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Conserved domains on  [gi|21885286|gb|AAL59692|]
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transcriptional repressor [Vibrio cholerae]

Protein Classification

LexA family transcriptional regulator( domain architecture ID 11449429)

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

CATH:  1.10.10.10
Gene Ontology:  GO:0003677
SCOP:  4000321

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-214 9.18e-45

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 147.75  E-value: 9.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286   1 MKTLSER-------LNHALQLTGV--TQSELARRIGIKQQSISQIcsgksarsrytmqiAEALRvNAHWLATGDGEiGLG 71
Cdd:COG1974   1 MKKLTKRqreildfIKEYIRERGYppSQREIAEALGLSSSAVHRH--------------LKALE-KKGYLRRDPGK-SRA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  72 VGNVEVGPDIKGrIPLINWVQAGDWTEiaegfAHEDAEEWREVTG---KAHEGCFALRVKGDSMENPSgkksIPEGAVIV 148
Cdd:COG1974  65 IELLPASPEVVG-LPLLGRVAAGFPIP-----AEENIEEYLDLPEelvKNPGATFALRVKGDSMIDAG----ILDGDLVI 134

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286 149 VDPELPYSSGSLVVARLDDskEATFKQLVIDGEQKYLKPLNPQYPAIPING-NCTIIGVVRQAIIDF 214
Cdd:COG1974 135 VDRQLEAENGDIVVALIDG--EATVKRLYKEGGRVRLQPENPAYPPIIIEGdDVEILGVVVGVIRRL 199
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-214 9.18e-45

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 147.75  E-value: 9.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286   1 MKTLSER-------LNHALQLTGV--TQSELARRIGIKQQSISQIcsgksarsrytmqiAEALRvNAHWLATGDGEiGLG 71
Cdd:COG1974   1 MKKLTKRqreildfIKEYIRERGYppSQREIAEALGLSSSAVHRH--------------LKALE-KKGYLRRDPGK-SRA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  72 VGNVEVGPDIKGrIPLINWVQAGDWTEiaegfAHEDAEEWREVTG---KAHEGCFALRVKGDSMENPSgkksIPEGAVIV 148
Cdd:COG1974  65 IELLPASPEVVG-LPLLGRVAAGFPIP-----AEENIEEYLDLPEelvKNPGATFALRVKGDSMIDAG----ILDGDLVI 134

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286 149 VDPELPYSSGSLVVARLDDskEATFKQLVIDGEQKYLKPLNPQYPAIPING-NCTIIGVVRQAIIDF 214
Cdd:COG1974 135 VDRQLEAENGDIVVALIDG--EATVKRLYKEGGRVRLQPENPAYPPIIIEGdDVEILGVVVGVIRRL 199
Peptidase_S24 pfam00717
Peptidase S24-like;
86-207 1.50e-33

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 116.54  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286    86 PLINWVQAGDWTEIAEGFahEDAEEWREVTGKAHEGCFALRVKGDSMENpsgkkSIPEGAVIVVDPELPYSSGSLVVARL 165
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEI--EGYLPLPESLLSPPGNLFALRVKGDSMEP-----GIPDGDLVLVDPSREARNGDIVVARL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21885286   166 DDskEATFKQLVIDGEQKYLKPLNPQYPAIPING--NCTIIGVV 207
Cdd:pfam00717  74 DG--EATVKRLYRDGGGIRLISLNPEYPPIELPAedDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 123-207 4.49e-23

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: 88.38  E-value: 4.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286 123 FALRVKGDSMENPsgkksIPEGAVIVVDPELPYSSGSLVVARLDDskEATFKQLVIDGEQK-YLKPLNPQYPAIPING-N 200
Cdd:cd06529   1 FALRVKGDSMEPT-----IPDGDLVLVDPSDTPRDGDIVVARLDG--ELTVKRLQRRGGGRlRLISDNPAYPPIEIDEeE 73


                ....*..
gi 21885286 201 CTIIGVV 207
Cdd:cd06529  74 LEIVGVV 80
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 75-207 4.32e-12

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: 62.43  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286    75 VEVGPDIKGRIPLINWVQAGDwteiaEGFAHEDAEEWREVTG---KAHEGCFALRVKGDSMENpsgkKSIPEGAVIVVDP 151
Cdd:TIGR00498  66 IRILDDEPKGVPLIGRVAAGE-----PILAEQHIEEYFPIDFsllKKPSAVFLLKVMGDSMVD----AGICDGDLLIVRS 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286   152 ELPYSSGSLVVARLDDskEATFKQLVIDGEQKYLKPLNPQYPAIPIN-GNCTIIGVV 207
Cdd:TIGR00498 137 QKDARNGEIVAAMIDG--EVTVKRFYKDGTKVELKPENPEFDPIVLNaEDVTILGKV 191
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-61 3.74e-08

