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Conserved domains on  [gi|2038545165|emb|CAG5297164|]
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transcriptional regulator [Streptococcus pneumoniae]

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 ...
3-332 7.23e-93

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: 287.50  E-value: 7.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   3 KQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLEIEV 82
Cdd:COG1167    10 SGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPAPRA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165  83 TDEHASA--------------------------YDDFRLCVNETLIGRENYLFNYYDNQeGLEDLRQSIHKLLFDQALYC 136
Cdd:COG1167    90 AAAVAAPalrrlleaapgvidlgsgapdpdlfpLAALRRALRRALRRLPPALLGYGDPQ-GLPELREAIARYLARRGVPA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 137 KANQLVLTSGTQQALFILSQIpFPSQAKEILVEQPTYHRMNRLLIAQGLDYQTIERGIDGIDLEELEGHFKTGKIKFFYT 216
Cdd:COG1167   169 SPDQILITSGAQQALDLALRA-LLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHRPRAVYV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 217 IPRFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDL--DSKKGQTFHYLDTEERVIYIKSFSTSLFPALRITALIL 294
Cdd:COG1167   248 TPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELryDGRPPPPLAALDAPGRVIYIGSFSKTLAPGLRLGYLVA 327
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2038545165 295 PNTIKEAFVAYKNILDYDSNLIMQKALSLYIDSQLFEK 332
Cdd:COG1167   328 PGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDR 365
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
3-332 7.23e-93

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: 287.50  E-value: 7.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   3 KQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLEIEV 82
Cdd:COG1167    10 SGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPAPRA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165  83 TDEHASA--------------------------YDDFRLCVNETLIGRENYLFNYYDNQeGLEDLRQSIHKLLFDQALYC 136
Cdd:COG1167    90 AAAVAAPalrrlleaapgvidlgsgapdpdlfpLAALRRALRRALRRLPPALLGYGDPQ-GLPELREAIARYLARRGVPA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 137 KANQLVLTSGTQQALFILSQIpFPSQAKEILVEQPTYHRMNRLLIAQGLDYQTIERGIDGIDLEELEGHFKTGKIKFFYT 216
Cdd:COG1167   169 SPDQILITSGAQQALDLALRA-LLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHRPRAVYV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 217 IPRFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDL--DSKKGQTFHYLDTEERVIYIKSFSTSLFPALRITALIL 294
Cdd:COG1167   248 TPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELryDGRPPPPLAALDAPGRVIYIGSFSKTLAPGLRLGYLVA 327
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2038545165 295 PNTIKEAFVAYKNILDYDSNLIMQKALSLYIDSQLFEK 332
Cdd:COG1167   328 PGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDR 365
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
104-327 2.96e-34

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: 130.54  E-value: 2.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 104 RENYLFNYYDNQeGLEDLRQSI-HKLLFDQALYCKANQLVLTSGTQQALFILSQIpFPSQAKEILVEQPTYHRMNRLLIA 182
Cdd:cd00609    25 LRAGLLGYYPDP-GLPELREAIaEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRA-LLNPGDEVLVPDPTYPGYEAAARL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 183 QGLDYQTIERGIDGIDLE--ELEGHFKTGKIKFFYTIPrFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDL--DS 258
Cdd:cd00609   103 AGAEVVPVPLDEEGGFLLdlELLEAAKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELvyDG 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545165 259 KKGQTFHYLDTEERVIYIKSFSTSL-FPALRITALILPNT-IKEAFVAYKNILDYDSNLIMQKALSLYIDS 327
Cdd:cd00609   182 EPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPPEeLLERLKKLLPYTTSGPSTLSQAAAAAALDD 252
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
10-69 4.94e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 60.67  E-value: 4.94e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   10 VVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
6-69 3.15e-10

