|
Name |
Accession |
Description |
Interval |
E-value |
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
16-490 |
0e+00 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 529.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 16 QQDGALNKRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDGNMLP 95
Cdd:COG1167 8 DSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 96 VNSSNAGEirepkhelsrrgmHLLGYAGASIRQWGAFMPGIPDIASFPHDLWRRIQTRLTRRVRPEQLSYSPIGGCPELQ 175
Cdd:COG1167 88 RAAAAVAA-------------PALRRLLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 176 LALVDYLRvARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPIDVDEQGLAPP-- 253
Cdd:COG1167 155 EAIARYLA-RRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDal 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 254 ETLAPDAAPRLICVTPSHQYPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPALQGLQSQSPVIYIGTFS 333
Cdd:COG1167 234 EAALRRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSFS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 334 KTLYPGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQATLAQFIREGHYAAHIRRMRLLYAKRRALLTSLIEQHLGADY 413
Cdd:COG1167 314 KTLAPGLRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513079 414 VGDSSNAGLHMLLSLPPHVDDVVLSAAILRRGVMVKPLSSYYLQPTQQRGLLLGYASVEEPQMEQAFSVIVACIQAL 490
Cdd:COG1167 394 RVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLREL 470
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
135-483 |
2.24e-70 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 227.99 E-value: 2.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 135 GIPDIASFPHDLWRRIQTRLtrrvRPEQLSYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCN 214
Cdd:cd00609 6 GEPDFPPPPEVLEALAAAAL----RAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRALLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 215 PGDLAWIEDPCYWGIRNVLTINGLRVAPIDVDEQGLAPPETLAPDAA----PRLICVTPsHQYPLGAVMSLARRQRLLAL 290
Cdd:cd00609 82 PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAktpkTKLLYLNN-PNNPTGAVLSEEELEELAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 291 AQEHGCWVVEDDYDSEFRFSGSPIPALQGLQSQSPVIYIGTFSKTLY-PGLRVSYMVLPP-LLAQSLKTAHSELYRGGHW 368
Cdd:cd00609 161 AKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFGlPGLRIGYLIAPPeELLERLKKLLPYTTSGPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 369 LTQATLAQFIREGHyaAHIRRMRLLYAKRRALLTSLIEQHLGADYVGDSsnAGLHMLLSLPPHVDDVVLSAAILRRGVMV 448
Cdd:cd00609 241 LSQAAAAAALDDGE--EHLEELRERYRRRRDALLEALKELGPLVVVKPS--GGFFLWLDLPEGDDEEFLERLLLEAGVVV 316
|
330 340 350
....*....|....*....|....*....|....*
gi 504513079 449 KPLSSYYlqPTQQRGLLLGYASVEEpQMEQAFSVI 483
Cdd:cd00609 317 RPGSAFG--EGGEGFVRLSFATPEE-ELEEALERL 348
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
135-490 |
1.46e-36 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 139.11 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 135 GIPDIASFPHdlwrrIQTRLTRRVRPEQLSYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCN 214
Cdd:COG0436 38 GEPDFPTPDH-----IREAAIEALDDGVTGYTPSAGIPELREAIAAYYKRRYGVDLDPDEILVTNGAKEALALALLALLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 215 PGDLAWIEDPCYWGIRNVLTINGLRVAPIDVD-EQGLAP-PETLAPDAAPR---LICVTPSHqyPLGAVMSLARRQRLLA 289
Cdd:COG0436 113 PGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDeENGFLPdPEALEAAITPRtkaIVLNSPNN--PTGAVYSREELEALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 290 LAQEHGCWVVEDD-YdSEFRFSGSP---IPALQGLQSQspVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSELYr 364
Cdd:COG0436 191 LAREHDLLVISDEiY-EELVYDGAEhvsILSLPGLKDR--TIVINSFSKSYaMTGWRIGYAVGPPELIAALLKLQSNLT- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 365 gghwLTQATLAQFIRE---GHYAAHIRRMRLLYAKRRALLTSLIEQhLGADYVgdSSNAGLHMLLSLPPHV-DDVVLSAA 440
Cdd:COG0436 267 ----SCAPTPAQYAAAaalEGPQDYVEEMRAEYRRRRDLLVEGLNE-IGLSVV--KPEGAFYLFADVPELGlDSEEFAER 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 504513079 441 ILRR-GVMVKPLSSYYlqPTQQRGLLLGYAsVEEPQMEQAFSVIVACIQAL 490
Cdd:COG0436 340 LLEEaGVAVVPGSAFG--PAGEGYVRISYA-TSEERLEEALERLARFLERY 387
|
|
| PRK15481 |
PRK15481 |
transcriptional regulatory protein PtsJ; Provisional |
25-478 |
1.34e-29 |
|
transcriptional regulatory protein PtsJ; Provisional
Pssm-ID: 185378 [Multi-domain] Cd Length: 431 Bit Score: 120.54 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 25 LYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDGNMlpvnssnagei 104
Cdd:PRK15481 10 IFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVAL----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 105 repkhELSRRGMHLLGYAGasirqwgafmpGIPDIASFPhDLWRRIQTRltrrvrpeqlSYSP-IGGCPELQLALVDYLR 183
Cdd:PRK15481 79 -----EGGDPGTPLHDLAG-----------GNPDPQRLP-DLSRYFARL----------SRTPrLYGDAPVSPELHAWAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 184 VARSVECTPEQVLitEGTHQAMDLLAKMLCN---PGDLAWIEDPCYWGIRNVLTINGLRVAPIDVDEQGLApPETL--AP 258
Cdd:PRK15481 132 RWLRDDCPVAFEI--DLTSGAIDAIERLLCAhllPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQ-PEKLerAL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 259 DAAPRLICVTPSHQYPLGAVMSLARRQRLLALAQEH-GCWVVEDDYdsefrFSgspipalqgLQSQSP---VIYIGT--- 331
Cdd:PRK15481 209 AQGARAVILTPRAHNPTGCSLSARRAAALRNLLARYpQVLVIIDDH-----FA---------LLSSSPyhsVIPQTTqrw 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 332 -----FSKTLYPGLRVSYMVLPPLLAQSLKTahsELYRGGHWLTQatLAQFIREGH-----YAAHIRRMRLLYAKRRALL 401
Cdd:PRK15481 275 alirsVSKALGPDLRLAFVASDSATSARLRL---RLNSGTQWVSH--LLQDLVYACltdpeYQARLAQARLFYAQRRQKL 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513079 402 TSLIEQH-LGADYVGDssnaGLHMLLSLPPHVDDVVLSAAilRRGVMVKPLSSYYLQpTQQRGLLLGYASVEEPQMEQ 478
Cdd:PRK15481 350 ARALQQYgIAIPSPGD----GLNLWLPLDTDSQATALTLA--KSGWLVREGEAFGVS-APSHGLRITLSTLNDAEINR 420
|
|
| WHTH_GntR |
cd07377 |
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ... |
23-85 |
3.57e-22 |
|
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.
