ALTGRPASAPDSDGQDSWDEALEAWAKQALSR 413
|
|
| phageshock_pspF |
TIGR02974 |
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ... |
210-457 |
1.00e-71 |
|
psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]
Pssm-ID: 274371 [Multi-domain] Cd Length: 329 Bit Score: 231.42 E-value: 1.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 210 SSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARp 289
Cdd:TIGR02974 4 ESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGAQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 290 EGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRL 369
Cdd:TIGR02974 83 KRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 370 NVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGL-PKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEH 448
Cdd:TIGR02974 163 AFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLfPGFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEEAPIDE 242
|
....*....
gi 15596070 449 IRLPDYGAP 457
Cdd:TIGR02974 243 IIIDPFASP 251
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
207-514 |
1.96e-70 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 232.05 E-value: 1.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 207 IFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEG 286
Cdd:PRK11361 145 ILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 287 ARPEgKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLY 366
Cdd:PRK11361 225 AQTL-RQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 367 HRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKA 446
Cdd:PRK11361 304 YRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFS 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596070 447 E----HIRLPDYGA----PQPLGdfslEGDLDAIVGRFEKAVL-ERLFREHPSSRQLGKRLGVSHTTAANKLRQHGV 514
Cdd:PRK11361 384 EdlppQIRQPVCNAgevkTAPVG----ERNLKEEIKRVEKRIImEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
|
|
| PRK10365 |
PRK10365 |
sigma-54-dependent response regulator transcription factor ZraR; |
210-509 |
2.02e-69 |
|
sigma-54-dependent response regulator transcription factor ZraR;
Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 229.15 E-value: 2.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 210 SSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGA-- 287
Cdd:PRK10365 144 KSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGAdk 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 288 RPEGKLglLElTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYH 367
Cdd:PRK10365 224 RREGRF--VE-ADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 368 RLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAE 447
Cdd:PRK10365 301 RLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISER 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596070 448 HIRLPDYGAPQPLGDfslEGDLDAIVGRFEKAVLERLFREHPSSRQLGKRLGVSHTTAANKL 509
Cdd:PRK10365 381 ELPLAIASTPIPLGQ---SQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
|
|
| propionate_PrpR |
TIGR02329 |
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ... |
182-509 |
2.38e-69 |
|
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR. [Regulatory functions, DNA interactions]
Pssm-ID: 274079 [Multi-domain] Cd Length: 526 Bit Score: 231.29 E-value: 2.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 182 TLHRADRVGERIYHVrkqelrgFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMA 261
Cdd:TIGR02329 196 TLRSATRNQLRTRYR-------LDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 262 LNCAGLPESMAETELFGYGPGAFEGARPEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLD 341
Cdd:TIGR02329 269 INCGAIAESLLEAELFGYEEGAFTGARRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVD 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 342 VRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQAL----ERLE 417
Cdd:TIGR02329 349 VRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVLagvaDPLQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 418 RYHWPGNVRQLENVLFQavsLCEGGTVKAEHIRLPDY---GAPQpLGDFSLEGDLDAIvgrfekAVLERLFREHPSSRQL 494
Cdd:TIGR02329 429 RYPWPGNVRELRNLVER---LALELSAMPAGALTPDVlraLAPE-LAEASGKGKTSAL------SLRERSRVEALAVRAA 498
|
330
....*....|....*
gi 15596070 495 GKRLGVSHTTAANKL 509
Cdd:TIGR02329 499 LERFGGDRDAAAKAL 513
|
|
| PRK15115 |
PRK15115 |
