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Conserved domains on  [gi|906389112|gb|KNB75864|]
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GntR family transcriptional regulator [Bacillus subtilis]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 11439382)

pyridoxal phosphate (PLP)-dependent aminotransferase family protein may catalyze the reversible exchange of an amino group from one molecule with a keto group from another molecule

CATH:  3.40.640.10
Gene Ontology:  GO:0030170
PubMed:  17109392
SCOP:  4000670

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 1-462 2.24e-169

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: 484.72  E-value: 2.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112   1 MDITpfLNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF--- 77
Cdd:COG1167    1 MLIR--LDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFvaa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  78 -ADYHDSDFAYDRMPSTTPIQQEAEENKQWIDFHYGNVDSSYFPFSAWRKSMVNSLDQYGHELYRPGHVLGEFELRTLIA 156
Cdd:COG1167   79 rLPAPAPAPRAAAAVAAPALRRLLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 157 EYLYQsRGVHCGPEQVIIGAGNPILLQILCQVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGICI----QKI 231
Cdd:COG1167  159 RYLAR-RGVPASPDQILITSGAQQALDLALRALlRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLdaleAAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 232 KEQQPNLVYVTPSHQFTLGTIMTINRRIQLLKWAAENQSFIIEDDYDGEFRYTGQPVPSLQGLDQHNRVIYMGTFSKSLL 311
Cdd:COG1167  238 RRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSFSKTLA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 312 PSLRISYMILPSPLLkkgHEITSLyKQTVSCHS----QLTLAEFIKNGEWQKHINRMRKLYRKKRAIVLEAVQRELGEHV 387
Cdd:COG1167  318 PGLRLGYLVAPGRLI---ERLARL-KRATDLGTspltQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGL 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906389112 388 RIRGENSGLRILLDVYLPFGEKELIEKAKKHGVKIYPVSLSYQHHPPTKTVSLGFAGVSESDIREGIKKLKAAWK 462
Cdd:COG1167  394 RVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLR 468
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 1-462 2.24e-169

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: 484.72  E-value: 2.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112   1 MDITpfLNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF--- 77
Cdd:COG1167    1 MLIR--LDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFvaa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  78 -ADYHDSDFAYDRMPSTTPIQQEAEENKQWIDFHYGNVDSSYFPFSAWRKSMVNSLDQYGHELYRPGHVLGEFELRTLIA 156
Cdd:COG1167   79 rLPAPAPAPRAAAAVAAPALRRLLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 157 EYLYQsRGVHCGPEQVIIGAGNPILLQILCQVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGICI----QKI 231
Cdd:COG1167  159 RYLAR-RGVPASPDQILITSGAQQALDLALRALlRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLdaleAAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 232 KEQQPNLVYVTPSHQFTLGTIMTINRRIQLLKWAAENQSFIIEDDYDGEFRYTGQPVPSLQGLDQHNRVIYMGTFSKSLL 311
Cdd:COG1167  238 RRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSFSKTLA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 312 PSLRISYMILPSPLLkkgHEITSLyKQTVSCHS----QLTLAEFIKNGEWQKHINRMRKLYRKKRAIVLEAVQRELGEHV 387
Cdd:COG1167  318 PGLRLGYLVAPGRLI---ERLARL-KRATDLGTspltQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGL 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906389112 388 RIRGENSGLRILLDVYLPFGEKELIEKAKKHGVKIYPVSLSYQHHPPTKTVSLGFAGVSESDIREGIKKLKAAWK 462
Cdd:COG1167  394 RVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLR 468
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 107-459 2.80e-66