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: 55.70  E-value: 3.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545165   6 KYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
PRK06207 PRK06207
pyridoxal phosphate-dependent aminotransferase;
112-250 1.89e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235742  Cd Length: 405  Bit Score: 59.01  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 112 YDNQEGLEDLRQSIHKLL--FDQALYCKANQLVLTSGTQQALFiLSQIPFPSQAKEILVEQPTYHrMNRLLIA--QG--- 184
Cdd:PRK06207   74 YTEYRGDADIRELLAARLaaFTGAPVDAADELIITPGTQGALF-LAVAATVARGDKVAIVQPDYF-ANRKLVEffEGemv 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545165 185 ---LDYQTIERGIdGIDLEELEGHFKTGKIKFFYTIPrfHYPLGHSYSEQDKRAILDLAAKYSVYIVED 250
Cdd:PRK06207  152 pvqLDYLSADKRA-GLDLDQLEEAFKAGVRVFLFSNP--NNPAGVVYSAEEIAQIAALARRYGATVIVD 217
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
109-322 1.28e-03

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: 40.79  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 109 FNYYDNQEGLEDLRQSIHKLLFDQALY-CKANQLVLTSGTQQAL-FILSQIPFPSQakEILVEQPTYHRMNRLLIAQGLD 186
Cdd:TIGR01265  66 FNGYAPSVGALAAREAVAEYLSSDLPGkLTADDVVLTSGCSQAIeICIEALANPGA--NILVPRPGFPLYDTRAAFSGLE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 187 ---YQTI-ERGIDgIDLEELEGHF--KTGKIkffyTIPRFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDLdSKK 260
Cdd:TIGR01265 144 vrlYDLLpEKDWE-IDLDGLESLAdeKTVAI----VVINPSNPCGSVFSRDHLQKIAEVAEKLGIPIIADEIYGHM-VFG 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545165 261 GQTFH---YLDTEERVIYIKSFSTSLF-PALRITALIL--PNTI--KEAFVAYKNILDY--DSNLIMQKALS 322
Cdd:TIGR01265 218 DAPFIpmaSFASIVPVLSLGGISKRWVvPGWRLGWIIIhdPHGIfrDTVLQGLKNLLQRilGPATIVQGALP 289
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
3-332 7.23e-93

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: 287.50  E-value: 7.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   3 KQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLEIEV 82
Cdd:COG1167    10 SGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPAPRA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165  83 TDEHASA--------------------------YDDFRLCVNETLIGRENYLFNYYDNQeGLEDLRQSIHKLLFDQALYC 136
Cdd:COG1167    90 AAAVAAPalrrlleaapgvidlgsgapdpdlfpLAALRRALRRALRRLPPALLGYGDPQ-GLPELREAIARYLARRGVPA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 137 KANQLVLTSGTQQALFILSQIpFPSQAKEILVEQPTYHRMNRLLIAQGLDYQTIERGIDGIDLEELEGHFKTGKIKFFYT 216
Cdd:COG1167   169 SPDQILITSGAQQALDLALRA-LLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHRPRAVYV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 217 IPRFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDL--DSKKGQTFHYLDTEERVIYIKSFSTSLFPALRITALIL 294
Cdd:COG1167   248 TPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELryDGRPPPPLAALDAPGRVIYIGSFSKTLAPGLRLGYLVA 327
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2038545165 295 PNTIKEAFVAYKNILDYDSNLIMQKALSLYIDSQLFEK 332
Cdd:COG1167   328 PGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDR 365
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
104-327 2.96e-34

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: 130.54  E-value: 2.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 104 RENYLFNYYDNQeGLEDLRQSI-HKLLFDQALYCKANQLVLTSGTQQALFILSQIpFPSQAKEILVEQPTYHRMNRLLIA 182
Cdd:cd00609    25 LRAGLLGYYPDP-GLPELREAIaEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRA-LLNPGDEVLVPDPTYPGYEAAARL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 183 QGLDYQTIERGIDGIDLE--ELEGHFKTGKIKFFYTIPrFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDL--DS 258
Cdd:cd00609   103 AGAEVVPVPLDEEGGFLLdlELLEAAKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELvyDG 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545165 259 KKGQTFHYLDTEERVIYIKSFSTSL-FPALRITALILPNT-IKEAFVAYKNILDYDSNLIMQKALSLYIDS 327
Cdd:cd00609   182 EPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPPEeLLERLKKLLPYTTSGPSTLSQAAAAAALDD 252
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
5-69 8.22e-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: 77.10  E-value: 8.22e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545165   5 SKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:cd07377     1 PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFV 65
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
7-79 2.90e-14

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 68.67  E-value: 2.90e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545165   7 YKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLE 79
Cdd:COG1725    12 YEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFVAEDARELLEE 84
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
1-79 2.82e-13