response regulator GlrR; Provisional |
205-438 |
3.16e-67 |
|
response regulator GlrR; Provisional
Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 223.56 E-value: 3.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 205 DSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAF 284
Cdd:PRK15115 134 EAIVTRSPLMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 285 EGARPEgKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQD 364
Cdd:PRK15115 214 TGAVSN-REGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFRED 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596070 365 LYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSL 438
Cdd:PRK15115 293 LYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVAL 366
|
|
| PRK15424 |
PRK15424 |
propionate catabolism operon regulatory protein PrpR; Provisional |
173-511 |
1.45e-66 |
|
propionate catabolism operon regulatory protein PrpR; Provisional
Pssm-ID: 237963 [Multi-domain] Cd Length: 538 Bit Score: 224.21 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 173 SEALAGAVLT-LHRADRVGERIYHVRkqelRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLA 251
Cdd:PRK15424 190 EDALDMTRMTlRHNTHYATRNALRTR----YVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 252 SP--------RGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRF 323
Cdd:PRK15424 266 YFarhdarqgKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRV 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 324 LQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIgc 403
Cdd:PRK15424 346 LEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAAL-- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 404 GLPkLSAQALERL-------ERYHWPGNVRQLENvlfqavsLCEggtvkaehiRLPDYGAPQPLGDFSLE---------- 466
Cdd:PRK15424 424 SAP-FSAALRQGLqqcetllLHYDWPGNVRELRN-------LME---------RLALFLSVEPTPDLTPQflqlllpela 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15596070 467 -GDLDAIVGRFEKAVLERLFREHPSSRQLGKR-LGVSHTTAANKLRQ 511
Cdd:PRK15424 487 rESAKTPAPRLLAATLQQALERFNGDKTAAANyLGISRTTLWRRLKA 533
|
|
| glnG |
PRK10923 |
nitrogen regulation protein NR(I); Provisional |
214-431 |
5.07e-65 |
|
nitrogen regulation protein NR(I); Provisional
Pssm-ID: 182842 [Multi-domain] Cd Length: 469 Bit Score: 218.20 E-value: 5.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 214 MAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARpEGKL 293
Cdd:PRK10923 147 MQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGAN-TIRQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 294 GLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLS 373
Cdd:PRK10923 226 GRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIR 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596070 374 LHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENV 431
Cdd:PRK10923 306 VHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENT 363
|
|
| PRK15429 |
PRK15429 |
formate hydrogenlyase transcriptional activator FlhA; |
204-514 |
8.13e-64 |
|
formate hydrogenlyase transcriptional activator FlhA;
Pssm-ID: 237965 [Multi-domain] Cd Length: 686 Bit Score: 220.09 E-value: 8.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 204 FDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGA 283
Cdd:PRK15429 375 FGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 284 FEGARPEgKLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQ 363
Cdd:PRK15429 455 FTGASAQ-RIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRS 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 364 DLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGT 443
Cdd:PRK15429 534 DLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNV 613
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596070 444 VKAEhirLPDYGAPQPlgDFSLEGDLDAIVGRFEKAVLERLFREH----PSSRQLGKRLGVSHTTAANKLRQHGV 514
Cdd:PRK15429 614 LQLS---LPDITLPEP--ETPPAATVVAQEGEDEYQLIVRVLKETngvvAGPKGAAQRLGLKRTTLLSRMKRLGI 683
|
|
| pspF |
PRK11608 |
phage shock protein operon transcriptional activator; Provisional |
217-436 |
1.69e-62 |
|
phage shock protein operon transcriptional activator; Provisional
Pssm-ID: 236936 [Multi-domain] Cd Length: 326 Bit Score: 207.22 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 217 VVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEgKLGLL 296