Pssm-ID: 153418 [Multi-domain] Cd Length: 66 Bit Score: 89.81 E-value: 3.57e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513079 23 KRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVT 85
Cdd:cd07377 4 EQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
162-410 |
7.23e-22 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 97.50 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 162 QLSYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVA 241
Cdd:PRK05764 61 KTKYTPAAGIPELREAIAAKLKRDNGLDYDPSQVIVTTGAKQALYNAFMALLDPGDEVIIPAPYWVSYPEMVKLAGGVPV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 242 PIDVD-EQGLAP-PETLAPDAAPR---LICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDD------YDSEFRFS 310
Cdd:PRK05764 141 FVPTGeENGFKLtVEQLEAAITPKtkaLILNSPSN--PTGAVYSPEELEAIADVAVEHDIWVLSDEiyeklvYDGAEFTS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 311 -GSPIPALQGLqsqspVIYIGTFSKTlY--PGLRVSYMVLPPLLAQSLKTAHSELYRGghwltQATLAQfireghYAA-- 385
Cdd:PRK05764 219 iASLSPELRDR-----TITVNGFSKA-YamTGWRLGYAAGPKELIKAMSKLQSHSTSN-----PTSIAQ------YAAva 281
|
250 260 270
....*....|....*....|....*....|..
gi 504513079 386 -------HIRRMRLLYAKRRALLTSLIEQHLG 410
Cdd:PRK05764 282 alngpqdEVEEMRQAFEERRDLMVDGLNEIPG 313
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
165-483 |
1.47e-21 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 95.84 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPI 243
Cdd:pfam00155 35 YGPTDGHPELREALAKFLGRSPVLKLDREaAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 D--------VDEQGLAPpetlAPDAAPRLICVT-PSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRF-SGSP 313
Cdd:pfam00155 115 PlydsndfhLDFDALEA----ALKEKPKVVLHTsPHN--PTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFgSPDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 314 IPALQGLQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSELYRGGHwLTQATLAQFIREGHYAAHIRRMRL 392
Cdd:pfam00155 189 VATRALLAEGPNLLVVGSFSKAFgLAGWRVGYILGNAAVISQLRKLARPFYSSTH-LQAAAAAALSDPLLVASELEEMRQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 393 LYAKRRALLTSLIeQHLGADYVGdsSNAGLHMLLSLPPHVDDVVLSAAILRRGVMVKPLSSYYLQPTqqrgLLLGYASVE 472
Cdd:pfam00155 268 RIKERRDYLRDGL-QAAGLSVLP--SQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPGVPGW----LRITVAGGT 340
|
330
....*....|.
gi 504513079 473 EPQMEQAFSVI 483
Cdd:pfam00155 341 EEELEELLEAI 351
|
|
| YhcF |
COG1725 |
DNA-binding transcriptional regulator YhcF, GntR family [Transcription]; |
25-87 |
1.58e-21 |
|
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
Pssm-ID: 441331 [Multi-domain] Cd Length: 114 Bit Score: 89.47 E-value: 1.58e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513079 25 LYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQ 87
Cdd:COG1725 15 IADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFVAED 77
|
|
| MngR |
COG2188 |
DNA-binding transcriptional regulator, GntR family [Transcription]; |
23-117 |
8.63e-17 |
|
DNA-binding transcriptional regulator, GntR family [Transcription];
Pssm-ID: 441791 [Multi-domain] Cd Length: 238 Bit Score: 79.52 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 23 KRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDGNMLPVNSsnag 102
Cdd:COG2188 8 LQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLSRLTS---- 83
|
90
....*....|....*
gi 504513079 103 eIREpkhELSRRGMH 117
Cdd:COG2188 84 -FTE---ELRARGRE 94
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
165-356 |
1.69e-16 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 81.16 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPID 244
Cdd:PRK07550 63 YGPVEGLPELREAYAAHYSRLYGAAISPEQVHITSGCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGIRPVYLP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 245 VDEQ-GLAP-PETLAPDAAPR---LICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVED----DYDSEfrfSGSPIP 315
Cdd:PRK07550 143 CDEGpGLLPdPAAAEALITPRtraIALVTPNN--PTGVVYPPELLHELYDLARRHGIALILDetyrDFDSG---GGAPHD 217
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513079 316 ALQGLQSQSPVIYIGTFSKTL-YPGLRVSYMVL-PPLLAQSLK 356
Cdd:PRK07550 218 LFADPDWDDTLVHLYSFSKSYaLTGHRVGAVVAsPARIAEIEK 260
|
|
| HTH_GNTR |
smart00345 |
helix_turn_helix gluconate operon transcriptional repressor; |
25-84 |
4.65e-15 |
|
helix_turn_helix gluconate operon transcriptional repressor;
Pssm-ID: 197669 [Multi-domain] Cd Length: 60 Bit Score: 69.53 E-value: 4.65e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 25 LYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFV 84
Cdd:smart00345 1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
|
|
| GntR |
pfam00392 |
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ... |
23-84 |
6.16e-15 |
|
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.
Pssm-ID: 306822 [Multi-domain] Cd Length: 64 Bit Score: 69.18 E-value: 6.16e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513079 23 KRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFV 84
Cdd:pfam00392 3 EQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
167-456 |
6.71e-15 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 75.94 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 167 PIGGCPELQLALVDYLRVarsvecTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPIDVD 246
Cdd:COG0079 46 PDPDATALREALAEYYGV------PPEQVLVGNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 247 EQGLAPPETL--APDAAPRLICVT----PShqyplGAVMSLARRQRLLALAQEHGcWVVEDD--YDsefrFSGSPIPALQ 318
Cdd:COG0079 120 EDFSLDLDALlaAITERTDLVFLCnpnnPT-----GTLLPREELEALLEALPADG-LVVVDEayAE----FVPEEDSALP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 319 GLQSQSPVIYIGTFSKTlY--PGLRVSYMVLPPLLAQSLKTAHselyrgGHW----LTQATLAQFIREghyAAHIRRMRL 392
Cdd:COG0079 190 LLARYPNLVVLRTFSKA-YglAGLRLGYAIASPELIAALRRVR------GPWnvnsLAQAAALAALED---RAYLEETRA 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513079 393 LYAKRRALLTSLIEQhLGADYVGDSSNaglHMLLSLPPHVDDVVlsAAILRRGVMVKPLSSYYL 456
Cdd:COG0079 260 RLRAERERLAAALRA-LGLTVYPSQAN---FVLVRVPEDAAELF--EALLERGILVRDFSSFGL 317
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
170-355 |
2.50e-14 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 74.59 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 170 GCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPIdvdeqG 249
Cdd:PRK06108 62 GIPELREALARYVSRLHGVATPPERIAVTSSGVQALMLAAQALVGPGDEVVAVTPLWPNLVAAPKILGARVVCV-----P 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 250 LAPPE---TLAPD---AA--PR---LICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRF-SGSPIPA- 316
Cdd:PRK06108 137 LDFGGggwTLDLDrllAAitPRtraLFINSPNN--PTGWTASRDDLRAILAHCRRHGLWIVADEVYERLYYaPGGRAPSf 214
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513079 317 LQGLQSQSPVIYIGTFSKT-LYPGLRVSYMVLPPLLAQSL 355
Cdd:PRK06108 215 LDIAEPDDRIIFVNSFSKNwAMTGWRLGWLVAPPALGQVL 254
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
164-402 |
4.74e-14 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 73.62 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAP 242
Cdd:PRK07682 52 SYTANAGLLELRQEIAKYLKKRFAVSYDPNdEIIVTVGASQALDVAMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 243 I--DVDEQGLAPPETLAPDAAPR----LICvTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDD------YDSEFrfs 310
Cdd:PRK07682 132 VatTLENEFKVQPAQIEAAITAKtkaiLLC-SPNN--PTGAVLNKSELEEIAVIVEKHDLIVLSDEiyaeltYDEAY--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 311 gSPIPALQGLQSQSpvIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSelyrggHWLTQA-TLAQF-----IREGhy 383
Cdd:PRK07682 206 -TSFASIKGMRERT--ILISGFSKGFaMTGWRLGFIAAPVYFSEAMLKIHQ------YSMMCApTMAQFaaleaLRAG-- 274
|
250
....*....|....*....