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 69.12  E-value: 2.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545165   1 MKKQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLE 79
Cdd:COG2188     1 SSPVPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLS 79
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
10-69 4.94e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 60.67  E-value: 4.94e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   10 VVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
6-69 3.15e-10

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: 55.70  E-value: 3.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545165   6 KYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
PRK06207 PRK06207
pyridoxal phosphate-dependent aminotransferase;
112-250 1.89e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235742  Cd Length: 405  Bit Score: 59.01  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 112 YDNQEGLEDLRQSIHKLL--FDQALYCKANQLVLTSGTQQALFiLSQIPFPSQAKEILVEQPTYHrMNRLLIA--QG--- 184
Cdd:PRK06207   74 YTEYRGDADIRELLAARLaaFTGAPVDAADELIITPGTQGALF-LAVAATVARGDKVAIVQPDYF-ANRKLVEffEGemv 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545165 185 ---LDYQTIERGIdGIDLEELEGHFKTGKIKFFYTIPrfHYPLGHSYSEQDKRAILDLAAKYSVYIVED 250
Cdd:PRK06207  152 pvqLDYLSADKRA-GLDLDQLEEAFKAGVRVFLFSNP--NNPAGVVYSAEEIAQIAALARRYGATVIVD 217
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
1-80 1.08e-08

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 55.32  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   1 MKKQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLEI 80
Cdd:COG2186     3 IRRRSLAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSPWALLDP 82
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
109-301 3.75e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 51.54  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 109 FNYYDNQEGLEDLRQSIHKLLFDQAL--YCKANQLVLTSGTQQALFILSQIPFPSQaKEILVEQPTYHRMNRLLIAQGLD 186
Cdd:pfam00155  32 RNLYGPTDGHPELREALAKFLGRSPVlkLDREAAVVFGSGAGANIEALIFLLANPG-DAILVPAPTYASYIRIARLAGGE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 187 YQTIERGID---GIDLEELEGHFKTGKIKFFYTIPrfHYPLGHSYSEQDKRAILDLAAKYSVYIVEDD-----YLGDLDS 258
Cdd:pfam00155 111 VVRYPLYDSndfHLDFDALEAALKEKPKVVLHTSP--HNPTGTVATLEELEKLLDLAKEHNILLLVDEayagfVFGSPDA 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038545165 259 KKGQTFhyLDTEERVIYIKSFSTSL-FPALRITALILPNTIKEA 301
Cdd:pfam00155 189 VATRAL--LAEGPNLLVVGSFSKAFgLAGWRVGYILGNAAVISQ 230
PRK08363 PRK08363
alanine aminotransferase; Validated
110-251 3.61e-06

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 48.65  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 110 NYYDNQEGLEDLRQSI-HKLLFDQALYCKANQLVLTSGTQQAL-FILSQIPFPSQakEILVEQPT---YHRMNRLLIAQG 184
Cdd:PRK08363   64 NYYGPSEGLPELREAIvKREKRKNGVDITPDDVRVTAAVTEALqLIFGALLDPGD--EILIPGPSyppYTGLVKFYGGVP 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545165 185 LDYQTIERGIDGIDLEELEGHFkTGKIKFFYTI-PrfHYPLGHSYSEQDKRAILDLAAKYSVYIVEDD 251
Cdd:PRK08363  142 VEYRTIEEEGWQPDIDDIRKKI-TEKTKAIAVInP--NNPTGALYEKKTLKEILDIAGEHDLPVISDE 206
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
223-375 8.89e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 47.44  E-value: 8.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 223 PLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDLDSKkgqtfHYLDTE---ERVIYIKSFSTSLFPA-LRITALILPNTI 298
Cdd:PRK06225  169 PLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDFARE-----HTLAAEyapEHTVTSYSFSKIFGMAgLRIGAVVATPDL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 299 KEAFVAYKnILDYDSNLIMQKA--LSLYIDSQLFEKNRLARLTNhesyQKQIEERITKTP-CPLPHYPLHDGLL-LDLRQ 374
Cdd:PRK06225  244 IEVVKSIV-INDLGTNVIAQEAaiAGLKVKDEWIDRIRRTTFKN----QKLIKEAVDEIEgVFLPVYPSHGNMMvIDISE 318