Cdd:PRK11608 18 VLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKR-HPGRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 297 ELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHI 376
Cdd:PRK11608 97 ERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596070 377 PPLRECLDGLAPLAEHFLDQASRQIGCGL-PKLSAQALERLERYHWPGNVRQLENVLFQAV 436
Cdd:PRK11608 177 PPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVERSV 237
|
|
| FhlA |
COG3604 |
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ... |
218-514 |
3.25e-60 |
|
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 442823 [Multi-domain] Cd Length: 338 Bit Score: 201.61 E-value: 3.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 218 VREARRMAPLDApLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETelfgygpgafegarpegklglle 297
Cdd:COG3604 106 LRLLETLASLAA-VAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES----------------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 298 ltaggtlfldgvgemsprlqakllrfLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIP 377
Cdd:COG3604 162 --------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 378 PLRECLDGLAPLAEHFLDQASRQIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHIRLPDygap 457
Cdd:COG3604 216 PLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGS---- 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596070 458 qplgdfslegdlDAIVGRFEKAVLERLFREHpSSRQLG--KRLGVSHTTAANKLRQHGV 514
Cdd:COG3604 292 ------------REALEEVEREHILEALERT-GGNIAGaaRLLGLTPSTLRSRMKKLGI 337
|
|
| PRK11388 |
PRK11388 |
DNA-binding transcriptional regulator DhaR; Provisional |
95-514 |
3.30e-51 |
|
DNA-binding transcriptional regulator DhaR; Provisional
Pssm-ID: 183114 [Multi-domain] Cd Length: 638 Bit Score: 184.88 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 95 VLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSryvEDLDLPELV-RANKARINGLRVKVKgdvfladiapLQSEHDES 173
Cdd:PRK11388 216 VIAWDEQGNLQFLNAQAARLLRLDATASQGRAIT---ELLTLPAVLqQAIKQAHPLKHVEVT----------FESQGQFI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 174 EAL-----------AGAVLTLHRADRVGERIYHVRKQELRGFDSIFQSSRVMAAVVREARRMAPLDAPLLIEGETGTGKE 242
Cdd:PRK11388 283 DAVitlkpiiegqgTSFILLLHPVEQMRQLMTSQLGKVSHTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 243 LLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGPGAfegaRPEGKLGLLELTAGGTLFLDGVGEMSPRLQAKLLR 322
Cdd:PRK11388 363 LLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDRTD----SENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 323 FLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRECLDGLAPLAEHFLDQASRQIG 402
Cdd:PRK11388 439 VLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFS 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 403 CGLpKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVK----AEHIRLP----DYGAPQPLGDFSLEgdldaivg 474
Cdd:PRK11388 519 TRL-KIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRlsdlPEHLFTEqatdDVSATRLSTSLSLA-------- 589
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15596070 475 RFEKAVLERLFREhpSSRQLG---KRLGVSHTTAANKLRQHGV 514
Cdd:PRK11388 590 ELEKEAIINAAQV--CGGRIQemaALLGIGRTTLWRKMKQHGI 630
|
|
| Regu_Geo_Pelo |
NF038230 |
GPMC system transcriptional regulator; Members of this family are family are sigma ... |
231-487 |
6.83e-40 |
|
GPMC system transcriptional regulator; Members of this family are family are sigma 54-interacting transcriptional regulators of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.
Pssm-ID: 468419 [Multi-domain] Cd Length: 935 Bit Score: 154.44 E-value: 6.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 231 LLIEGETGTGKELLARACH---------LASPRGQSPFMALNCAGLPESMAETELFGYGPGAFEGARPEGKlGLLELTAG 301
Cdd:NF038230 594 ILITGETGSGKEFLFNNLYsrlnemyreQLNPRGELPVKKTNIAAYSGELTYSELFGHKRGAFTGAHADRK-GILEEAHG 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 302 GTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLRE 381
Cdd:NF038230 673 GVVFLDEIGDADPKTQVQLLRFLDNGGFVRLGENQTRFSRVLLVAATNKDLRQLIAEGLFREDLYHRLSELTIEVPSLNE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 382 CLDGLAPLAEHFLDQASR------QIGCGLPKLSAQALERLERYHWPGNVRQLENVLFQAVSLCEGGTVKAEHIRLPDYG 455
Cdd:NF038230 753 RREDIPDLAVHFLGKLYRvyrgpeETEEDPPILSEDAKQLLVQHHYTGNIRELRSILLRALFFRRGRVITGEDIRRALAG 832
|
250 260 270
....*....|....*....|....*....|..
