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Conserved domains on  [gi|512748087|ref|WP_016504289|]
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PLP-dependent aminotransferase family protein [Pasteurella multocida]

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 ...
4-464 2.62e-137

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: 403.44  E-value: 2.62e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087   4 LNYQLDKGKKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQP 83
Cdd:COG1167    1 MLIRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  84 SLFFSAPKQTQPHTVA-----LRHSTIAFDFNPHYIDSKHFPLKNWRKAGKALFQARHSSLLGLGDKQGESHLRQQICDY 158
Cdd:COG1167   81 PAPAPAPRAAAAVAAPalrrlLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIARY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 159 LfSSRGVKCHIDQIIICGGLENAIQQLMLLFTHLYQTpvvhYGMEFYGYQTLEKLLTLAHQKVIKLPLnaDDQQLDLDFL 238
Cdd:COG1167  161 L-ARRGVPASPDQILITSGAQQALDLALRALLRPGDT----VAVESPTYPGALAALRAAGLRLVPVPV--DEDGLDLDAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 239 A----QSSVNIACVTPSHLYPFGHVLSITQRQQLLAWAKAQpQRYIIEDDYDSEFRYQGKPIPALQSLDKNDSVIYLGSF 314
Cdd:COG1167  234 EaalrRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRH-GVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 315 SKLLMPSLRVSFMVLPTSLLAAYQQHCGFINCAVSRFEQQRLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLAPYA-TQ 393
Cdd:COG1167  313 SKTLAPGLRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLpDG 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512748087 394 IRYYGEHSGFYLLIELiAESRSLETLTQLAYDKGVKVYP-----VDCAARRLFSLGFGDLSETQLVEGVSCLLNAW 464
Cdd:COG1167  393 LRVTGPPGGLHLWLEL-PEGVDAEALAAAALARGILVAPgsafsADGPPRNGLRLGFGAPSEEELEEALRRLAELL 467
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
4-464 2.62e-137

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: 403.44  E-value: 2.62e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087   4 LNYQLDKGKKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQP 83
Cdd:COG1167    1 MLIRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  84 SLFFSAPKQTQPHTVA-----LRHSTIAFDFNPHYIDSKHFPLKNWRKAGKALFQARHSSLLGLGDKQGESHLRQQICDY 158
Cdd:COG1167   81 PAPAPAPRAAAAVAAPalrrlLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIARY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 159 LfSSRGVKCHIDQIIICGGLENAIQQLMLLFTHLYQTpvvhYGMEFYGYQTLEKLLTLAHQKVIKLPLnaDDQQLDLDFL 238
Cdd:COG1167  161 L-ARRGVPASPDQILITSGAQQALDLALRALLRPGDT----VAVESPTYPGALAALRAAGLRLVPVPV--DEDGLDLDAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 239 A----QSSVNIACVTPSHLYPFGHVLSITQRQQLLAWAKAQpQRYIIEDDYDSEFRYQGKPIPALQSLDKNDSVIYLGSF 314
Cdd:COG1167  234 EaalrRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRH-GVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 315 SKLLMPSLRVSFMVLPTSLLAAYQQHCGFINCAVSRFEQQRLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLAPYA-TQ 393
Cdd:COG1167  313 SKTLAPGLRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLpDG 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512748087 394 IRYYGEHSGFYLLIELiAESRSLETLTQLAYDKGVKVYP-----VDCAARRLFSLGFGDLSETQLVEGVSCLLNAW 464
Cdd:COG1167  393 LRVTGPPGGLHLWLEL-PEGVDAEALAAAALARGILVAPgsafsADGPPRNGLRLGFGAPSEEELEEALRRLAELL 467
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
129-432 1.35e-42