gi 504513079 384 AAHIRRMRLLYAKRRALLT 402
Cdd:PRK07682 275 NDDVIRMRDSYRKRRNFFV 293
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
165-345 |
8.31e-14 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 72.92 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTI-NGLRVAPI 243
Cdd:PRK08363 66 YGPSEGLPELREAIVKREKRKNGVDITPDDVRVTAAVTEALQLIFGALLDPGDEILIPGPSYPPYTGLVKFyGGVPVEYR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 DVDEQGLAP-PETLAP--DAAPRLICVTPSHQyPLGAVMSLARRQRLLALAQEHGCWVVEDD------YDSEFRFSGSpi 314
Cdd:PRK08363 146 TIEEEGWQPdIDDIRKkiTEKTKAIAVINPNN-PTGALYEKKTLKEILDIAGEHDLPVISDEiydlmtYEGKHVSPGS-- 222
|
170 180 190
....*....|....*....|....*....|..
gi 504513079 315 palqgLQSQSPVIYIGTFSKT-LYPGLRVSYM 345
Cdd:PRK08363 223 -----LTKDVPVIVMNGLSKVyFATGWRLGYI 249
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
164-347 |
1.38e-13 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 72.37 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPI 243
Cdd:TIGR01265 68 GYAPSVGALAAREAVAEYLSSDLPGKLTADDVVLTSGCSQAIEICIEALANPGANILVPRPGFPLYDTRAAFSGLEVRLY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 D--------VDEQGLappETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIP 315
Cdd:TIGR01265 148 DllpekdweIDLDGL---ESLADEKTVAIVVINPSN--PCGSVFSRDHLQKIAEVAEKLGIPIIADEIYGHMVFGDAPFI 222
|
170 180 190
....*....|....*....|....*....|...
gi 504513079 316 ALQGLQSQSPVIYIGTFSKT-LYPGLRVSYMVL 347
Cdd:TIGR01265 223 PMASFASIVPVLSLGGISKRwVVPGWRLGWIII 255
|
|
| FadR |
COG2186 |
DNA-binding transcriptional regulator, FadR family [Transcription]; |
24-91 |
1.47e-13 |
|
DNA-binding transcriptional regulator, FadR family [Transcription];
Pssm-ID: 441789 [Multi-domain] Cd Length: 232 Bit Score: 69.96 E-value: 1.47e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513079 24 RLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDG 91
Cdd:COG2186 11 QVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSPWA 78
|
|
| PLN00143 |
PLN00143 |
tyrosine/nicotianamine aminotransferase; Provisional |
164-346 |
8.71e-13 |
|
tyrosine/nicotianamine aminotransferase; Provisional
Pssm-ID: 165711 [Multi-domain] Cd Length: 409 Bit Score: 70.04 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCY-----WGIRNVLTINGL 238
Cdd:PLN00143 69 SYAPTGGILPARRAIADYLSNDLPYQLSPDDVYLTLGCKHAAEIIIKVLARPEANILLPRPGFpdvetYAIFHHLEIRHF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 239 RVAPIDVDEQGLAPPETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPALQ 318
Cdd:PLN00143 149 DLLPEKGWEVDLDAVEAIADENTIAMVIINPGN--PCGSVYSYEHLNKIAETARKLGILVIADEVYGHIVFGSKPFVPMG 226
|
170 180
....*....|....*....|....*....
gi 504513079 319 GLQSQSPVIYIGTFSKT-LYPGLRVSYMV 346
Cdd:PLN00143 227 LFASIVPVITLGSISKRwMIPGWGLGWLV 255
|
|
| PLN02656 |
PLN02656 |
tyrosine transaminase |
165-346 |
2.36e-11 |
|
tyrosine transaminase
Pssm-ID: 178262 [Multi-domain] Cd Length: 409 Bit Score: 65.33 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPID 244
Cdd:PLN02656 69 YAPTVGLPQARRAIAEYLSRDLPYKLSLDDVFITSGCTQAIDVALSMLARPGANILLPRPGFPIYELCAAFRHLEVRYVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 245 -VDEQG----LAPPETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPALQG 319
Cdd:PLN02656 149 lLPEKGwevdLDAVEALADQNTVALVIINPGN--PCGNVYSYQHLKKIAETAEKLKILVIADEVYGHLAFGSNPFVPMGV 226
|
170 180
....*....|....*....|....*...