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: 216.44  E-value: 2.80e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 107 IDFHYGNVDSSYFPFSAWRKSmvnsLDQYGHELYRPGHVLGEFELRTLIAEYLYQSRGVHCGPEQVIIGAGNPILLQILC 186
Cdd:cd00609    1 IDLSIGEPDFPPPPEVLEALA----AAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 187 QVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGIC------IQKIKEQQPNLVYVTPSHQFTlGTIMTINRRI 259
Cdd:cd00609   77 RALlNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlldlelLEAAKTPKTKLLYLNNPNNPT-GAVLSEEELE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 260 QLLKWAAENQSFIIEDDYDGEFRYTGQPVPSLQGLDQHNRVIYMGTFSKSL-LPSLRISYMILPSPLLKkgHEITSLYKQ 338
Cdd:cd00609  156 ELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPPEELL--ERLKKLLPY 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 339 TVSC---HSQLTLAEFIKNGEwqKHINRMRKLYRKKRAIVLEAVQRELGEHVRIrgENSGLRILLDVYLPFGEKELIEKA 415
Cdd:cd00609  234 TTSGpstLSQAAAAAALDDGE--EHLEELRERYRRRRDALLEALKELGPLVVVK--PSGGFFLWLDLPEGDDEEFLERLL 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 906389112 416 KKHGVKIYPvsLSYQHHPPTKTVSLGFAGvSESDIREGIKKLKA 459
Cdd:cd00609  310 LEAGVVVRP--GSAFGEGGEGFVRLSFAT-PEEELEEALERLAE 350
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 28-382 1.34e-13

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 72.39  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  28 HRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWFADYHDSDFAYDRMPSTTPIqqeaeenkqwI 107
Cdd:PRK15481  19 QAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPGTPL----------H 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 108 DFHYGNVDSSYFPfsawrksmvnSLDQY-GHELYRPgHVLGEFELRTLIAEYLYQSRGVHCGPE---QVIIGAGNPIlLQ 183
Cdd:PRK15481  89 DLAGGNPDPQRLP----------DLSRYfARLSRTP-RLYGDAPVSPELHAWAARWLRDDCPVAfeiDLTSGAIDAI-ER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 184 ILCQVFEPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGICIQKIKEQQPN---LVYVTPSHQFTLGTIMTINR--R 258
Cdd:PRK15481 157 LLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQgarAVILTPRAHNPTGCSLSARRaaA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 259 IQLLkWAAENQSFIIEDDYdgeFRYT-GQPV-PSLQGLDQHNRVIYmgTFSKSLLPSLRISYM---ILPSPLLKK----G 329
Cdd:PRK15481 237 LRNL-LARYPQVLVIIDDH---FALLsSSPYhSVIPQTTQRWALIR--SVSKALGPDLRLAFVasdSATSARLRLrlnsG 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 906389112 330 HEITSLYKQTVSChSQLTLAEFikngewQKHINRMRKLYRKKRAIVLEAVQRE 382
Cdd:PRK15481 311 TQWVSHLLQDLVY-ACLTDPEY------QARLAQARLFYAQRRQKLARALQQY 356
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 15-77 1.42e-12

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: 62.25  E-value: 1.42e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 906389112   15 LYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTF 63
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-77 2.20e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 61.82  E-value: 2.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 906389112    19 LYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTF 59
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
 16-68 8.28e-03

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: 37.73  E-value: 8.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 906389112   16 YQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYI 68
Cdd:TIGR02404   2 YEQIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYI 54
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 1-462 2.24e-169

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: 484.72  E-value: 2.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112   1 MDITpfLNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF--- 77
Cdd:COG1167    1 MLIR--LDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFvaa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  78 -ADYHDSDFAYDRMPSTTPIQQEAEENKQWIDFHYGNVDSSYFPFSAWRKSMVNSLDQYGHELYRPGHVLGEFELRTLIA 156
Cdd:COG1167   79 rLPAPAPAPRAAAAVAAPALRRLLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 157 EYLYQsRGVHCGPEQVIIGAGNPILLQILCQVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGICI----QKI 231
Cdd:COG1167  159 RYLAR-RGVPASPDQILITSGAQQALDLALRALlRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLdaleAAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 232 KEQQPNLVYVTPSHQFTLGTIMTINRRIQLLKWAAENQSFIIEDDYDGEFRYTGQPVPSLQGLDQHNRVIYMGTFSKSLL 311
Cdd:COG1167  238 RRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSFSKTLA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 312 PSLRISYMILPSPLLkkgHEITSLyKQTVSCHS----QLTLAEFIKNGEWQKHINRMRKLYRKKRAIVLEAVQRELGEHV 387
Cdd:COG1167  318 PGLRLGYLVAPGRLI---ERLARL-KRATDLGTspltQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGL 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906389112 388 RIRGENSGLRILLDVYLPFGEKELIEKAKKHGVKIYPVSLSYQHHPPTKTVSLGFAGVSESDIREGIKKLKAAWK 462
Cdd:COG1167  394 RVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLR 468
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 107-459 2.80e-66