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: 154.04  E-value: 1.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 129 KALFQARHSSLLGLGDKQGESHLRQQICDYLFSSRGVKCHIDQIIICGGLENAIQQLMLLFTH-----LYQTPvvhygme 203
Cdd:cd00609   19 ALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRALLNpgdevLVPDP------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 204 fyGYQTLEKLLTLAHQKVIKLPLNADDQQLD----LDFLAQSSVNIACVTPSHlYPFGHVLSITQRQQLLAWAKaQPQRY 279
Cdd:cd00609   92 --TYPGYEAAARLAGAEVVPVPLDEEGGFLLdlelLEAAKTPKTKLLYLNNPN-NPTGAVLSEEELEELAELAK-KHGIL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 280 IIEDDYDSEFRYQGKPIPALQSLDKNDSVIYLGSFSKLL-MPSLRVSFMVLP-TSLLAAYQQHCGFINCAVSRFEQQRLA 357
Cdd:cd00609  168 IISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPpEELLERLKKLLPYTTSGPSTLSQAAAA 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512748087 358 YFMQQGefEKHINRMRKIYRRKMALLCSLLAPYATQIRYYGEHsGFYLLIELiAESRSLETLTQLAYDKGVKVYP 432
Cdd:cd00609  248 AALDDG--EEHLEELRERYRRRRDALLEALKELGPLVVVKPSG-GFFLWLDL-PEGDDEEFLERLLLEAGVVVRP 318
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
16-79 2.55e-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: 61.86  E-value: 2.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512748087   16 LYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
20-79 1.63e-10

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 56.43  E-value: 1.63e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087    20 LYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
19-423 1.60e-08

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 56.59  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  19 QLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQPSLFfsAPKQTQPHTv 98
Cdd:PRK15481   9 EIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPV--ALEGGDPGT- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  99 ALRhstiafDF---NPhyiDSKHFPlknwrkagkalfqaRHSSLLGLGDKQ----GESHLRQQICDYLFSSRGVKCHID- 170
Cdd:PRK15481  86 PLH------DLaggNP---DPQRLP--------------DLSRYFARLSRTprlyGDAPVSPELHAWAARWLRDDCPVAf 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 171 QIIICGGLENAIQQlmLLFTHLYQTPVVhyGMEFYGYqtLEKLLTLAHQKVIKLPLNADDQQLDLDFLAQSSVNIA---C 247
Cdd:PRK15481 143 EIDLTSGAIDAIER--LLCAHLLPGDSV--AVEDPCF--LSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGAravI 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 248 VTPSHLYPFGHVLSITQR---QQLLAwakAQPQRYIIEDDYdseFryqgkpipALQSLDKNDSVIYLG--------SFSK 316
Cdd:PRK15481 217 LTPRAHNPTGCSLSARRAaalRNLLA---RYPQVLVIIDDH---F--------ALLSSSPYHSVIPQTtqrwalirSVSK 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 317 LLMPSLRVSF--------MVLPTSLLAAYQQhcgfincaVSRFEQQRLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLA 388
Cdd:PRK15481 283 ALGPDLRLAFvasdsatsARLRLRLNSGTQW--------VSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKLARALQ 354
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 512748087 389 pyATQIRYYGEHSGFYLLIELIAESRSleTLTQLA 423
Cdd:PRK15481 355 --QYGIAIPSPGDGLNLWLPLDTDSQA--TALTLA 385
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
17-79 2.17e-06

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: 48.90  E-value: 2.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512748087   17 YLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:TIGR02404   2 YEQIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYIQKIQGKGSIV 64
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
4-464 2.62e-137

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: 403.44  E-value: 2.62e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087   4 LNYQLDKGKKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQP 83
Cdd:COG1167    1 MLIRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  84 SLFFSAPKQTQPHTVA-----LRHSTIAFDFNPHYIDSKHFPLKNWRKAGKALFQARHSSLLGLGDKQGESHLRQQICDY 158
Cdd:COG1167   81 PAPAPAPRAAAAVAAPalrrlLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPALLGYGDPQGLPELREAIARY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 159 LfSSRGVKCHIDQIIICGGLENAIQQLMLLFTHLYQTpvvhYGMEFYGYQTLEKLLTLAHQKVIKLPLnaDDQQLDLDFL 238
Cdd:COG1167  161 L-ARRGVPASPDQILITSGAQQALDLALRALLRPGDT----VAVESPTYPGALAALRAAGLRLVPVPV--DEDGLDLDAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 239 A----QSSVNIACVTPSHLYPFGHVLSITQRQQLLAWAKAQpQRYIIEDDYDSEFRYQGKPIPALQSLDKNDSVIYLGSF 314
Cdd:COG1167  234 EaalrRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRH-GVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 315 SKLLMPSLRVSFMVLPTSLLAAYQQHCGFINCAVSRFEQQRLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLAPYA-TQ 393
Cdd:COG1167  313 SKTLAPGLRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLpDG 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512748087 394 IRYYGEHSGFYLLIELiAESRSLETLTQLAYDKGVKVYP-----VDCAARRLFSLGFGDLSETQLVEGVSCLLNAW 464
Cdd:COG1167  393 LRVTGPPGGLHLWLEL-PEGVDAEALAAAALARGILVAPgsafsADGPPRNGLRLGFGAPSEEELEEALRRLAELL 467
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
129-432 1.35e-42