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 48.28  E-value: 3.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21885286      7 RLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTMQ-IAEALRVNAHWL 61
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKkLAKALGVSLDEL 56
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
121-207 9.38e-06

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 43.63  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  121 GCFALRVKGDSMENpsgkKSIPEGAVIVVDPELPYSSGSLVVARLDDskEATFKQLvidgeQKY----LKPLNPQYPAIP 196
Cdd:PRK10276  50 ATYFVKASGDSMID----AGISDGDLLIVDSAITASHGDIVIAAVDG--EFTVKKL-----QLRptvqLIPMNSAYSPIT 118

                         90
                 ....*....|...
gi 21885286  197 INGNCT--IIGVV 207
Cdd:PRK10276 119 ISSEDTldVFGVV 131
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-214 9.18e-45

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 147.75  E-value: 9.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286   1 MKTLSER-------LNHALQLTGV--TQSELARRIGIKQQSISQIcsgksarsrytmqiAEALRvNAHWLATGDGEiGLG 71
Cdd:COG1974   1 MKKLTKRqreildfIKEYIRERGYppSQREIAEALGLSSSAVHRH--------------LKALE-KKGYLRRDPGK-SRA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  72 VGNVEVGPDIKGrIPLINWVQAGDWTEiaegfAHEDAEEWREVTG---KAHEGCFALRVKGDSMENPSgkksIPEGAVIV 148
Cdd:COG1974  65 IELLPASPEVVG-LPLLGRVAAGFPIP-----AEENIEEYLDLPEelvKNPGATFALRVKGDSMIDAG----ILDGDLVI 134

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286 149 VDPELPYSSGSLVVARLDDskEATFKQLVIDGEQKYLKPLNPQYPAIPING-NCTIIGVVRQAIIDF 214
Cdd:COG1974 135 VDRQLEAENGDIVVALIDG--EATVKRLYKEGGRVRLQPENPAYPPIIIEGdDVEILGVVVGVIRRL 199
Peptidase_S24 pfam00717
Peptidase S24-like;
86-207 1.50e-33

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 116.54  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286    86 PLINWVQAGDWTEIAEGFahEDAEEWREVTGKAHEGCFALRVKGDSMENpsgkkSIPEGAVIVVDPELPYSSGSLVVARL 165
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEI--EGYLPLPESLLSPPGNLFALRVKGDSMEP-----GIPDGDLVLVDPSREARNGDIVVARL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21885286   166 DDskEATFKQLVIDGEQKYLKPLNPQYPAIPING--NCTIIGVV 207
Cdd:pfam00717  74 DG--EATVKRLYRDGGGIRLISLNPEYPPIELPAedDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 123-207 4.49e-23

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: 88.38  E-value: 4.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286 123 FALRVKGDSMENPsgkksIPEGAVIVVDPELPYSSGSLVVARLDDskEATFKQLVIDGEQK-YLKPLNPQYPAIPING-N 200
Cdd:cd06529   1 FALRVKGDSMEPT-----IPDGDLVLVDPSDTPRDGDIVVARLDG--ELTVKRLQRRGGGRlRLISDNPAYPPIEIDEeE 73


                ....*..
gi 21885286 201 CTIIGVV 207
Cdd:cd06529  74 LEIVGVV 80
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 85-207 9.67e-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: 73.07  E-value: 9.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  85 IPLIN-WVQAGDWTEIAegfaHEDAEEWREVTGKAHEGCFALRVKGDSMEnPsgkkSIPEGAVIVVDPELP-YSSGSLVV 162
Cdd:COG2932   1 VPLYDgEASAGGGAFNE----VEEPVDKLEFPGLPPDNLFAVRVSGDSME-P----TIRDGDIVLVDPSDTeIRDGGIYV 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21885286 163 ARLDDskEATFKQLVIDGEQKY-LKPLNPQYPAIPING----NCTIIGVV 207
Cdd:COG2932  72 VRTDG--ELLVKRLQRRPDGKLrLISDNPAYPPIEIPPedadEIEIIGRV 119
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 123-207 3.51e-14

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: 65.36  E-value: 3.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286 123 FALRVKGDSMENpsgkkSIPEGAVIVVDPELP-YSSGSLVVARLDDsKEATFKQLVIDGEQK--YLKPLNPQYPAIPING 199
Cdd:cd06462   1 FALRVEGDSMEP-----TIPDGDLVLVDKSSYePKRGDIVVFRLPG-GELTVKRVIGLPGEGhyFLLGDNPNSPDSRIDG 74