gi 504513079 320 LQSQSPVIYIGTFSKT-LYPGLRVSYMV 346
Cdd:PLN02656 227 FGSIVPVLTLGSLSKRwIVPGWRLGWFV 254
|
|
| PRK07681 |
PRK07681 |
LL-diaminopimelate aminotransferase; |
160-450 |
4.76e-11 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 181081 Cd Length: 399 Bit Score: 64.44 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 160 PEQLSYSpIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGL 238
Cdd:PRK07681 61 KESYGYT-LSGIQEFHEAVTEYYNNTHNVILNADkEVLLLMGSQDGLVHLPMVYANPGDIILVPDPGYTAYETGIQMAGA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 239 RVAPIDVDEQ-GLAP-----PETLApDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSG- 311
Cdd:PRK07681 140 TSYYMPLKKEnDFLPdleliPEEIA-DKAKMMILNFPGN--PVPAMAHEDFFKEVIAFAKKHNIIVVHDFAYAEFYFDGn 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 312 SPIPALQGLQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQATLAQFIREGhyAAHIRRM 390
Cdd:PRK07681 217 KPISFLSVPGAKEVGVEINSLSKSYsLAGSRIGYMIGNEEIVRALTQFKSNTDYGVFLPIQKAACAALRNG--AAFCEKN 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513079 391 RLLYAKRRALLTSLIeQHLGadYVGDSSNAGLHMLLSLPPHVDDVVLS-AAILRRGVMVKP 450
Cdd:PRK07681 295 RGIYQERRDTLVDGF-RTFG--WNVDKPAGSMFVWAEIPKGWTSLSFAyALMDRANVVVTP 352
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
160-356 |
1.40e-10 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 62.78 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 160 PEQLSYSPIGGCPELQLALVDYLRVARSVECTPEQ-VLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGL 238
Cdd:PRK05957 56 PENHKYQAVQGIPPLLEAITQKLQQDNGIELNNEQaIVVTAGSNMAFMNAILAITDPGDEIILNTPYYFNHEMAITMAGC 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 239 RVAPIDVDEQGLAPPETLAPDAAPRL-ICVTPSHQYPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPI--P 315
Cdd:PRK05957 136 QPILVPTDDNYQLQPEAIEQAITPKTrAIVTISPNNPTGVVYPEALLRAVNQICAEHGIYHISDEAYEYFTYDGVKHfsP 215
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513079 316 ALQGlQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLK 356
Cdd:PRK05957 216 GSIP-GSGNHTISLYSLSKAYgFASWRIGYMVIPIHLLEAIK 256
|
|
| PRK10421 |
PRK10421 |
DNA-binding transcriptional repressor LldR; Provisional |
21-90 |
1.56e-10 |
|
DNA-binding transcriptional repressor LldR; Provisional
Pssm-ID: 236690 [Multi-domain] Cd Length: 253 Bit Score: 61.71 E-value: 1.56e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 21 LNKRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPD 90
Cdd:PRK10421 3 LSDEVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRWRHET 72
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
135-473 |
4.64e-10 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 61.47 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 135 GIPDiasFPHDlwRRIQTRLTRRVRPEQLSYSPIGGCPELQLALVDylRVARSVECTPE---QVLITEGTHQAmdLLAKM 211
Cdd:PRK09082 38 GFPD---FDGP--PYLVEALAYAMAAGHNQYPPMTGVAALREAIAA--KTARLYGRQYDadsEITVTAGATEA--LFAAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 212 LC--NPGDLAWIEDPCYWGIRNVLTINGLRVAPIDVDEQGLAPP-ETLAPDAAP--RLICVTPSHQyPLGAVMSLARRQR 286
Cdd:PRK09082 109 LAlvRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDwQRFAAAISPrtRLIILNTPHN-PSGTVWSAADMRA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 287 LLALAQEHGCWVVEDD------YDSEFRFSGSPIPalqGLQSQSPViyIGTFSKTLY-PGLRVSYMVLPPLLAQSLKTAH 359
Cdd:PRK09082 188 LWQLIAGTDIYVLSDEvyehivFDGAGHASVLRHP---ELRERAFV--VSSFGKTYHvTGWKVGYCVAPAALSAEFRKVH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 360 SELYRGGHWLTQATLAQFIREghYAAHIRRMRLLYAKRRALLTSLIEQH------------LGADYvgdssnaglhmllS 427
Cdd:PRK09082 263 QYNTFTVNTPAQLALADYLRA--EPEHYLELPAFYQAKRDRFRAALANSrfkllpcegtyfQLVDY-------------S 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504513079 428 LPPHVDDVVLSAAILRR-GVMVKPLSSYYLQPTQQRGLLLGYASVEE 473
Cdd:PRK09082 328 AISDLDDVEFCQWLTREhGVAAIPLSVFYADPFPHRLVRLCFAKQEE 374
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
156-458 |
2.70e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 59.09 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 156 RRVRPEQLSYSPIGGCPELQLALVDYLRvARSVECTPEQVLITEGTHQAMdLLAKM-LCNPGDLAWIEDPCYWGIRNVLT 234
Cdd:PRK07568 53 KNYDEEVLAYSHSQGIPELREAFAKYYK-KWGIDVEPDEILITNGGSEAI-LFAMMaICDPGDEILVPEPFYANYNGFAT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 235 INGLRVAPIDVD-EQGLAPPETLAPDAA--PR----LICvTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEF 307
Cdd:PRK07568 131 SAGVKIVPVTTKiEEGFHLPSKEEIEKLitPKtkaiLIS-NPGN--PTGVVYTKEELEMLAEIAKKHDLFLISDEVYREF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 308 RFSGSP-IPALQ--GLQSQspVIYIGTFSKTlYP--GLRVSYMVL--PPLLAQSLKTAHSElyrgghwLTQATLAQFIRE 380
Cdd:PRK07568 208 VYDGLKyTSALSleGLEDR--VIIIDSVSKR-YSacGARIGCLISknKELIAAAMKLCQAR-------LSPPTLEQIGAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 381 GHYAA---HIRRMRLLYAKRRALLTSLIEQHLGAdYVGDSSNAgLHMLLSLPphVDDVVLSAAIL-------RRGVMVKP 450
Cdd:PRK07568 278 ALLDTpesYFDEVREEYKKRRDILYEELNKIPGV-VCEKPKGA-FYIIAKLP--VDDAEDFAKWLltdfnynGETVMVAP 353
|
....*...