gi 15596070 456 APQPlgDFSLEGDLDAIVGRFEKAVLERLFRE 487
Cdd:NF038230 833 GGAG--SESAAGSAEELAGQLADEILERIERG 862
|
|
| RtcR |
COG4650 |
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ... |
229-498 |
5.04e-32 |
|
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 443688 [Multi-domain] Cd Length: 534 Bit Score: 129.18 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 229 APLLIEGETGTGKELLARACH-LASPRGQ--SPFMALNCAGLPESMAETELFGYGPGAFEGA---RPegklGLLELTAGG 302
Cdd:COG4650 209 APILLTGPTGAGKSQLARRIYeLKKARHQvsGRFVEVNCATLRGDGAMSALFGHVKGAFTGAvsdRA----GLLRSADGG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 303 TLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYLDVRVICATQVDLSELCAKGEFRQDLYHRLNVLSLHIPPLREC 382
Cdd:COG4650 285 VLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAER 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 383 LDGLAPLAEHFLDQASRQIGcGLPKLSAQALERLERY------HWPGNVRQLENVLFQAVSLCEGG-----TVKAEHIRL 451
Cdd:COG4650 365 REDIEPNLDYELARFAREQG-RRVRFNKEARARYLAFatspeaLWSGNFRDLNASVTRMATLAEGGritvaLVDEEIARL 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596070 452 PD--YGAPQPLGDFSLEGDLDAIVG----RFEKAVLE---RLFREHPSSRQLGKRL 498
Cdd:COG4650 444 RRlwQRAEAATGDDLLAELLGAEQAaeldLFDRVQLAaviRVCRRSRSLSEAGRTL 499
|
|
| HTH_TypR |
TIGR04381 |
TyrR family helix-turn-helix domain; This model describes the C-terminal DNA-binding ... |
469-516 |
6.98e-21 |
|
TyrR family helix-turn-helix domain; This model describes the C-terminal DNA-binding helix-turn-helix domain of several regulators of aromatic amino acid metabolism. Examples include TyrR in Escherichia coli and PhhR in Pseudomonas putida. Most members of this family have a sigma-54 interaction domain. [Regulatory functions, DNA interactions]
Pssm-ID: 275174 [Multi-domain] Cd Length: 49 Bit Score: 85.87 E-value: 6.98e-21
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15596070 469 LDAIVGRFEKAVLERLFREHPSSRQLGKRLGVSHTTAANKLRQHGVGQ 516
Cdd:TIGR04381 2 LDEIMKRFEASLLRRLYASYPSTRQLAKRLGVSHTAIANKLREYGIGK 49
|
|
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
230-431 |
2.53e-20 |
|
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 94.79 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 230 PLLIEGETGTGKELLARACH---LASPRGQ--SPFMALNCAGL---PE-SMAEteLFGYGPGAFEGARPEgKLGLLELTA 300
Cdd:COG1221 132 HTLILGPTGVGKSFFAELMYeyaIEIGVLPedAPFVVFNCADYannPQlLMSQ--LFGYVKGAFTGADKD-KEGLIEKAD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 301 GGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVY-LDVRVICATQVDLSElcakgefrqdlyhrlnVL------- 372
Cdd:COG1221 209 GGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKTRkANVRIIFATTEDPES----------------SLlktflrr 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596070 373 ---SLHIPPLREcldglAPLAE------HFLDQASRQIGCGLpKLSAQALERLERYHWPGNVRQLENV 431
Cdd:COG1221 273 ipmVIKLPSLEE-----RSLEErlelikHFFKEEAKRLNKPI-KVSKEVLKALLLYDCPGNIGQLKSD 334
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
214-378 |
3.26e-19 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 84.51 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 214 MAAVVREARRMAPLD--APLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESMAETELFGYGpgafegaRPEG 291
Cdd:cd00009 3 QEEAIEALREALELPppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF-------LVRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 292 KLGLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGCFRRVGSDeevylDVRVICATQVDLSelcakGEFRQDLYHRLNv 371
Cdd:cd00009 76 LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPLL-----GDLDRALYDRLD- 144
|
....*..