                        90
                ....*....|
gi 21885286 200 --NCTIIGVV 207
Cdd:cd06462  75 ppELDIVGVV 84
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 75-207 4.32e-12

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: 62.43  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286    75 VEVGPDIKGRIPLINWVQAGDwteiaEGFAHEDAEEWREVTG---KAHEGCFALRVKGDSMENpsgkKSIPEGAVIVVDP 151
Cdd:TIGR00498  66 IRILDDEPKGVPLIGRVAAGE-----PILAEQHIEEYFPIDFsllKKPSAVFLLKVMGDSMVD----AGICDGDLLIVRS 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286   152 ELPYSSGSLVVARLDDskEATFKQLVIDGEQKYLKPLNPQYPAIPIN-GNCTIIGVV 207
Cdd:TIGR00498 137 QKDARNGEIVAAMIDG--EVTVKRFYKDGTKVELKPENPEFDPIVLNaEDVTILGKV 191
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-67 2.54e-10

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 55.00  E-value: 2.54e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21885286   1 MKTLSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTM-QIAEALRVNAHWLATGDGE 67
Cdd:COG1396   5 KKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLlKLAKALGVSLDELLGGADE 72
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 5-61 7.42e-10

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 52.94  E-value: 7.42e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21885286   5 SERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTMQ-IAEALRVNAHWL 61
Cdd:cd00093   1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEkLAKALGVSLDEL 58
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-66 1.11e-08

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 50.23  E-value: 1.11e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21885286   1 MKTLSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTM-QIAEALRVNAHWLATGDG 66
Cdd:COG1476   2 KKKLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELAlKIARALGVSLEELFSLEE 68
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-61 3.74e-08

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 48.28  E-value: 3.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21885286      7 RLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTMQ-IAEALRVNAHWL 61
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKkLAKALGVSLDEL 56
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 3-72 4.80e-07

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 46.55  E-value: 4.80e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21885286   3 TLSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTMQ-IAEALRVNAHWLATGDGEIGLGV 72
Cdd:COG3620  17 TLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEkIAEALGKELSAVLVVDDGKLVGI 87
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 16-61 5.51e-07

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 45.22  E-value: 5.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 21885286    16 GVTQSELARRIGIKQQSISQICSGKSARSRYTMQ-IAEALRVNAHWL 61
Cdd:pfam01381   9 GLSQEELAEKLGVSRSTISKIENGKREPSLETLKkLAEALGVSLDEL 55
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 6-67 4.39e-06

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 43.05  E-value: 4.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21885286     6 ERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTM-QIAEALRVNAHWLATGDGE 67
Cdd:pfam12844   2 ERLRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLyKIAELLGVPANWLLQGEGE 64
Phage_CI_repr pfam07022
Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI ...
 6-68 8.93e-06

Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI repressor proteins and related bacterial sequences. The CI repressor is known to function as a transcriptional switch, determining whether transcription is lytic or lysogenic.


Pssm-ID: 311152  Cd Length: 65  Bit Score: 41.93  E-value: 8.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21885286     6 ERLNHALQLTGV-TQSELARRIGIKQQSISQICSGKSARSRYTMQIAEALRVNAHWLATGDGEI 68
Cdd:pfam07022   1 AVIERLMKAYGFkSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGDGEL 64
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
121-207 9.38e-06

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 43.63  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885286  121 GCFALRVKGDSMENpsgkKSIPEGAVIVVDPELPYSSGSLVVARLDDskEATFKQLvidgeQKY----LKPLNPQYPAIP 196
Cdd:PRK10276  50 ATYFVKASGDSMID----AGISDGDLLIVDSAITASHGDIVIAAVDG--EFTVKKL-----QLRptvqLIPMNSAYSPIT 118

                         90
                 ....*....|...
gi 21885286  197 INGNCT--IIGVV 207
Cdd:PRK10276 119 ISSEDTldVFGVV 131
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
 12-42 3.17e-05

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 40.95  E-value: 3.17e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 21885286  12 LQLTGVTQSELARRIGIKQQSISQICSGKSA 42
Cdd:COG3093  18 LEPLGLSQTELAKALGVSRQRISEILNGKRA 48
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 1-68 3.34e-05