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: 154.04  E-value: 1.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 129 KALFQARHSSLLGLGDKQGESHLRQQICDYLFSSRGVKCHIDQIIICGGLENAIQQLMLLFTH-----LYQTPvvhygme 203
Cdd:cd00609   19 ALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRALLNpgdevLVPDP------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 204 fyGYQTLEKLLTLAHQKVIKLPLNADDQQLD----LDFLAQSSVNIACVTPSHlYPFGHVLSITQRQQLLAWAKaQPQRY 279
Cdd:cd00609   92 --TYPGYEAAARLAGAEVVPVPLDEEGGFLLdlelLEAAKTPKTKLLYLNNPN-NPTGAVLSEEELEELAELAK-KHGIL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 280 IIEDDYDSEFRYQGKPIPALQSLDKNDSVIYLGSFSKLL-MPSLRVSFMVLP-TSLLAAYQQHCGFINCAVSRFEQQRLA 357
Cdd:cd00609  168 IISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFgLPGLRIGYLIAPpEELLERLKKLLPYTTSGPSTLSQAAAA 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512748087 358 YFMQQGefEKHINRMRKIYRRKMALLCSLLAPYATQIRYYGEHsGFYLLIELiAESRSLETLTQLAYDKGVKVYP 432
Cdd:cd00609  248 AALDDG--EEHLEELRERYRRRRDALLEALKELGPLVVVKPSG-GFFLWLDL-PEGDDEEFLERLLLEAGVVVRP 318
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
15-80 9.52e-21

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: 85.58  E-value: 9.52e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512748087  15 PLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVC 80
Cdd:cd07377    1 PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
7-80 5.36e-19

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 82.15  E-value: 5.36e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512748087   7 QLDKGKKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVC 80
Cdd:COG1725    2 RIDFDSGVPIYEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFVA 75
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
13-83 4.11e-14

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 71.82  E-value: 4.11e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512748087  13 KEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQP 83
Cdd:COG2188    3 PVPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPK 73
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
151-388 1.19e-13

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: 72.09  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 151 LRQQICDYLFSSRGVKCHIDQIIICGGLENAIQQLMLLFTH-----LYQTPvvhygmefyGYQTLEKLLTLAHQKVIKLP 225
Cdd:COG0436   72 LREAIAAYYKRRYGVDLDPDEILVTNGAKEALALALLALLNpgdevLVPDP---------GYPSYRAAVRLAGGKPVPVP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 226 LNADDQ-QLDLDFLAQSS--------VNiacvTPSHlyPFGHVLSITQRQQLLAWAKaqpQR--YIIEDD-YdSEFRYQG 293
Cdd:COG0436  143 LDEENGfLPDPEALEAAItprtkaivLN----SPNN--PTGAVYSREELEALAELAR---EHdlLVISDEiY-EELVYDG 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 294 -KPIPALQSLDKNDSVIYLGSFSK-LLMPSLRVSFMVLPTSLLAA---YQQHCGFincAVSRFEQQRLAYFMQQGefEKH 368
Cdd:COG0436  213 aEHVSILSLPGLKDRTIVINSFSKsYAMTGWRIGYAVGPPELIAAllkLQSNLTS---CAPTPAQYAAAAALEGP--QDY 287
                        250       260
                 ....*....|....*....|
gi 512748087 369 INRMRKIYRRKMALLCSLLA 388
Cdd:COG0436  288 VEEMRAEYRRRRDLLVEGLN 307
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
16-79 2.55e-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: 61.86  E-value: 2.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512748087   16 LYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
20-79 1.63e-10

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 56.43  E-value: 1.63e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087    20 LYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
12-79 2.92e-09

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 57.24  E-value: 2.92e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512748087  12 KKEPLYLQLYQQLRDLIYTQQLAFGEQLpSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:COG1802    8 RRESLAEQVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARV 74
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
19-423 1.60e-08