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: 216.44  E-value: 2.80e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 107 IDFHYGNVDSSYFPFSAWRKSmvnsLDQYGHELYRPGHVLGEFELRTLIAEYLYQSRGVHCGPEQVIIGAGNPILLQILC 186
Cdd:cd00609    1 IDLSIGEPDFPPPPEVLEALA----AAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 187 QVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGIC------IQKIKEQQPNLVYVTPSHQFTlGTIMTINRRI 259
Cdd:cd00609   77 RALlNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlldlelLEAAKTPKTKLLYLNNPNNPT-GAVLSEEELE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 260 QLLKWAAENQSFIIEDDYDGEFRYTGQPVPSLQGLDQHNRVIYMGTFSKSL-LPSLRISYMILPSPLLKkgHEITSLYKQ 338
Cdd:cd00609  156 ELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPPEELL--ERLKKLLPY 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 339 TVSC---HSQLTLAEFIKNGEwqKHINRMRKLYRKKRAIVLEAVQRELGEHVRIrgENSGLRILLDVYLPFGEKELIEKA 415
Cdd:cd00609  234 TTSGpstLSQAAAAAALDDGE--EHLEELRERYRRRRDALLEALKELGPLVVVK--PSGGFFLWLDLPEGDDEEFLERLL 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 906389112 416 KKHGVKIYPvsLSYQHHPPTKTVSLGFAGvSESDIREGIKKLKA 459
Cdd:cd00609  310 LEAGVVVRP--GSAFGEGGEGFVRLSFAT-PEEELEEALERLAE 350
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 14-77 1.09e-18

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: 79.80  E-value: 1.09e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906389112  14 PLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:cd07377    1 PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTF 64
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 107-384 2.10e-18

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: 86.72  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 107 IDFHYGNVDssyFPFSAW-RKSMVNSLDQyGHELYrpGHVLGEFELRTLIAEYLYQSRGVHCGPEQVIIGAG-NPILLQI 184
Cdd:COG0436   33 IDLGIGEPD---FPTPDHiREAAIEALDD-GVTGY--TPSAGIPELREAIAAYYKRRYGVDLDPDEILVTNGaKEALALA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 185 LCQVFEPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEG---ICIQKIKEQ-QPN---LVYVTPShqftlGTIMTINR 257
Cdd:COG0436  107 LLALLNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgflPDPEALEAAiTPRtkaIVLNSPNnp--tGAVYSREE 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 258 RIQLLKWAAENQSFIIEDD-YDgEFRYTGQPVPS-LQGLDQHNRVIYMGTFSKSL-LPSLRISYMILPSPLLKkghEITS 334
Cdd:COG0436  185 LEALAELAREHDLLVISDEiYE-ELVYDGAEHVSiLSLPGLKDRTIVINSFSKSYaMTGWRIGYAVGPPELIA---ALLK 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 906389112 335 LYKQTVSC---HSQLTLAEFIKNGewQKHINRMRKLYRKKRAIVLEAVqRELG 384
Cdd:COG0436  261 LQSNLTSCaptPAQYAAAAALEGP--QDYVEEMRAEYRRRRDLLVEGL-NEIG 310
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
7-77 7.16e-17

DNA-binding transcriptional regulator YhcF, GntR family [Transcription];


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 76.37  E-value: 7.16e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906389112   7 LNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:COG1725    3 IDFDSGVPIYEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTF 73
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
13-77 8.72e-15

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 73.74  E-value: 8.72e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906389112  13 IPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:COG2188    4 VPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTF 68
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 28-382 1.34e-13

