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LexA family transcriptional regulator [Thermoanaerobacterium thermosaccharolyticum]

Protein Classification

helix-turn-helix domain-containing protein( domain architecture ID 17581992)

helix-turn-helix domain-containing protein such as an XRE (Xenobiotic Response Element) family transcriptional regulator with a peptidase S24 LexA-like domain

PubMed:  10473770|15808743|10556324

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, ...
 105-259 8.26e-39

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 134.27  E-value: 8.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 105 NKVQEYINQLKEASN-EVDKAKEALHSLLQSSKPVTYVPVYaNKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNV 179
Cdd:COG1974   40 SAVHRHLKALEKKGYlRRDPGKSRAIELLPASPEVVGLPLL-GRVAAGFPIPA-EENIEEYLDLPEELvknpGATFALRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 180 TGDSMINAGIDDGDIVFATINTTADYGDIIIAVSeNGEVTIKYFIQKDNQYFLMPANPDYKPIPF-TNDFRIVGIVTGIL 258
Cdd:COG1974  118 KGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-DGEATVKRLYKEGGRVRLQPENPAYPPIIIeGDDVEILGVVVGVI 196


                 .
gi 505124744 259 K 259
Cdd:COG1974  197 R 197
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
6-84 4.15e-10

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


:

Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 55.00  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744   6 DKVAANIGAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD-QKVFAGTDDDIINIALEQ 84
Cdd:COG1396    2 STLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSlDELLGGADEELPEALLSE 81
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 105-259 8.26e-39

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 134.27  E-value: 8.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 105 NKVQEYINQLKEASN-EVDKAKEALHSLLQSSKPVTYVPVYaNKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNV 179
Cdd:COG1974   40 SAVHRHLKALEKKGYlRRDPGKSRAIELLPASPEVVGLPLL-GRVAAGFPIPA-EENIEEYLDLPEELvknpGATFALRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 180 TGDSMINAGIDDGDIVFATINTTADYGDIIIAVSeNGEVTIKYFIQKDNQYFLMPANPDYKPIPF-TNDFRIVGIVTGIL 258
Cdd:COG1974  118 KGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-DGEATVKRLYKEGGRVRLQPENPAYPPIIIeGDDVEILGVVVGVI 196


                 .
gi 505124744 259 K 259
Cdd:COG1974  197 R 197
Peptidase_S24 pfam00717
Peptidase S24-like;
142-254 1.04e-22

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 89.96  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744  142 PVYaNKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNVTGDSMInAGIDDGDIVFATINTTADYGDIIIAvSENGE 217
Cdd:pfam00717   1 PLI-GRVAAGAPILA-EEEIEGYLPLPESLlsppGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVA-RLDGE 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 505124744  218 VTIKYFIQKDNQYFLMPANPDYKPIPFTN--DFRIVGIV 254
Cdd:pfam00717  77 ATVKRLYRDGGGIRLISLNPEYPPIELPAedDVEIIGRV 115
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 141-259 1.94e-20

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: 86.31  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744  141 VPVYAnKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNVTGDSMINAGIDDGDIVFATINTTADYGDIIIAVSEnG 216
Cdd:TIGR00498  76 VPLIG-RVAAGEPILA-EQHIEEYFPIDFSLlkkpSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMID-G 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 505124744  217 EVTIKYFIQKDNQYFLMPANPDYKPIPFTN-DFRIVGIVTGILK 259
Cdd:TIGR00498 153 EVTVKRFYKDGTKVELKPENPEFDPIVLNAeDVTILGKVVGVIR 196
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
141-259 6.20e-18

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 77.92  E-value: 6.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 141 VPVYANKIPAGYPNEvGTD------DICDWYVV-PSeipADFAVNVTGDSMINAGIDDGDIVFATINTTADYGDIIIAvS 213
Cdd:PRK10276  15 FPLFSDLVQCGFPSP-AADyveqriDLNELLIQhPS---ATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIA-A 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 505124744 214 ENGEVTIKYfIQKDNQYFLMPANPDYKPIPFTND--FRIVGIVTGILK 259
Cdd:PRK10276  90 VDGEFTVKK-LQLRPTVQLIPMNSAYSPITISSEdtLDVFGVVTHIVK 136
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 175-255 3.07e-17