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 43.96  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21885286    1 MKTLSERLNHALQLTGVTQSELARRI---GIK--QQSISQICSGKSARSRYTMQI-AEALRVNAHWLATGDGEI 68
Cdd:PRK13355   1 KTTFAERLKQAMKARGLKQEDLVHAAearGVKlgKSHISQYVSGKTGPRRDVLPFlAAILGVSEDWLLGGESPA 74
PRK09706 PRK09706
transcriptional repressor DicA; Reviewed
 2-65 1.03e-04

transcriptional repressor DicA; Reviewed


Pssm-ID: 182039 [Multi-domain]  Cd Length: 135  Bit Score: 40.99  E-value: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21885286    2 KTLSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSA-RSRYTMQIAEALRVNAHWLATGD 65
Cdd:PRK09706   4 LTLGQRIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEpTGKNLFALAKALQCSPTWLLFGD 68
HTH_31 pfam13560
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
 4-56 1.78e-04

Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433309 [Multi-domain]  Cd Length: 64  Bit Score: 38.28  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21885286     4 LSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTM--QIAEALRV 56
Cdd:pfam13560   2 LGARLRRLRERAGLSQEALARRLGVSRSTLSRLETGRRGRPSPAVveRLARALGV 56
PHA00542 PHA00542
putative Cro-like protein
 10-51 2.25e-04

putative Cro-like protein


Pssm-ID: 106954  Cd Length: 82  Bit Score: 38.63  E-value: 2.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 21885286   10 HALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTMQIA 51
Cdd:PHA00542  25 CALIRAGWSQEQIADATDVSQPTICRIYSGRHKDPRYSVVEK 66
YdaS COG4197
DNA-binding transcriptional regulator YdaS, prophage-encoded, Cro superfamily [Transcription];
8-41 3.07e-04

DNA-binding transcriptional regulator YdaS, prophage-encoded, Cro superfamily [Transcription];


Pssm-ID: 443351  Cd Length: 68  Bit Score: 37.97  E-value: 3.07e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 21885286   8 LNHALQLTGvTQSELARRIGIKQQSISQICSGKS 41
Cdd:COG4197   1 LEKAIEALG-SQSALARALGVSQQAVSQWLNGKR 33
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
 7-57 1.60e-03

Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433211 [Multi-domain]  Cd Length: 63  Bit Score: 35.59  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21885286     7 RLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYT--MQIAEALRVN 57
Cdd:pfam13443   1 KLRKLMADRGISKSDLARATGISRATLSRLRKGKPKRVSLDtlDKICDALGCQ 53
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 3-57 1.69e-03

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 36.07  E-value: 1.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21885286   3 TLSERLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYTM-QIAEALRVN 57
Cdd:COG1813  12 DYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLrKLEKALGIS 67
PRK09726 PRK09726
type II toxin-antitoxin system antitoxin HipB;
2-34 3.72e-03

type II toxin-antitoxin system antitoxin HipB;


Pssm-ID: 182049  Cd Length: 88  Bit Score: 35.34  E-value: 3.72e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 21885286    2 KTLSERLNHALQLTGVTQSELARRIGIKQQSIS 34
Cdd:PRK09726  11 TQLANAMKLVRQQNGWTQSELAKKIGIKQATIS 43
YozG COG3655
DNA-binding transcriptional regulator, XRE family [Transcription];
7-57 4.22e-03

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


Pssm-ID: 442872 [Multi-domain]  Cd Length: 69  Bit Score: 34.73  E-value: 4.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21885286   7 RLNHALQLTGVTQSELARRIGIKQQSISQICSGKSARSRYT--MQIAEALRVN 57
Cdd:COG3655   5 KLDELLAERGMTKKELAEATGISRATLSRLKNGKAKAVRLDtlEKICKALDCQ 57
antidote_HigA TIGR02607
addiction module antidote protein, HigA family; Members of this family form a distinct clade ...
 6-42 5.50e-03

addiction module antidote protein, HigA family; Members of this family form a distinct clade within the larger family HTH_3 of helix-turn-helix proteins, described by pfam01381. Members of this clade are strictly bacterial and nearly always shorter than 110 amino acids. This family includes the characterized member HigA, without which the killer protein HigB cannot be cloned. The hig (host inhibition of growth) system is noted to be unusual in that killer protein is uncoded by the upstream member of the gene pair. [Regulatory functions, DNA interactions, Regulatory functions, Protein interactions, Mobile and extrachromosomal element functions, Other]


Pssm-ID: 274228 [Multi-domain]  Cd Length: 78  Bit Score: 34.52  E-value: 5.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21885286     6 ERLNHA-LQLTGVTQSELARRIGIKQQSISQICSGKSA 42
Cdd:TIGR02607   7 EILLEEfLEPLGLSVRALAKALGVSRSTLSRIVNGRAA 44
 
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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