                  .
gi 2038545165 375 Y 375
Cdd:PRK06225  319 A 319
PRK11523 PRK11523
transcriptional regulator ExuR;
7-89 2.66e-05

transcriptional regulator ExuR;


Pssm-ID: 183176 [Multi-domain]  Cd Length: 253  Bit Score: 45.61  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165   7 YKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQGQHQDLEIEVTDEH 86
Cdd:PRK11523   10 YQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSGIHVVSNQPRHQQAADNNMEF 89

                  ...
gi 2038545165  87 ASA 89
Cdd:PRK11523   90 ANY 92
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
2-69 4.24e-05

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 44.53  E-value: 4.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545165   2 KKQSKYKEVVSYLKNGIESGRFPTGSRLpSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYV 69
Cdd:COG1802     8 RRESLAEQVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARV 74
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
111-280 2.76e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 42.92  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 111 YYDNQEGLEDLRQSIHKLLFDQALYCKANQLVLTSGTQQAL-FILSQIPFPSQakEILVEQPTYHRMNRLLIAQGLDYQT 189
Cdd:PRK07568   61 AYSHSQGIPELREAFAKYYKKWGIDVEPDEILITNGGSEAIlFAMMAICDPGD--EILVPEPFYANYNGFATSAGVKIVP 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 190 IERGI-DGIDL---EELEGHF--KTGKIKFfyTIPrfHYPLGHSYSEQDKRAILDLAAKYSVYIVED----DYLGDlDSK 259
Cdd:PRK07568  139 VTTKIeEGFHLpskEEIEKLItpKTKAILI--SNP--GNPTGVVYTKEELEMLAEIAKKHDLFLISDevyrEFVYD-GLK 213
                         170       180
                  ....*....|....*....|.
gi 2038545165 260 KGQTFHYLDTEERVIYIKSFS 280
Cdd:PRK07568  214 YTSALSLEGLEDRVIIIDSVS 234
PRK09764 PRK09764
GntR family transcriptional regulator;
1-72 7.57e-04

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 40.97  E-value: 7.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545165   1 MKKQSKYKEVVSYLKNGIESGRFPTGSRLPSIRQLSLDFHCSKDTIQRALLELRHEQYLYAKPQSGYYVLEQ 72
Cdd:PRK09764    1 MGHKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVKEE 72
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
109-322 1.28e-03

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: 40.79  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 109 FNYYDNQEGLEDLRQSIHKLLFDQALY-CKANQLVLTSGTQQAL-FILSQIPFPSQakEILVEQPTYHRMNRLLIAQGLD 186
Cdd:TIGR01265  66 FNGYAPSVGALAAREAVAEYLSSDLPGkLTADDVVLTSGCSQAIeICIEALANPGA--NILVPRPGFPLYDTRAAFSGLE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 187 ---YQTI-ERGIDgIDLEELEGHF--KTGKIkffyTIPRFHYPLGHSYSEQDKRAILDLAAKYSVYIVEDDYLGDLdSKK 260
Cdd:TIGR01265 144 vrlYDLLpEKDWE-IDLDGLESLAdeKTVAI----VVINPSNPCGSVFSRDHLQKIAEVAEKLGIPIIADEIYGHM-VFG 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545165 261 GQTFH---YLDTEERVIYIKSFSTSLF-PALRITALIL--PNTI--KEAFVAYKNILDY--DSNLIMQKALS 322
Cdd:TIGR01265 218 DAPFIpmaSFASIVPVLSLGGISKRWVvPGWRLGWIIIhdPHGIfrDTVLQGLKNLLQRilGPATIVQGALP 289
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
166-292 4.05e-03

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 39.26  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545165 166 ILVEQPTYHRMNRLLIAQGLDYQTIERGIDGIDLEELEGHFKTGKIKFFYTiPRFHYPLGHSYSEQDKRAILDLAAKY-S 244
Cdd:PRK15481  168 VAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGARAVILT-PRAHNPTGCSLSARRAAALRNLLARYpQ 246
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2038545165 245 VYIVEDDYLGDLDSKKGQTFHYLDTeERVIYIKSFSTSLFPALRITAL 292
Cdd:PRK15481  247 VLVIIDDHFALLSSSPYHSVIPQTT-QRWALIRSVSKALGPDLRLAFV 293
 
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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