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: 74.52  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 175 FAVNVTGDSMINAgIDDGDIVFATINTTADYGDIIIAVSeNGEVTIK-YFIQKDNQYFLMPANPDYKPIPFTND-FRIVG 252
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKrLQRRGGGRLRLISDNPAYPPIEIDEEeLEIVG 78


                 ...
gi 505124744 253 IVT 255
Cdd:cd06529   79 VVG 81
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
6-84 4.15e-10

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


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 55.00  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744   6 DKVAANIGAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD-QKVFAGTDDDIINIALEQ 84
Cdd:COG1396    2 STLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSlDELLGGADEELPEALLSE 81
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 13-66 6.69e-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: 53.71  E-value: 6.69e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505124744  13 GAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVS 54
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
16-66 1.11e-09

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 53.29  E-value: 1.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 505124744    16 LRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVS 52
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 16-66 1.95e-08

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: 49.46  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 505124744   16 LRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVS 51
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 105-259 8.26e-39

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 134.27  E-value: 8.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 105 NKVQEYINQLKEASN-EVDKAKEALHSLLQSSKPVTYVPVYaNKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNV 179
Cdd:COG1974   40 SAVHRHLKALEKKGYlRRDPGKSRAIELLPASPEVVGLPLL-GRVAAGFPIPA-EENIEEYLDLPEELvknpGATFALRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 180 TGDSMINAGIDDGDIVFATINTTADYGDIIIAVSeNGEVTIKYFIQKDNQYFLMPANPDYKPIPF-TNDFRIVGIVTGIL 258
Cdd:COG1974  118 KGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-DGEATVKRLYKEGGRVRLQPENPAYPPIIIeGDDVEILGVVVGVI 196


                 .
gi 505124744 259 K 259
Cdd:COG1974  197 R 197
Peptidase_S24 pfam00717
Peptidase S24-like;
142-254 1.04e-22

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 89.96  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744  142 PVYaNKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNVTGDSMInAGIDDGDIVFATINTTADYGDIIIAvSENGE 217
Cdd:pfam00717   1 PLI-GRVAAGAPILA-EEEIEGYLPLPESLlsppGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVA-RLDGE 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 505124744  218 VTIKYFIQKDNQYFLMPANPDYKPIPFTN--DFRIVGIV 254
Cdd:pfam00717  77 ATVKRLYRDGGGIRLISLNPEYPPIELPAedDVEIIGRV 115
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 141-259 1.94e-20

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: 86.31  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744  141 VPVYAnKIPAGYPNEVgTDDICDWYVVPSEI----PADFAVNVTGDSMINAGIDDGDIVFATINTTADYGDIIIAVSEnG 216
Cdd:TIGR00498  76 VPLIG-RVAAGEPILA-EQHIEEYFPIDFSLlkkpSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMID-G 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 505124744  217 EVTIKYFIQKDNQYFLMPANPDYKPIPFTN-DFRIVGIVTGILK 259
Cdd:TIGR00498 153 EVTVKRFYKDGTKVELKPENPEFDPIVLNAeDVTILGKVVGVIR 196
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
141-259 6.20e-18

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 77.92  E-value: 6.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 141 VPVYANKIPAGYPNEvGTD------DICDWYVV-PSeipADFAVNVTGDSMINAGIDDGDIVFATINTTADYGDIIIAvS 213
Cdd:PRK10276  15 FPLFSDLVQCGFPSP-AADyveqriDLNELLIQhPS---ATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIA-A 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 505124744 214 ENGEVTIKYfIQKDNQYFLMPANPDYKPIPFTND--FRIVGIVTGILK 259
Cdd:PRK10276  90 VDGEFTVKK-LQLRPTVQLIPMNSAYSPITISSEdtLDVFGVVTHIVK 136
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 175-255 3.07e-17