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 56.59  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  19 QLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVCFQPSLFfsAPKQTQPHTv 98
Cdd:PRK15481   9 EIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPV--ALEGGDPGT- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  99 ALRhstiafDF---NPhyiDSKHFPlknwrkagkalfqaRHSSLLGLGDKQ----GESHLRQQICDYLFSSRGVKCHID- 170
Cdd:PRK15481  86 PLH------DLaggNP---DPQRLP--------------DLSRYFARLSRTprlyGDAPVSPELHAWAARWLRDDCPVAf 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 171 QIIICGGLENAIQQlmLLFTHLYQTPVVhyGMEFYGYqtLEKLLTLAHQKVIKLPLNADDQQLDLDFLAQSSVNIA---C 247
Cdd:PRK15481 143 EIDLTSGAIDAIER--LLCAHLLPGDSV--AVEDPCF--LSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGAravI 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 248 VTPSHLYPFGHVLSITQR---QQLLAwakAQPQRYIIEDDYdseFryqgkpipALQSLDKNDSVIYLG--------SFSK 316
Cdd:PRK15481 217 LTPRAHNPTGCSLSARRAaalRNLLA---RYPQVLVIIDDH---F--------ALLSSSPYHSVIPQTtqrwalirSVSK 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 317 LLMPSLRVSF--------MVLPTSLLAAYQQhcgfincaVSRFEQQRLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLA 388
Cdd:PRK15481 283 ALGPDLRLAFvasdsatsARLRLRLNSGTQW--------VSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKLARALQ 354
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 512748087 389 pyATQIRYYGEHSGFYLLIELIAESRSleTLTQLA 423
Cdd:PRK15481 355 --QYGIAIPSPGDGLNLWLPLDTDSQA--TALTLA 385
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
12-80 2.45e-08

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 54.55  E-value: 2.45e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512748087  12 KKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFVC 80
Cdd:COG2186    4 RRRSLAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVR 72
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
115-432 1.22e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 50.38  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  115 DSKHFPLKNWRKAGKALFQARhsSLLGLGDKQGESHLRQQICDYLFSSRGVKC-HIDQIIICGGLENAIQQLMLLFTH-- 191
Cdd:pfam00155  10 EYLGDTLPAVAKAEKDALAGG--TRNLYGPTDGHPELREALAKFLGRSPVLKLdREAAVVFGSGAGANIEALIFLLANpg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  192 ---LYQTPVvhygmeFYGYQTLeklLTLAHQKVIKLPLN-ADDQQLDLD----FLAQSSVNIACVTPSHlyPFGHVLSIT 263
Cdd:pfam00155  88 daiLVPAPT------YASYIRI---ARLAGGEVVRYPLYdSNDFHLDFDaleaALKEKPKVVLHTSPHN--PTGTVATLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  264 QRQQLLAWAKAQPQRYIIEDDYdSEFRYQGK-PIPALQSLDKNDSVIYLGSFSK-LLMPSLRVSFMVLPTSLLAAYQQHC 341
Cdd:pfam00155 157 ELEKLLDLAKEHNILLLVDEAY-AGFVFGSPdAVATRALLAEGPNLLVVGSFSKaFGLAGWRVGYILGNAAVISQLRKLA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087  342 GFINcaVSRFEQQ-RLAYFMQQGEFEKHINRMRKIYRRKMALLCSLLApyATQIRYYGEHSGFYLLIELiAESRSLETLT 420
Cdd:pfam00155 236 RPFY--SSTHLQAaAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQ--AAGLSVLPSQAGFFLLTGL-DPETAKELAQ 310
                         330
                  ....*....|..
gi 512748087  421 QLAYDKGVKVYP 432
Cdd:pfam00155 311 VLLEEVGVYVTP 322
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
19-83 1.81e-06

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 49.00  E-value: 1.81e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512748087  19 QLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESiaRR--GFFVCFQP 83
Cdd:PRK10421   6 EVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLS--RRggGTFIRWRH 70
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
17-79 2.17e-06

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: 48.90  E-value: 2.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512748087   17 YLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:TIGR02404   2 YEQIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYIQKIQGKGSIV 64
PRK05839 PRK05839
succinyldiaminopimelate transaminase;
136-432 2.26e-06

succinyldiaminopimelate transaminase;