gi 504513079 451 LSSYYLQP 458
Cdd:PRK07568 354 ASGFYATP 361
|
|
| PRK09148 |
PRK09148 |
LL-diaminopimelate aminotransferase; |
122-401 |
3.44e-09 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 181674 [Multi-domain] Cd Length: 405 Bit Score: 58.54 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 122 AGASIRQWGafMpGIPDIASFPHdlwrrIQTRLTRRVR-PEQLSYSPIGGCPELQLALVDYLRVARSVECTPE-QVLITE 199
Cdd:PRK09148 28 AGADIIDLG--M-GNPDLPTPQH-----IVDKLCETAQdPRTHRYSASKGIPGLRRAQAAYYARRFGVKLNPDtQVVATL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 200 GTHQAMDLLAKMLCNPGDLAWIEDPCY----WGirnvLTING--LRVAPIDVDEQGLAPPETLAPDAAPR---LICVTPS 270
Cdd:PRK09148 100 GSKEGFANMAQAITAPGDVILCPNPSYpihaFG----FIMAGgvIRSVPAEPDEEFFPALERAVRHSIPKpiaLIVNYPS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 271 HqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPA-LQGLQSQSPVIYIGTFSKTL-YPGLRVSYMVLP 348
Cdd:PRK09148 176 N--PTAYVADLDFYKDVVAFAKKHDIIILSDLAYSEIYFDGNPPPSvLQVPGAKDVTVEFTSMSKTFsMAGWRMGFAVGN 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513079 349 PLLAQSLKTAHSELYRGGHWLTQATLAqfireghyAA------HIRRMRLLYAKRRALL 401
Cdd:PRK09148 254 ERLIAALTRVKSYLDYGAFTPIQVAAT--------AAlngpqdCIAEMRELYKKRRDVL 304
|
|
| GntR |
COG1802 |
DNA-binding transcriptional regulator, GntR family [Transcription]; |
24-86 |
3.84e-09 |
|
DNA-binding transcriptional regulator, GntR family [Transcription];
Pssm-ID: 441407 [Multi-domain] Cd Length: 222 Bit Score: 56.85 E-value: 3.84e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513079 24 RLYDSIRQAILDGAITAGERLpSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTE 86
Cdd:COG1802 15 QVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAP 76
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
165-398 |
4.12e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 58.58 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPI 243
Cdd:PRK07309 63 YTGMAGLLELRQAAADFVKEKYNLDYAPEnEILVTIGATEALSASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 DVDEQGLA-PPETLA------PDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPA 316
Cdd:PRK07309 143 DTTENDFVlTPEMLEkaileqGDKLKAVILNYPAN--PTGVTYSREQIKALADVLKKYDIFVISDEVYSELTYTGEPHVS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 317 L-QGLQSQspVIYIGTFSKT-LYPGLRVSYMVLPPLLAQSLKTAHSELyrgghwLTQA-TLAQF-----IREGHYAAHIr 388
Cdd:PRK07309 221 IaEYLPDQ--TILINGLSKShAMTGWRIGLIFAPAEFTAQLIKSHQYL------VTAAtTMAQFaaveaLTNGKDDALP- 291
|
250
....*....|
gi 504513079 389 rMRLLYAKRR 398
Cdd:PRK07309 292 -MKKEYIKRR 300
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
165-347 |
4.35e-09 |
|
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273529 [Multi-domain] Cd Length: 401 Bit Score: 58.26 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSvECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPID 244
Cdd:TIGR01264 69 YAPTVGALSAREAIASYYHNPDG-PIEADDVVLCSGCSHAIEMCIAALANAGQNILVPRPGFPLYETLAESMGIEVKLYN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 245 V--DEQ---GLAPPETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPALQG 319
Cdd:TIGR01264 148 LlpDKSweiDLKQLESLIDEKTAALIVNNPSN--PCGSVFSRQHLEEILAVAERQCLPIIADEIYGDMVFSGATFEPLAS 225
|
170 180
....*....|....*....|....*....
gi 504513079 320 LQSQSPVIYIGTFSKT-LYPGLRVSYMVL 347
Cdd:TIGR01264 226 LSSTVPILSCGGLAKRwLVPGWRLGWIII 254
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
165-401 |
4.63e-09 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 58.35 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDP---CYWGIRNVLTINGLRVa 241
Cdd:PRK08361 66 YTPNAGIPELREAIAEYYKKFYGVDVDVDNVIVTAGAYEATYLAFESLLEEGDEVIIPDPafvCYVEDAKIAEAKPIRI- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 242 PIDVDEQGLAPPETL--APDAAPRLICVT-PSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSP-IPAL 317
Cdd:PRK08361 145 PLREENEFQPDPDELleLITKRTRMIVINyPNN--PTGATLDKEVAKAIADIAEDYNIYILSDEPYEHFLYEGAKhYPMI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 318 QglQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQATLAQFIREGHYAAHIRRMRLLYAK 396
Cdd:PRK08361 223 K--YAPDNTILANSFSKTFaMTGWRLGFVIAPEQVIKDMIKLHAYIIGNVASFVQIAGIEALRSKESWKAVEEMRKEYNE 300
|
....*
gi 504513079 397 RRALL 401
Cdd:PRK08361 301 RRKLV 305
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
165-356 |
5.12e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 58.23 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLrvarsvECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPID 244
Cdd:PRK06225 62 YPPPEGFPELRELILKDL------GLDDDEALITAGATESLYLVMRAFLSPGDNAVTPDPGYLIIDNFASRFGAEVIEVP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 245 V-DEQ---GLAPPETLAP-DAAPRLI-CVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVeddYDSEFR-FSGSPIPAL 317
Cdd:PRK06225 136 IySEEcnyKLTPELVKENmDENTRLIyLIDPLN--PLGSSYTEEEIKEFAEIARDNDAFLL---HDCTYRdFAREHTLAA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513079 318 QGLQSQSPVIYigTFSKTL-YPGLRVSYMVLPPLLAQSLK 356
Cdd:PRK06225 211 EYAPEHTVTSY--SFSKIFgMAGLRIGAVVATPDLIEVVK 248
|
|
| pdhR |
PRK09464 |
pyruvate dehydrogenase complex transcriptional repressor PdhR; |
24-88 |
5.35e-09 |
|
pyruvate dehydrogenase complex transcriptional repressor PdhR;
Pssm-ID: 181879 [Multi-domain] Cd Length: 254 Bit Score: 56.95 E-value: 5.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513079 24 RLYDSIRQA----ILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQL 88
Cdd:PRK09464 10 KLSDVIEQQleflILEGTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGGGTFVQSSL 78
|
|
| PRK08175 |
PRK08175 |
aminotransferase; Validated |
132-401 |
8.95e-09 |
|
aminotransferase; Validated
Pssm-ID: 181268 [Multi-domain] Cd Length: 395 Bit Score: 57.41 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 132 FMPGIPDIASFPHdlwrrIQTRLTRRV-RPEQLSYSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLA 209
Cdd:PRK08175 34 FSMGNPDGPTPPH-----IVEKLCEVAqRPDTHGYSTSRGIPRLRRAISRWYQDRYDVDIDPEsEAIVTIGSKEGLAHLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 210 KMLCNPGDLAWIEDPCY----WGIrnVLTINGLRVAPIDVDEQGLAPPETLAPDAAPR---LICVTPSHqyPLGAVMSLA 282
Cdd:PRK08175 109 LATLDHGDTVLVPNPSYpihiYGA--VIAGAQVRSVPLVEGVDFFNELERAIRESYPKpkmMILGFPSN--PTAQCVELE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 283 RRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPA-LQGLQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHS 360
Cdd:PRK08175 185 FFEKVVALAKRYDVLVVHDLAYADIVYDGWKAPSiMQVPGAKDVAVEFFTLSKSYnMAGWRIGFMVGNPELVSALARIKS 264
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504513079 361 ELYRGGHWLTQ-ATLAQFirEGHYAAhIRRMRLLYAKRRALL 401
Cdd:PRK08175 265 YHDYGTFTPLQvAAIAAL--EGDQQC-VRDIAEQYKRRRDVL 303
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
164-414 |
1.23e-08 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 57.04 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAP 242
Cdd:PRK07683 60 SYTHNAGLLELRKAACNFVKDKYDLHYSPEsEIIVTIGASEAIDIAFRTILEPGTEVILPAPIYPGYEPIIRLCGAKPVF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 243 IDVDEQGLA-PPETLAPDAAPRLIC-VTPSHQYPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGS--PIPALQ 318
Cdd:PRK07683 140 IDTRSTGFRlTAEALENAITEKTRCvVLPYPSNPTGVTLSKEELQDIADVLKDKNIFVLSDEIYSELVYEQPhtSIAHFP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 319 GLQSQSpvIYIGTFSKT-LYPGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQATLAQFIREGHYAAHIrrMRLLYAKR 397
Cdd:PRK07683 220 EMREKT--IVINGLSKShSMTGWRIGFLFAPSYLAKHILKVHQYNVTCASSISQYAALEALTAGKDDAKM--MRHQYKKR 295
|
250 260
....*....|....*....|....
