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Conserved domains on  [gi|1937014296|gb|QPI42506|]
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repressor LexA [Pectobacterium aroidearum]

Protein Classification

transcriptional repressor LexA( domain architecture ID 11489206)

transcriptional repressor LexA represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA

CATH:  1.10.10.10
EC:  3.4.21.88
Gene Ontology:  GO:0004252|GO:0006282|GO:0006355|GO:0003677
SCOP:  4000321

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-200 4.42e-101

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


:

Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 290.46  E-value: 4.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296   1 MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVG 80
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPKGVPLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  81 RVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLK 159
Cdd:TIGR00498  81 RVAAGEPILAEQHIEEYFPIDFSLLKkPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937014296 160 KQGNMVHLLAENEEFAPIVVDLRqqSFSIEGLAVGVIRNSD 200
Cdd:TIGR00498 161 KDGTKVELKPENPEFDPIVLNAE--DVTILGKVVGVIRNFQ 199
 
Name Accession Description Interval E-value
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-200 4.42e-101

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 290.46  E-value: 4.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296   1 MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVG 80
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPKGVPLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  81 RVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLK 159
Cdd:TIGR00498  81 RVAAGEPILAEQHIEEYFPIDFSLLKkPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937014296 160 KQGNMVHLLAENEEFAPIVVDLRqqSFSIEGLAVGVIRNSD 200
Cdd:TIGR00498 161 KDGTKVELKPENPEFDPIVLNAE--DVTILGKVVGVIRNFQ 199
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-198 8.15e-85

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 249.06  E-value: 8.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296   1 MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSpNAAEEHLKALARKGVIEIVSGASRGIRLL--MEEETGIPL 78
Cdd:COG1974     1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLpaSPEVVGLPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  79 VGRVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKR 157
Cdd:COG1974    80 LGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937014296 158 LKKQGNMVHLLAENEEFAPIVVDLrqQSFSIEGLAVGVIRN 198
Cdd:COG1974   160 LYKEGGRVRLQPENPAYPPIIIEG--DDVEILGVVVGVIRR 198
Peptidase_S24 pfam00717
Peptidase S24-like;
77-193 1.88e-40

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 133.48  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  77 PLVGRVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDiGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTV 155
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSpPGNLFALRVKGDSMEP-GIPDGDLVLVDPSREARNGDIVVARLDGEATV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937014296 156 KRLKKQGNMVHLLAENEEFAPIVVDlRQQSFSIEGLAV 193
Cdd:pfam00717  80 KRLYRDGGGIRLISLNPEYPPIELP-AEDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 111-180 3.91e-20

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 80.30  E-value: 3.91e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937014296 111 FLLRVSGMSMKDIgIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQG-NMVHLLAENEEFAPIVVD 180
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGgGRLRLISDNPAYPPIEID 70
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
82-197 1.86e-17

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 75.22  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  82 VAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKK 160
Cdd:PRK10276   22 VQCGFPSPAADYVEQRIDLNELLIQhPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQL 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1937014296 161 QGNmVHLLAENEEFAPIVVDlRQQSFSIEGLAVGVIR 197
Cdd:PRK10276  102 RPT-VQLIPMNSAYSPITIS-SEDTLDVFGVVTHIVK 136
 
Name Accession Description Interval E-value
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-200 4.42e-101

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 290.46  E-value: 4.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296   1 MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVG 80
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPKGVPLIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  81 RVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLK 159
Cdd:TIGR00498  81 RVAAGEPILAEQHIEEYFPIDFSLLKkPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937014296 160 KQGNMVHLLAENEEFAPIVVDLRqqSFSIEGLAVGVIRNSD 200
Cdd:TIGR00498 161 KDGTKVELKPENPEFDPIVLNAE--DVTILGKVVGVIRNFQ 199
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-198 8.15e-85

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 249.06  E-value: 8.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296   1 MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSpNAAEEHLKALARKGVIEIVSGASRGIRLL--MEEETGIPL 78
Cdd:COG1974     1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLpaSPEVVGLPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  79 VGRVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKR 157
Cdd:COG1974    80 LGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937014296 158 LKKQGNMVHLLAENEEFAPIVVDLrqQSFSIEGLAVGVIRN 198
Cdd:COG1974   160 LYKEGGRVRLQPENPAYPPIIIEG--DDVEILGVVVGVIRR 198
Peptidase_S24 pfam00717
Peptidase S24-like;
77-193 1.88e-40

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 133.48  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  77 PLVGRVAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDiGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTV 155
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSpPGNLFALRVKGDSMEP-GIPDGDLVLVDPSREARNGDIVVARLDGEATV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937014296 156 KRLKKQGNMVHLLAENEEFAPIVVDlRQQSFSIEGLAV 193
Cdd:pfam00717  80 KRLYRDGGGIRLISLNPEYPPIELP-AEDDVEIIGRVV 116
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 4-65 2.22e-29

LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor which prevents expression of DNA repair proteins. The aligned region contains a variant form of the helix-turn-helix DNA binding motif. This domain is found associated with pfam00717 the auto-proteolytic domain of LexA EC:3.4.21.88.