Pssm-ID: 180281  Cd Length: 374  Bit Score: 49.69  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 136 HSSLLGLGDKQ-GESHLRQQICDYLFSSRGVKCHIDQIIICGGLENAIQQLMLLFTHLYQTPVVHYGMEFYgyQTLEKLL 214
Cdd:PRK05839  49 NAHLLNKYPKSaGEESLREAQRGFFKRRFKIELKENELIPTFGTREVLFNFPQFVLFDKQNPTIAYPNPFY--QIYEGAA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 215 TLAHQKVIKLPLNAD-DQQLDLDFLAQSSVNIACV-TPSHlyPFGHVLSItqrQQLLAWAKAQPQR--YIIEDDYDSEFr 290
Cdd:PRK05839 127 IASRAKVLLMPLTKEnDFTPSLNEKELQEVDLVILnSPNN--PTGRTLSL---EELIEWVKLALKHdfILINDECYSEI- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 291 YQGKPIPAL--QSLDKNDS----VIYLGSFSKLL-MPSLRVSFMVLPTSLLAAYQQHCGFINCAVSRFEQQRLAYFMQQG 363
Cdd:PRK05839 201 YENTPPPSLleASILVGNEsfknVLVINSISKRSsAPGLRSGFIAGDASILKKYKAYRTYLGCASPLPLQKAAAVAWLDD 280
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512748087 364 EfekHINRMRKIYRRKMALLCSLL---APYATqiryygehsgFYLLIELIAEsrslETLTQLAY-DKGVKVYP 432
Cdd:PRK05839 281 E---HAEFFRNIYAKNLKLAREILgitIPPAT----------FYVWLPVDND----EEFTKKLYqNEGIKVLP 336
PRK11402 PRK11402
transcriptional regulator PhoB;
8-79 2.50e-06

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 48.68  E-value: 2.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512748087   8 LDKGKKEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:PRK11402   2 TDRYSHQLLYATVRQRLLDDIAQGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFV 73
PRK08361 PRK08361
aspartate aminotransferase; Provisional
147-432 4.30e-04

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 42.56  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 147 GESHLRQQICDYLFSSRGVKCHIDQIIICGGlenAIQQLMLLFTHLYQT--PVVHYGMEFYGYQTLEKlltLAHQKVIKL 224
Cdd:PRK08361  71 GIPELREAIAEYYKKFYGVDVDVDNVIVTAG---AYEATYLAFESLLEEgdEVIIPDPAFVCYVEDAK---IAEAKPIRI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 225 PLNADDQ-QLDLDFL----AQSSVNIACVTPSHlyPFGHVLsitqrQQLLAWAKAQPQR----YIIEDDYDSEFRYQG-K 294
Cdd:PRK08361 145 PLREENEfQPDPDELleliTKRTRMIVINYPNN--PTGATL-----DKEVAKAIADIAEdyniYILSDEPYEHFLYEGaK 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512748087 295 PIPALQSldKNDSVIYLGSFSKLL-MPSLRVSFMVLPTSLLAAYQQHCGFINCAVSRFEQQRLAYFMQQGEFEKHINRMR 373
Cdd:PRK08361 218 HYPMIKY--APDNTILANSFSKTFaMTGWRLGFVIAPEQVIKDMIKLHAYIIGNVASFVQIAGIEALRSKESWKAVEEMR 295
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512748087 374 KIY--RRKMALLCSLLAPYATQIRYYGehsGFYLLIELIAESRSLETLTQLAYDK-GVKVYP 432
Cdd:PRK08361 296 KEYneRRKLVLKRLKEMPHIKVFEPKG---AFYVFANIDETGMSSEDFAEWLLEKaRVVVIP 354
PRK09764 PRK09764
GntR family transcriptional regulator;
13-79 5.56e-04

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 41.35  E-value: 5.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512748087  13 KEPLYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIESIARRGFFV 79
Cdd:PRK09764   3 HKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYV 69
PRK11523 PRK11523
transcriptional regulator ExuR;
16-76 9.32e-03

transcriptional regulator ExuR;


Pssm-ID: 183176 [Multi-domain]  Cd Length: 253  Bit Score: 37.90  E-value: 9.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512748087  16 LYLQLYQQLRDLIYTQQLAFGEQLPSKRALCDYLQISQNTVEAAYAQLLAEGYIEsiARRG 76
Cdd:PRK11523   9 LYQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVE--VRKG 67
 
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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