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 72.39  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  28 HRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWFADYHDSDFAYDRMPSTTPIqqeaeenkqwI 107
Cdd:PRK15481  19 QAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPGTPL----------H 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 108 DFHYGNVDSSYFPfsawrksmvnSLDQY-GHELYRPgHVLGEFELRTLIAEYLYQSRGVHCGPE---QVIIGAGNPIlLQ 183
Cdd:PRK15481  89 DLAGGNPDPQRLP----------DLSRYfARLSRTP-RLYGDAPVSPELHAWAARWLRDDCPVAfeiDLTSGAIDAI-ER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 184 ILCQVFEPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGICIQKIKEQQPN---LVYVTPSHQFTLGTIMTINR--R 258
Cdd:PRK15481 157 LLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQgarAVILTPRAHNPTGCSLSARRaaA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 259 IQLLkWAAENQSFIIEDDYdgeFRYT-GQPV-PSLQGLDQHNRVIYmgTFSKSLLPSLRISYM---ILPSPLLKK----G 329
Cdd:PRK15481 237 LRNL-LARYPQVLVIIDDH---FALLsSSPYhSVIPQTTQRWALIR--SVSKALGPDLRLAFVasdSATSARLRLrlnsG 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 906389112 330 HEITSLYKQTVSChSQLTLAEFikngewQKHINRMRKLYRKKRAIVLEAVQRE 382
Cdd:PRK15481 311 TQWVSHLLQDLVY-ACLTDPEY------QARLAQARLFYAQRRQKLARALQQY 356
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 143-377 1.20e-12

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 69.00  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 143 GHVLGEFELRTLIAEYLYQSRGVHCGPEQVIIGAG-NPILLQILCQVFEPnisiGYE----DPG---YPRARKIFEAnrm 214
Cdd:PRK05764  65 TPAAGIPELREAIAAKLKRDNGLDYDPSQVIVTTGaKQALYNAFMALLDP----GDEviipAPYwvsYPEMVKLAGG--- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 215 niVPIPVD---DEGICI------QKIKEQQPNLVYVTPSHQfTlGTIMTINRRIQLLKWAAENQSFIIEDD------YDG 279
Cdd:PRK05764 138 --VPVFVPtgeENGFKLtveqleAAITPKTKALILNSPSNP-T-GAVYSPEELEAIADVAVEHDIWVLSDEiyeklvYDG 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 280 EFRYT-GQPVPSLqgldqHNRVIYMGTFSKSL-LPSLRISYMILPSPLLKKgheITSLYKQTVSCHSQLT----LAEFik 353
Cdd:PRK05764 214 AEFTSiASLSPEL-----RDRTITVNGFSKAYaMTGWRLGYAAGPKELIKA---MSKLQSHSTSNPTSIAqyaaVAAL-- 283

                        250       260
                 ....*....|....*....|....
gi 906389112 354 NGEwQKHINRMRKLYRKKRAIVLE 377
Cdd:PRK05764 284 NGP-QDEVEEMRQAFEERRDLMVD 306
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 15-77 1.42e-12

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: 62.25  E-value: 1.42e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 906389112   15 LYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTF 63
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-77 2.20e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 61.82  E-value: 2.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 906389112    19 LYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTF 59
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 149-387 7.63e-12

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: 66.31  E-value: 7.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 149 FELRTLIAEYLyqsrgvHCGPEQVIIGAGNPILLQILCQVF-EPNISIGYEDPGYPRARKIFEANRMNIVPIPVDDE-GI 226
Cdd:COG0079   51 TALREALAEYY------GVPPEQVLVGNGSDELIQLLARAFlGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDEDfSL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 227 CIQKIKEQ---QPNLVYVT----PShqftlGTIMTINRRIQLLKWAAENQSFIIedD--YdGEFryTGQPVPSLQGLDQH 297
Cdd:COG0079  125 DLDALLAAiteRTDLVFLCnpnnPT-----GTLLPREELEALLEALPADGLVVV--DeaY-AEF--VPEEDSALPLLARY 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 298 NRVIYMGTFSKSL-LPSLRISYMILPSPLLKKGHEITSLYkqTVSCHSQLTLAEFIKNGEWQKhinRMRKLYRKKRAIVL 376
Cdd:COG0079  195 PNLVVLRTFSKAYgLAGLRLGYAIASPELIAALRRVRGPW--NVNSLAQAAALAALEDRAYLE---ETRARLRAERERLA 269