gi 504513079 398 RAL----LTSL---IEQHLGADYV 414
Cdd:PRK07683 296 RDYvynrLISMgldVEKPTGAFYL 319
|
|
| PRK11402 |
PRK11402 |
transcriptional regulator PhoB; |
25-111 |
1.36e-08 |
|
transcriptional regulator PhoB;
Pssm-ID: 183118 [Multi-domain] Cd Length: 241 Bit Score: 55.61 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 25 LYDSIRQAILD----GAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDGNMLPVNS-S 99
Cdd:PRK11402 10 LYATVRQRLLDdiaqGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQSQKVENALLTVSGfT 89
|
90
....*....|....
gi 504513079 100 NAGEI--REPKHEL 111
Cdd:PRK11402 90 DFGVSqgKATKEKV 103
|
|
| C_P_lyase_phnF |
TIGR02325 |
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for ... |
20-87 |
4.20e-08 |
|
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond. [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]
Pssm-ID: 131378 [Multi-domain] Cd Length: 238 Bit Score: 54.02 E-value: 4.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513079 20 ALNKRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQ 87
Cdd:TIGR02325 8 ALWRQIADKIEQEIAAGHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGTFVAAR 75
|
|
| PRK10225 |
PRK10225 |
Uxu operon transcriptional regulator; |
16-98 |
6.79e-08 |
|
Uxu operon transcriptional regulator;
Pssm-ID: 182318 [Multi-domain] Cd Length: 257 Bit Score: 53.49 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 16 QQDGALnkrlydsIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQLPDGNMLP 95
Cdd:PRK10225 12 QEVGAM-------IRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAGIYVLDSSGSHNTDS 84
|
...
gi 504513079 96 VNS 98
Cdd:PRK10225 85 PDA 87
|
|
| PRK09764 |
PRK09764 |
GntR family transcriptional regulator; |
23-87 |
1.54e-07 |
|
GntR family transcriptional regulator;
Pssm-ID: 182065 [Multi-domain] Cd Length: 240 Bit Score: 52.52 E-value: 1.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513079 23 KRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEQ 87
Cdd:PRK09764 8 RQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVKEE 72
|
|
| PRK11523 |
PRK11523 |
transcriptional regulator ExuR; |
21-84 |
1.85e-07 |
|
transcriptional regulator ExuR;
Pssm-ID: 183176 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513079 21 LNKRLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFV 84
Cdd:PRK11523 9 LYQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSGIHV 72
|
|
| PRK06107 |
PRK06107 |
aspartate transaminase; |
165-361 |
2.59e-07 |
|
aspartate transaminase;
Pssm-ID: 180403 Cd Length: 402 Bit Score: 52.81 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPcYW-GIRNVLTINGLRvaPI 243
Cdd:PRK06107 66 YTLVNGTPALRKAIIAKLERRNGLHYADNEITVGGGAKQAIFLALMATLEAGDEVIIPAP-YWvSYPDMVLANDGT--PV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 DVD---EQG-LAPPETLAPDAAPR---LICVTPSHqyPLGAVMSLARRQRLLALAQEH-GCWVVEDDYDSEFRFSGSPIP 315
Cdd:PRK06107 143 IVAcpeEQGfKLTPEALEAAITPRtrwLILNAPSN--PTGAVYSRAELRALADVLLRHpHVLVLTDDIYDHIRFDDEPTP 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513079 316 AlqgLQSQSP-----VIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSE 361
Cdd:PRK06107 221 H---LLAAAPelrdrVLVTNGVSKTYaMTGWRIGYAAGPADLIAAINKLQSQ 269
|
|
| PLN02187 |
PLN02187 |
rooty/superroot1 |
164-347 |
7.92e-07 |
|
rooty/superroot1
Pssm-ID: 215119 [Multi-domain] Cd Length: 462 Bit Score: 51.27 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPI 243
Cdd:PLN02187 103 SYGPGAGILPARRAVADYMNRDLPHKLTPEDIFLTAGCNQGIEIVFESLARPNANILLPRPGFPHYDARAAYSGLEVRKF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 D--------VDEQGLappETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIP 315
Cdd:PLN02187 183 DllpekeweIDLEGI---EAIADENTVAMVVINPNN--PCGNVYSHDHLKKVAETARKLGIMVISDEVYDRTIFGDNPFV 257
|
170 180 190
....*....|....*....|....*....|...