gi 15596070 372 LSLHIPP 378
Cdd:cd00009 145 IRIVIPL 151
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
210-379 |
3.41e-16 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 75.46 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 210 SSRVMAAVVREARRMAPLDAPLLIEGETGTGKELLARACHLASPRGQSPFMALNCAGLPESmaetelfgygpgafegarp 289
Cdd:pfam14532 3 ASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLE------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 290 egklgLLELTAGGTLFLDGVGEMSPRLQAKLLRFLQDGcfrrvgsdeEVYlDVRVICATQVDLSELCAKGEFRQDLYHRL 369
Cdd:pfam14532 64 -----LLEQAKGGTLYLKDIADLSKALQKGLLLLLAKA---------EGY-RVRLVCTSSKDLPQLAAAGLFDEQLYFEL 128
|
170
....*....|
gi 15596070 370 NVLSLHIPPL 379
Cdd:pfam14532 129 SALRLHVPPL 138
|
|
| ACT_TyrR |
cd04877 |
N-terminal ACT domain of the TyrR protein; ACT_TyrR: N-terminal ACT domain of the TyrR protein. ... |
1-76 |
4.58e-15 |
|
N-terminal ACT domain of the TyrR protein; ACT_TyrR: N-terminal ACT domain of the TyrR protein. The TyrR protein of Escherichia coli controls the expression of a group of transcription units (TyrR regulon) whose gene products are involved in the biosynthesis or transport of the aromatic amino acids. Binding to specific DNA sequences known as TyrR boxes, the TyrR protein can either activate or repress transcription at different sigma70 promoters. Its regulatory activity occurs in response to intracellular levels of tyrosine, phenylalanine and tryptophan. The TyrR protein consists of an N-terminal region important for transcription activation with an ATP-independent aromatic amino acid binding site (contained within the ACT domain) and is involved in dimerization; a central region with an ATP binding site, an ATP-dependent aromatic amino acid binding site and is involved in hexamerization; and a helix turn helix DNA binding C-terminal region. In solution, in the absence of cofactors or in the presence of phenylalanine alone, the TyrR protein exists as a dimer. However, in the presence of ATP and tyrosine the TyrR protein self-aggregates to form a hexamer. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153149 [Multi-domain] Cd Length: 74 Bit Score: 70.00 E-value: 4.58e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596070 1 MRIKVHCQNRVGILRDILNLLVDYGINVNRGEVggDQGNAIYLLCPNMINLQLQSLRPKLEAVPGVFGVKRVGLMP 76
Cdd:cd04877 1 MRLEITCEDRLGITQEVLDLLVEHNIDLRGIEI--DPKGRIYLNFPTIEFEKLQTLMPEIRRIDGVEDVKTVPYMP 74
|
|
| HTH_50 |
pfam18024 |
Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription ... |
466-514 |
1.42e-10 |
|
Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose major function is to control the expression of genes important in the biosynthesis and transport of aromatic amino acids. This entry represents the C-terminal helix-turn-helix DNA-binding domain of TyrR and related proteins.
Pssm-ID: 407862 [Multi-domain] Cd Length: 50 Bit Score: 56.65 E-value: 1.42e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15596070 466 EGDLDAIVGRFEKAVLERLFREHPSSRQLGKRLGVSHTTAANKLRQHGV 514
Cdd:pfam18024 1 EMSLKEYVSYIERELIGAAYENYKSARKVAKALGLSHTTIANKMKRYGI 49
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
230-369 |
3.65e-09 |
|
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: 55.46 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 230 PLLIEGETGTGKELLARACHLASPRGQSPFMALNC----AGLPESMAETELFGYGPGAFEGARPEGKLGLLELTAGGTLF 305
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLI 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596070 306 LDGVGEMSPRLQAKLLRFLQDgcfRRVGSDEEVYLDVRVICATQ--VDLSELCAKGEFRQDLYHRL 369
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNdeKDLGPALLRRRFDRRIVLLL 146
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
2-65 |
1.52e-06 |
|
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5
Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 45.76 E-value: 1.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596070 2 RIKVHCQNRVGILRDILNLLVDYGINVNRGEVGGDQGNA-IYLLCPNMINLQLQSLRPKLEAVPG 65
Cdd:pfam01842 2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGgIVFVVIVVDEEDLEEVLEALKKLEG 66
|
|
| ACT_RelA-SpoT |
cd04876 |
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
3-71 |
5.18e-06 |
|
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153148 [Multi-domain] Cd Length: 71 Bit Score: 44.36 E-value: 5.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596070 3 IKVHCQNRVGILRDILNLLVDYGINVNRGEVGGDQGN-AIyllcpnmINL--------QLQSLRPKLEAVPGVFGVKR 71
Cdd:cd04876 1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGlAT-------IRLtlevrdleHLARIMRKLRQIPGVIDVRR 71
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
92-149 |
1.00e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 44.55 E-value: 1.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596070 92 DFPVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARING 149
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSG 59
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
94-148 |
1.48e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.77 E-value: 1.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15596070 94 PVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARIN 148
Cdd:smart00091 13 GIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
2-71 |
2.87e-05 |
|
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.