                        250
                 ....*....|.
gi 906389112 377 EAVqRELGEHV 387
Cdd:COG0079  270 AAL-RALGLTV 279
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
115-457 3.39e-10

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 61.55  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  115 DSSYFPFSAWRKSMVNSLDQYGHELYRPGHVLGEFelRTLIAEYLYQSRGVHCGPE-QVIIGAGNPILLQILCQVF-EPN 192
Cdd:pfam00155  10 EYLGDTLPAVAKAEKDALAGGTRNLYGPTDGHPEL--REALAKFLGRSPVLKLDREaAVVFGSGAGANIEALIFLLaNPG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  193 ISIGYEDPGYPRARKIFEANRMNIVPIPVDDEGIC------IQKIKEQQPNLVYVT-PSHqfTLGTIMTINRRIQLLKWA 265
Cdd:pfam00155  88 DAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFhldfdaLEAALKEKPKVVLHTsPHN--PTGTVATLEELEKLLDLA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  266 AENQSFIIEDDYDGEFRYTGQ-PVPSLQGLDQHNRVIYMGTFSKSL-LPSLRISYMILPSPLLKKGHEITSLYkqTVSCH 343
Cdd:pfam00155 166 KEHNILLLVDEAYAGFVFGSPdAVATRALLAEGPNLLVVGSFSKAFgLAGWRVGYILGNAAVISQLRKLARPF--YSSTH 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112  344 SQLTLAEFIKNGE-WQKHINRMRKLYRKKRAIVLEAVQrELGehVRIRGENSGLrILLDVYLPFGEKELIEK-AKKHGVK 421
Cdd:pfam00155 244 LQAAAAAALSDPLlVASELEEMRQRIKERRDYLRDGLQ-AAG--LSVLPSQAGF-FLLTGLDPETAKELAQVlLEEVGVY 319

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 906389112  422 IYPVSlsyqhhPPTKTVSL--GFAGVSESDIREGIKKL 457
Cdd:pfam00155 320 VTPGS------SPGVPGWLriTVAGGTEEELEELLEAI 351
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
1-77 2.21e-07

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 51.46  E-value: 2.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906389112   1 MDITPFLNRTldiPLYQQLYRYFKENMHRGRIQKGMKLpSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:COG1802    1 MTSPSPLRRE---SLAEQVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGAR 73
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
15-77 3.87e-07

DNA-binding transcriptional regulator, FadR family [Transcription];


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 51.09  E-value: 3.87e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 906389112  15 LYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWF 77
Cdd:COG2186    8 LAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTF 70
PRK11523 PRK11523
transcriptional regulator ExuR;
15-75 3.09e-06

transcriptional regulator ExuR;


Pssm-ID: 183176 [Multi-domain]  Cd Length: 253  Bit Score: 48.30  E-value: 3.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906389112  15 LYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSG 75
Cdd:PRK11523   9 LYQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSG 69
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
 32-106 3.88e-06

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 48.22  E-value: 3.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906389112  32 IQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWFADYHDSDFAYDRMpsTTPIQQEAEENKQW 106
Cdd:PRK10421  20 LEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRWRHETWSEQNI--VQPLKTLMADDPDY 92
PRK03317 PRK03317
histidinol-phosphate aminotransferase; Provisional
 150-308 7.91e-06

histidinol-phosphate aminotransferase; Provisional


Pssm-ID: 235115  Cd Length: 368  Bit Score: 47.94  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 150 ELRTLIAEYLYQSRGVHCGPEQVIIGAG-NPILLQILcQVFE-PNIS-IGYEdPGYPRARKIFEANRMNIVPIP-VDDEG 225
Cdd:PRK03317  69 ALRADLAAYLTAQTGVGLTVENVWAANGsNEILQQLL-QAFGgPGRTaLGFV-PSYSMHPIIARGTHTEWVEGPrAADFT 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 226 I----CIQKIKEQQPNLVYVT----PShqftlGTIMTIN--RRIqllkwAAENQSFIIEDDYDGEFRYTGQPvPSLQGLD 295
Cdd:PRK03317 147 LdvdaAVAAIAEHRPDVVFLTspnnPT-----GTALPLDdvEAI-----LDAAPGIVVVDEAYAEFRRSGTP-SALTLLP 215