gi 504513079 316 ALQGLQSQSPVIYIGTFSKT-LYPGLRVSYMVL 347
Cdd:PLN02187 258 SMGKFASIVPVLTLAGISKGwVVPGWKIGWIAL 290
|
|
| trehalos_R_Bsub |
TIGR02404 |
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ... |
24-84 |
8.14e-07 |
|
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages and does not include the TreR from E. coli. [Regulatory functions, DNA interactions]
Pssm-ID: 274116 [Multi-domain] Cd Length: 233 Bit Score: 50.05 E-value: 8.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513079 24 RLYDSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFV 84
Cdd:TIGR02404 4 QIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYIQKIQGKGSIV 64
|
|
| PRK08636 |
PRK08636 |
LL-diaminopimelate aminotransferase; |
159-450 |
1.77e-06 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 236316 Cd Length: 403 Bit Score: 50.09 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 159 RPEQLSYSPIGGCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTING 237
Cdd:PRK08636 61 KPKTHGYSVSKGIYKLRLAICNWYKRKYNVDLDPEtEVVATMGSKEGYVHLVQAITNPGDVAIVPDPAYPIHSQAFILAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 238 LRVAPI--------DVDEQG-LAPPETLAPDAAPR--LICVTPSHQyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSE 306
Cdd:PRK08636 141 GNVHKMpleynedfELDEDQfFENLEKALRESSPKpkYVVVNFPHN-PTTATVEKSFYERLVALAKKERFYIISDIAYAD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 307 FRFSGSPIPA-LQGLQSQSPVIYIGTFSKTlY--PGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQ--ATLAQfirEG 381
Cdd:PRK08636 220 ITFDGYKTPSiLEVEGAKDVAVESYTLSKS-YnmAGWRVGFVVGNKKLVGALKKIKSWLDYGMFTPIQvaATIAL---DG 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513079 382 HYAAhIRRMRLLYAKRRALltsLIEQHLGADYVGDSSNAGLHMLLSLPP---HVDDVVLSAAILRRG-VMVKP 450
Cdd:PRK08636 296 DQSC-VEEIRETYRKRRDV---LIESFANAGWELQKPRASMFVWAKIPEparHLGSLEFSKQLLTEAkVAVSP 364
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
170-465 |
1.90e-06 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 50.25 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 170 GCPELQLALVDYLRVARSVECTPE-QVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPIDVDEQ 248
Cdd:PLN00175 92 GVPELNSAIAERFKKDTGLVVDPEkEVTVTSGCTEAIAATILGLINPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 249 GLAPPE---TLAPDAAPRLICVTPSHQyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIP--ALQGLQSQ 323
Cdd:PLN00175 172 DFAVPEdelKAAFTSKTRAILINTPHN-PTGKMFTREELELIASLCKENDVLAFTDEVYDKLAFEGDHISmaSLPGMYER 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 324 SPVI-YIG-TFSKTlypGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQATLAQFIR--EGHYAAHIRRmrllYAKRRA 399
Cdd:PLN00175 251 TVTMnSLGkTFSLT---GWKIGWAIAPPHLTWGVRQAHSFLTFATATPMQWAAVAALRapESYYEELKRD----YSAKKD 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513079 400 LLTSlieqhlGADYVG----DSSNAGLHMLLSLPPHVD-DVVLSAAILRR-GVMVKPLSSYYLQPTQQRGLL 465
Cdd:PLN00175 324 ILVE------GLKEVGfkvyPSSGTYFVMVDHTPFGFEnDIAFCEYLIEEvGVAAIPPSVFYLNPEDGKNLV 389
|
|
| PLN00145 |
PLN00145 |
tyrosine/nicotianamine aminotransferase; Provisional |
164-346 |
1.20e-05 |
|
tyrosine/nicotianamine aminotransferase; Provisional
Pssm-ID: 215074 [Multi-domain] Cd Length: 430 Bit Score: 47.46 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 164 SYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPI 243
Cdd:PLN00145 89 SYSTCVGLLPARRAIAEYLSRDLPYELSTDDIYLTAGCAQAIEIIMSVLAQPGANILLPRPGYPLYEARAVFSGLEVRHF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 244 D--------VDEQGLappETLAPDAAPRLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIP 315
Cdd:PLN00145 169 DllpergweVDLEGV---EALADENTVAMVIINPNN--PCGSVYSYEHLAKIAETARKLGILVIADEVYDHLTFGSKPFV 243
|
170 180 190
....*....|....*....|....*....|..
gi 504513079 316 ALQGLQSQSPVIYIGTFSKT-LYPGLRVSYMV 346
Cdd:PLN00145 244 PMGVFGEVAPVLTLGSISKRwVVPGWRLGWIA 275
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
193-336 |
2.04e-05 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 45.07 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 193 EQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNV-LTINGLRVAPIDVDEQG-----LAPPETLAPDAAPRLIC 266
Cdd:cd01494 18 DKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVaAELAGAKPVPVPVDDAGyggldVAILEELKAKPNVALIV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 267 VTPSHQYPLGAVMSLARRqrllALAQEHGCWVVeddYDSEFRFSGSPIPALQGLQSQSPVIYiGTFSKTL 336
Cdd:cd01494 98 ITPNTTSGGVLVPLKEIR----KIAKEYGILLL---VDAASAGGASPAPGVLIPEGGADVVT-FSLHKNL 159
|
|
| PTZ00433 |
PTZ00433 |
tyrosine aminotransferase; Provisional |
165-347 |
3.07e-05 |
|
tyrosine aminotransferase; Provisional
Pssm-ID: 185613 Cd Length: 412 Bit Score: 46.32 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRV------ARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPC---------YWGI 229
Cdd:PTZ00433 71 YPPTVGSPEAREAVATYWRNsfvhkeSLKSTIKKDNVVLCSGVSHAILMALTALCDEGDNILVPAPGfphyetvckAYGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 230 R-NVLTINGLRVAPIDVDE-QGLAPPETLApdaaprLICVTPSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEF 307
Cdd:PTZ00433 151 EmRFYNCRPEKDWEADLDEiRRLVDDRTKA------LIMTNPSN--PCGSNFSRKHVEDIIRLCEELRLPLISDEIYAGM 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513079 308 RFSGSPIPALQGLQSQSPVIYIGTFSKTLY-PGLRVSYMVL 347
Cdd:PTZ00433 223 VFNGATFTSVADFDTTVPRVILGGTAKNLVvPGWRLGWLLL 263
|
|
| PRK09990 |
PRK09990 |
DNA-binding transcriptional regulator GlcC; Provisional |
27-84 |
7.97e-05 |
|
DNA-binding transcriptional regulator GlcC; Provisional
Pssm-ID: 182186 [Multi-domain] Cd Length: 251 Bit Score: 44.37 E-value: 7.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513079 27 DSIRQAILDGAITAGERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFV 84
Cdd:PRK09990 14 ERIERLIVDGVLKVGQALPSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRGSFV 71
|
|
| PRK14999 |
PRK14999 |
histidine utilization repressor; Provisional |
25-117 |
1.47e-04 |
|
histidine utilization repressor; Provisional
Pssm-ID: 184961 [Multi-domain] Cd Length: 241 Bit Score: 43.38 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 25 LYDSIRQAILDgAITAG-----ERLPSSRDLAQQLALSRNTVLTAYEQLLAEGYIEARKGSGTFVTEqlpdgnmlPVNSS 99
Cdd:PRK14999 13 FYETVKQDICK-KIAGGvwqphDRIPSEAELVAQYGFSRMTINRALRELTDEGWLVRLQGVGTFVAE--------PKGQS 83
|
90
....*....|....*....
gi 504513079 100 NAGEIREPKHEL-SRRGMH 117
Cdd:PRK14999 84 ALFEVRSIAEEIaARRHQH 102
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
195-295 |
2.62e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.97 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 195 VLITEGThQAMDLLAKMLCNPGDLAWIEDPC---YWGIRNVLTINGLRVAPIDVDEQGLAPPETLA---------PDAAP 262
Cdd:pfam01212 51 LFVPSGT-AANQLALMAHCQRGDEVICGEPAhihFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEaairevgadIFPPT 129
|
90 100 110
....*....|....*....|....*....|...