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: 74.52  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 175 FAVNVTGDSMINAgIDDGDIVFATINTTADYGDIIIAVSeNGEVTIK-YFIQKDNQYFLMPANPDYKPIPFTND-FRIVG 252
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKrLQRRGGGRLRLISDNPAYPPIEIDEEeLEIVG 78


                 ...
gi 505124744 253 IVT 255
Cdd:cd06529   79 VVG 81
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 175-254 4.87e-16

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: 71.14  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 175 FAVNVTGDSMINAgIDDGDIVFA-TINTTADYGDIIIAVSENGEVTIKYFIQK--DNQYFLMPANPDYKPIPFT--NDFR 249
Cdd:cd06462    1 FALRVEGDSMEPT-IPDGDLVLVdKSSYEPKRGDIVVFRLPGGELTVKRVIGLpgEGHYFLLGDNPNSPDSRIDgpPELD 79


                 ....*
gi 505124744 250 IVGIV 254
Cdd:cd06462   80 IVGVV 84
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 141-256 1.58e-15

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 71.15  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744 141 VPVYANKIPAGYPNEVGTDDICDWYVVPSEIPAD-FAVNVTGDSMINAgIDDGDIVFATINTTADYGDIIIAVSENGEVT 219
Cdd:COG2932    1 VPLYDGEASAGGGAFNEVEEPVDKLEFPGLPPDNlFAVRVSGDSMEPT-IRDGDIVLVDPSDTEIRDGGIYVVRTDGELL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 505124744 220 IK-YFIQKDNQYFLMPANPDYKPIPFT----NDFRIVGIVTG 256
Cdd:COG2932   80 VKrLQRRPDGKLRLISDNPAYPPIEIPpedaDEIEIIGRVVW 121
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
6-84 4.15e-10

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


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 55.00  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505124744   6 DKVAANIGAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD-QKVFAGTDDDIINIALEQ 84
Cdd:COG1396    2 STLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSlDELLGGADEELPEALLSE 81
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 13-66 6.69e-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: 53.71  E-value: 6.69e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505124744  13 GAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVS 54
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
16-66 1.11e-09

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 53.29  E-value: 1.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 505124744    16 LRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVS 52
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 16-66 1.95e-08

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: 49.46  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 505124744   16 LRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVS 51
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 1-66 1.04e-07

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: 48.01  E-value: 1.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505124744   1 MDKLHDK-VAANIGAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVD 66
Cdd:COG1813    1 MAKESTGeLVEDYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGIS 67
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 13-75 1.91e-05

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: 41.51  E-value: 1.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505124744   13 GAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVDQK-VFAGTDD 75
Cdd:pfam12844   1 GERLRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLYKIAELLGVPANwLLQGEGE 64
HigA COG5499
Antitoxin component HigA of the HigAB toxin-antitoxin module, contains an N-terminal HTH ...
 14-70 6.06e-05

Antitoxin component HigA of the HigAB toxin-antitoxin module, contains an N-terminal HTH domain [Defense mechanisms];


Pssm-ID: 444250  Cd Length: 127  Bit Score: 41.74  E-value: 6.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505124744  14 AVLRQLKERNNVTIHQIAEAVNvTDGAVAKYLSGERKPNKQVIKRLAEFFHVDQKVF 70
Cdd:COG5499   68 EALKFLMEQHGLTQKDLAPEIG-SKSRVSEILNGKRSLTLEMIRKLAERFGIPAELF 123
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 4-76 1.72e-04

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: 39.62  E-value: 1.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505124744   4 LHDKVAANIGAVLRQLKERNNVTIHQIAEAVNVTDGAVAKYLSGERKPNKQVIKRLAEFFHVDQKVFAGTDDD 76
Cdd:COG3620   10 VTVSPDDTLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALGKELSAVLVVDDG 82
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 91-143 3.32e-03

Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 36.82  E-value: 3.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505124744  91 QLNALKESIAEaplnkVQEYINQLKEASNEVDKAKEALhSLLQSSKPVTYVPV 143
Cdd:cd00584    4 QLQELREQIEA-----LQEEIEQLEEEQAEIDEAKEAL-EELKKEGSEVLVPL 50
 
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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