                        170
                 ....*....|...
gi 906389112 296 QHNRVIYMGTFSK 308
Cdd:PRK03317 216 EYPRLVVSRTMSK 228
PRK11402 PRK11402
transcriptional regulator PhoB;
7-80 7.33e-05

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 44.06  E-value: 7.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906389112   7 LNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSGWFADY 80
Cdd:PRK11402   2 TDRYSHQLLYATVRQRLLDDIAQGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQS 75
PRK09764 PRK09764
GntR family transcriptional regulator;
14-75 5.30e-04

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 41.35  E-value: 5.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906389112  14 PLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIVSKPRSG 75
Cdd:PRK09764   5 PLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSG 66
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
147-384 1.55e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 40.86  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 147 GEFELRTLIAEYLYQSRGVHCGPEQ---VIIGAGNPI---LLQILcqvfEPNISIGYEDPGYPRARKIFEANRMNIVPIP 220
Cdd:PRK07309  68 GLLELRQAAADFVKEKYNLDYAPENeilVTIGATEALsasLTAIL----EPGDKVLLPAPAYPGYEPIVNLVGAEIVEID 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 221 VDDEGICI------QKIKEQQPNLVYVT---PSHQftlgTIMTINR-RIQ-LLKWAAENQSFIIEDDYDGEFRYTGQPVP 289
Cdd:PRK07309 144 TTENDFVLtpemleKAILEQGDKLKAVIlnyPANP----TGVTYSReQIKaLADVLKKYDIFVISDEVYSELTYTGEPHV 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 290 SLQGLdQHNRVIYMGTFSKS-LLPSLRISYMILPSPL---LKKGHEitslYKQTV-SCHSQLTLAEFIKNGewQKHINRM 364
Cdd:PRK07309 220 SIAEY-LPDQTILINGLSKShAMTGWRIGLIFAPAEFtaqLIKSHQ----YLVTAaTTMAQFAAVEALTNG--KDDALPM 292

                        250       260
                 ....*....|....*....|
gi 906389112 365 RKLYRKKRAIVLEAVQrELG 384
Cdd:PRK07309 293 KKEYIKRRDYIIEKMT-DLG 311
PRK08960 PRK08960
pyridoxal phosphate-dependent aminotransferase;
136-224 2.53e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181595  Cd Length: 387  Bit Score: 40.04  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906389112 136 GHELYRPGhvLGEFELRTLIAEYLYQSRGVHCGPEQVII--GAGNPILLQILCQVfEPNISIGYEDPGYPRARKIFEANR 213
Cdd:PRK08960  61 GHTRYTAA--RGLPALREAIAGFYAQRYGVDVDPERILVtpGGSGALLLASSLLV-DPGKHWLLADPGYPCNRHFLRLVE 137

                         90
                 ....*....|.
gi 906389112 214 MNIVPIPVDDE 224
Cdd:PRK08960 138 GAAQLVPVGPD 148
PRK14999 PRK14999
histidine utilization repressor; Provisional
 4-69 8.23e-03

histidine utilization repressor; Provisional


Pssm-ID: 184961 [Multi-domain]  Cd Length: 241  Bit Score: 37.99  E-value: 8.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 906389112   4 TPFLNRTLDIPLYQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYIV 69
Cdd:PRK14999   2 YSSRSRSAPAPFYETVKQDICKKIAGGVWQPHDRIPSEAELVAQYGFSRMTINRALRELTDEGWLV 67
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
 16-68 8.28e-03

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: 37.73  E-value: 8.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 906389112   16 YQQLYRYFKENMHRGRIQKGMKLPSKRLLANQLSISQTTVERAYEQLAAEGYI 68
Cdd:TIGR02404   2 YEQIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYI 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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