Pssm-ID: 396335 [Multi-domain]  Cd Length: 63  Bit Score: 103.62  E-value: 2.22e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937014296   4 LTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRG 65
Cdd:pfam01726   2 LTERQREVLDFIKASIEETGYPPSRREIARALGLRSPNAAEEHLKALERKGYIERDPGKPRA 63
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 111-180 3.91e-20

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 80.30  E-value: 3.91e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937014296 111 FLLRVSGMSMKDIgIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQG-NMVHLLAENEEFAPIVVD 180
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGgGRLRLISDNPAYPPIEID 70
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
82-197 1.86e-17

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 75.22  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  82 VAAGEPLLAQEHIECHYQVDPAMFK-PSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKK 160
Cdd:PRK10276   22 VQCGFPSPAADYVEQRIDLNELLIQhPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQL 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1937014296 161 QGNmVHLLAENEEFAPIVVDlRQQSFSIEGLAVGVIR 197
Cdd:PRK10276  102 RPT-VQLIPMNSAYSPITIS-SEDTLDVFGVVTHIVK 136
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 76-183 8.69e-17

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 72.69  E-value: 8.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937014296  76 IPLV-GRVAAGEP-LLAQEHIECHYQVDPamFKPSADFLLRVSGMSMKDIgIMDGDLLAVHKTE-DVRNGQIVVARIDDE 152
Cdd:COG2932     1 VPLYdGEASAGGGaFNEVEEPVDKLEFPG--LPPDNLFAVRVSGDSMEPT-IRDGDIVLVDPSDtEIRDGGIYVVRTDGE 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1937014296 153 VTVKRLKKQ-GNMVHLLAENEEFAPIVVDLRQ 183
Cdd:COG2932    78 LLVKRLQRRpDGKLRLISDNPAYPPIEIPPED 109
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 111-180 6.07e-12

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 59.20  E-value: 6.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937014296 111 FLLRVSGMSMKDiGIMDGDLLAVHKT-EDVRNGQIVVARIDD-EVTVKRLKKQG--NMVHLLAENEEFAPIVVD 180
Cdd:cd06462     1 FALRVEGDSMEP-TIPDGDLVLVDKSsYEPKRGDIVVFRLPGgELTVKRVIGLPgeGHYFLLGDNPNSPDSRID 73
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
4-57 4.93e-05

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 42.60  E-value: 4.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937014296   4 LTARQQQVYDLIRDHiaqtgMPPTRAEIAQQLGFrSPNAAEEHLKALARKGVIE 57
Cdd:COG2345    11 ADPTRRRILELLKRA-----GPVTAAELAEALGL-TPNAVRRHLDALEEEGLVE 58
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 9-61 1.35e-03

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: 35.89  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1937014296   9 QQVYDLIRDHIA----QTGMP-PTRAEIAQQLGFrSPNAAEEHLKALARKGVIEIVSG 61
Cdd:cd07377     4 EQIADQLREAILsgelKPGDRlPSERELAEELGV-SRTTVREALRELEAEGLVERRPG 60
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 8-67 6.12e-03

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: 34.13  E-value: 6.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937014296   8 QQQVYDLIRDHIAQT----GMP-PTRAEIAQQLGFrSPNAAEEHLKALARKGVIEIVSGasRGIR 67
Cdd:pfam00392   2 YEQVYARLREDILSGrlrpGDKlPSERELAAEFGV-SRTTVREALRRLEAEGLVERRQG--RGTF 63
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
 4-59 6.75e-03

Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 36.63  E-value: 6.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937014296   4 LTARQQQVYDLIRDHiaqtGMPPTRAEIAQQLGFrSPNAaeehLKALARKGVIEIV 59
Cdd:COG1198   129 RAPKQRRVLEALREH----GGPLTLSELAKEAGV-SRSV----LKALVKKGLLEIE 175
 
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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