gi 504513079 263 RLICVTPSHQYPLGAVMSLARRQRLLALAQEHG 295
Cdd:pfam01212 130 GLISLENTHNSAGGQVVSLENLREIAALAREHG 162
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
135-355 |
3.86e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 42.74 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 135 GIPDIASFPhdlwrRIQTRLTRRVRPEQLSYSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCN 214
Cdd:PRK07337 38 GEPDFTAPE-----PVVEAAARALRRGVTQYTSALGLAPLREAIAAWYARRFGLDVAPERIVVTAGASAALLLACLALVE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 215 PGDLAWIEDPCYWGIRNVLtinglrvapidvdeqglappetLAPDAAPRLICVTPSHQYPLGA-------------VM-- 279
Cdd:PRK07337 113 RGDEVLMPDPSYPCNRHFV----------------------AAAEGRPVLVPSGPAERFQLTAadveaawgertrgVLla 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 280 --------SLARR--QRLLALAQEHGCWVVEDDYDSEFRFSGSPIPALQGLQSqspVIYIGTFSKTL-YPGLRVSYMVLP 348
Cdd:PRK07337 171 spsnptgtSIAPDelRRIVEAVRARGGFTIVDEIYQGLSYDAAPVSALSLGDD---VITINSFSKYFnMTGWRLGWLVVP 247
|
250
....*....|....
gi 504513079 349 PLL-------AQSL 355
Cdd:PRK07337 248 EALvgtfeklAQNL 261
|
|
| PRK08960 |
PRK08960 |
pyridoxal phosphate-dependent aminotransferase; |
165-400 |
1.54e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181595 Cd Length: 387 Bit Score: 40.81 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 165 YSPIGGCPELQLALVDYLRVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTI--NGLRVAP 242
Cdd:PRK08960 65 YTAARGLPALREAIAGFYAQRYGVDVDPERILVTPGGSGALLLASSLLVDPGKHWLLADPGYPCNRHFLRLveGAAQLVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 243 IDVDEQGLAPPETLA----PDAAPRLIcVTPSHqyPLGAVMSLARRQRL-LALAQEHGCWVVEDDYDSefrfSGSPIPAL 317
Cdd:PRK08960 145 VGPDSRYQLTPALVErhwnADTVGALV-ASPAN--PTGTLLSRDELAALsQALRARGGHLVVDEIYHG----LTYGVDAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 318 QGLQSQSPVIYIGTFSKTL-YPGLRVSYMVLPPLLAQSLKTAHSELYRGGHWLTQ-ATLAQF------IREGHYAAHIRR 389
Cdd:PRK08960 218 SVLEVDDDAFVLNSFSKYFgMTGWRLGWLVAPPAAVPELEKLAQNLYISASTPAQhAALACFepetlaILEARRAEFARR 297
|
250
....*....|.
gi 504513079 390 MRLLYAKRRAL 400
Cdd:PRK08960 298 RDFLLPALREL 308
|
|
| PLN02607 |
PLN02607 |
1-aminocyclopropane-1-carboxylate synthase |
192-342 |
2.61e-03 |
|
1-aminocyclopropane-1-carboxylate synthase
Pssm-ID: 215327 [Multi-domain] Cd Length: 447 Bit Score: 40.26 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 192 PEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGI-RNVLTINGLRVAPIDVDE--------QGL--APPETLAPDA 260
Cdd:PLN02607 120 PDRIVLTAGATAANELLTFILADPGDALLVPTPYYPGFdRDLRWRTGVKIVPIHCDSsnnfqvtpQALeaAYQEAEAANI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 261 APRLICVT-PSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYDSEFRFSGSPIPAL------QGLQSQSPVIYI-GTF 332
Cdd:PLN02607 200 RVRGVLITnPSN--PLGATVQRSVLEDILDFVVRKNIHLVSDEIYSGSVFSASEFVSVaeiveaRGYKGVAERVHIvYSL 277
|
170
....*....|.
gi 504513079 333 SKTL-YPGLRV 342
Cdd:PLN02607 278 SKDLgLPGFRV 288
|
|
| PRK05166 |
PRK05166 |
histidinol-phosphate transaminase; |
183-450 |
2.69e-03 |
|
histidinol-phosphate transaminase;
Pssm-ID: 179950 Cd Length: 371 Bit Score: 40.12 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 183 RVARSVECTPEQVLITEGTHQAMDLLAKMLCNPGDLAWIEDPCYWGIRNVLTINGLRVAPIDV-DEQGLAPPETLAPDA- 260
Cdd:PRK05166 79 AIAARTGVPADRIILGNGSEDLIAVICRAVLRPGDRVVTLYPSFPLHEDYPTMMGARVERVTVtPDLGFDLDALCAAVAr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 261 APRLICVT-PSHqyPLGAVMSLARRQRLLALAQEHGCWVVEDDYdSEFRFSGSPIPALQGLQSQS-PVIYIGTFSKTL-Y 337
Cdd:PRK05166 159 APRMLMFSnPSN--PVGSWLTADQLARVLDATPPETLIVVDEAY-AEYAAGDDYPSALTLLKARGlPWIVLRTFSKAYgL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513079 338 PGLRVSY-MVLPPLLAQSLKTAHSELYRGGHWLtQATLAQFIREGHYAahiRRMRLLYAKRRALLTSLIEqhLGADYVGD 416
Cdd:PRK05166 236 AGLRVGYgLVSDPELVGLLDRVRTPFNVNGAAQ-AAALAALDDEEHLA---KGVALALAERERLKKELAE--MGYRIAPS 309
|
250 260 270
....*....|....*....|....*....|....
gi 504513079 417 SSNaglhmLLSLPPHVDDVVLSAAILRRGVMVKP 450
Cdd:PRK05166 310 RAN-----FLFFDARRPASAVAEALLRQGVIVKP 338
|
|
| Lrp |
COG1522 |
DNA-binding transcriptional regulator, Lrp family [Transcription]; |
27-75 |
5.67e-03 |
|
DNA-binding transcriptional regulator, Lrp family [Transcription];
Pssm-ID: 441131 [Multi-domain] Cd Length: 138 Bit Score: 37.07 E-value: 5.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 504513079 27 DSIRQAILDgAITAGERLPSsRDLAQQLALSRNTVLTAYEQLLAEGYIE 75
Cdd:COG1522 4 DEIDRRILR-LLQEDGRLSF-AELAERVGLSESTVLRRVRRLEEAGVIR 50
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
29-74 |
6.33e-03 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 34.72 E-value: 6.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 504513079 29 IRQAILDgAITAGERLpSSRDLAQQLALSRNTVLTAYEQLLAEGYI 74
Cdd:pfam13412 2 TDRKILN-LLQENPRI-SQRELAERLGLSPSTVNRRLKRLEEEGVI 45
|
|
| |