Pssm-ID: 463831 [Multi-domain] Cd Length: 79 Bit Score: 42.16 E-value: 2.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596070 2 RIKVHCQNRVGILRDILNLLVDYGINVNRGEVGGDQGNAIYLLcpnMINL------QLQSLRPKLEAVPGVFGVKR 71
Cdd:pfam13291 7 DLEVEAIDRPGLLADITQVISEEKANIVSVNAKTRKKDGTAEI---KITLevkdveHLERLMAKLRRIPGVIDVER 79
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
95-225 |
3.96e-05 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 46.11 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 95 VLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARINGLRVKVKGD---VFLADIAPLQSEhd 171
Cdd:COG5000 103 VIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRDgrrTLLVRASPLRDD-- 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15596070 172 esealaGAVLTLHRADRVgeriyhVRKQElrgfdsifqssrvMAAVVREARRMA 225
Cdd:COG5000 181 ------GYVIVFDDITEL------LRAER-------------LAAWGELARRIA 209
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
94-201 |
4.53e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 45.61 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 94 PVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYV----EDLDLPELVRANKARINGLRVKVK---GDVFLADI--A 164
Cdd:COG3852 19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFpedsPLRELLERALAEGQPVTEREVTLRrkdGEERPVDVsvS 98
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15596070 165 PLQSEHDESealaGAVLTLH---RADRVGERIYHVRKQEL 201
Cdd:COG3852 99 PLRDAEGEG----GVLLVLRditERKRLERELRRAEKLAA 134
|
|
| SpoT |
COG0317 |
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
2-72 |
1.59e-04 |
|
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 44.38 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596070 2 RIKVHCQNRVGILRDILNLLVDYGINVNRGEVGGDQGN-AIYLLCPNMINL-QLQSLRPKLEAVPGVFGVKRV 72
Cdd:COG0317 648 DIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGtATIRFTVEVRDLdHLARVLRKLRKVPGVISVRRV 720
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
92-184 |
4.62e-04 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 39.71 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 92 DFPVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKARINGLRVKVKGDV--FLADIAPLQSE 169
Cdd:pfam00989 11 PDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVsfRVPDGRPRHVE 90
|
90 100
....*....|....*....|.
gi 15596070 170 ------HDESEALAGAVLTLH 184
Cdd:pfam00989 91 vraspvRDAGGEILGFLGVLR 111
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
230-345 |
6.68e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 39.97 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596070 230 PLLIEGETGTGKELLARacHLASP-RGQSPFMALncagLPESMAETELFG-YGPGAFEGARPEGKLgLLELTAGGTLFLD 307
Cdd:pfam07728 1 GVLLVGPPGTGKTELAE--RLAAAlSNRPVFYVQ----LTRDTTEEDLFGrRNIDPGGASWVDGPL-VRAAREGEIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15596070 308 GVGEMSPRLQAKLLRFLQDGCFRRVGSDEEVYL---DVRVI 345
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLI 114
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
3-45 |
2.10e-03 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 36.50 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15596070 3 IKVHCQNRVGILRDILNLLVDYGINVNRGEVGGDQGNAIYLLC 45
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIF 43
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| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
94-146 |
4.77e-03 |
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PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 35.60 E-value: 4.77e-03
10 20 30 40 50
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gi 15596070 94 PVLSVDMGGQIVAANRAAAQLLGVRVDEVPGIPLSRYVEDLDLPELVRANKAR 146
Cdd:pfam13188 13 GILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELLRELR 65
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| ACT_3PGDH |
cd04901 |
C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in ... |
5-66 |
9.22e-03 |
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C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria; The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153173 Cd Length: 69 Bit Score: 34.79 E-value: 9.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596070 5 VHcQNRVGILRDILNLLVDYGINV------NRGEVGgdqgnaiYllcpNMINL---QLQSLRPKLEAVPGV 66
Cdd:cd04901 5 IH-KNVPGVLGQINTILAEHNINIaaqylqTRGEIG-------Y----VVIDIdseVSEELLEALRAIPGT 63
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