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Conserved domains on  [gi|446433235|ref|WP_000511090|]
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MULTISPECIES: XRE family transcriptional regulator [Staphylococcus]

Protein Classification

XRE family transcriptional regulator( domain architecture ID 10056342)

XRE family transcriptional regulator containing an N-terminal XRE family helix-turn-helix (HTH) DNA-binding domain, and a C-terminal S24 family peptidase domain similar to LexA, that carries out autolysis using a serine/lysine dyad, and is involved in the SOS response leading to the repair of single-stranded DNA within the cell

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S24 pfam00717
Peptidase S24-like;
130-242 1.28e-28

Peptidase S24-like;


:

Pssm-ID: 425835  Cd Length: 116  Bit Score: 104.59  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235  130 GATGAGIGEELYDDILHEEVFFKEDETPSNADFCILVNGDSMEPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVD 209
Cdd:pfam00717   4 GRVAAGAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLY 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446433235  210 ICEDYINLVSLNPKYDDIKVASFSNIKVMGKVV 242
Cdd:pfam00717  84 RDGGGIRLISLNPEYPPIELPAEDDVEIIGRVV 116
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-74 6.30e-13

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


:

Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 61.79  E-value: 6.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446433235   1 MGIGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESN 74
Cdd:COG1476    3 KKLGNRLKELRKERGLTQEELA--------ELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSLEE 68
 
Name Accession Description Interval E-value
Peptidase_S24 pfam00717
Peptidase S24-like;
130-242 1.28e-28

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 104.59  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235  130 GATGAGIGEELYDDILHEEVFFKEDETPSNADFCILVNGDSMEPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVD 209
Cdd:pfam00717   4 GRVAAGAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLY 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446433235  210 ICEDYINLVSLNPKYDDIKVASFSNIKVMGKVV 242
Cdd:pfam00717  84 RDGGGIRLISLNPEYPPIELPAEDDVEIIGRVV 116
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 133-242 3.49e-22

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 88.10  E-value: 3.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 133 GAGIGEELYDDILHEEVFFkeDETPSNADFCILVNGDSMEPMLKQGTYAFIKKEDS-IKDGTIALVVLDGVSLIKRV-DI 210
Cdd:COG2932    9 SAGGGAFNEVEEPVDKLEF--PGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTeIRDGGIYVVRTDGELLVKRLqRR 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446433235 211 CEDYINLVSLNPKYDDIKVAS--FSNIKVMGKVV 242
Cdd:COG2932   87 PDGKLRLISDNPAYPPIEIPPedADEIEIIGRVV 120
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 162-242 6.71e-16

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: 70.28  E-value: 6.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 162 FCILVNGDSMEPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVDIC-EDYINLVSLNPKYDDIKVaSFSNIKVMGK 240
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRgGGRLRLISDNPAYPPIEI-DEEELEIVGV 79


                 ..
gi 446433235 241 VV 242
Cdd:cd06529   80 VG 81
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-74 6.30e-13

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


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 61.79  E-value: 6.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446433235   1 MGIGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESN 74
Cdd:COG1476    3 KKLGNRLKELRKERGLTQEELA--------ELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSLEE 68
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 4-69 4.06e-12

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: 59.49  E-value: 4.06e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446433235   4 GEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:cd00093    1 GERLKELRKEKGLTQEELA--------EKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-69 3.56e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 54.06  E-value: 3.56e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446433235     7 LKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:smart00530   2 LKELREEKGLTQEELA--------EKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 7-69 3.41e-09

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: 51.39  E-value: 3.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446433235    7 LKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:pfam01381   1 LKELREELGLSQEELA--------EKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 4-85 9.50e-06

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 45.88  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235   4 GEGLKKLRKNKNMTMEQL---ATDLNnkypdlMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESNTTYKDD 80
Cdd:PRK13355   5 AERLKQAMKARGLKQEDLvhaAEARG------VKLGKSHISQYVSGKTGPRRDVLPFLAAILGVSEDWLLGGESPADQES 78


                 ....*
gi 446433235  81 NDITS 85
Cdd:PRK13355  79 DASAV 83
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 146-242 9.65e-05

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: 42.01  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235  146 HEEVFFKEDETP---SNADFCILVNGDSM-EPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVDICEDYINLVSLN 221
Cdd:TIGR00498  93 HIEEYFPIDFSLlkkPSAVFLLKVMGDSMvDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFYKDGTKVELKPEN 172

                          90       100
                  ....*....|....*....|.
gi 446433235  222 PKYDDIkVASFSNIKVMGKVV 242
Cdd:TIGR00498 173 PEFDPI-VLNAEDVTILGKVV 192
 
Name Accession Description Interval E-value
Peptidase_S24 pfam00717
Peptidase S24-like;
130-242 1.28e-28

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 104.59  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235  130 GATGAGIGEELYDDILHEEVFFKEDETPSNADFCILVNGDSMEPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVD 209
Cdd:pfam00717   4 GRVAAGAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLY 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446433235  210 ICEDYINLVSLNPKYDDIKVASFSNIKVMGKVV 242
Cdd:pfam00717  84 RDGGGIRLISLNPEYPPIELPAEDDVEIIGRVV 116
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 133-242 3.49e-22

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 88.10  E-value: 3.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 133 GAGIGEELYDDILHEEVFFkeDETPSNADFCILVNGDSMEPMLKQGTYAFIKKEDS-IKDGTIALVVLDGVSLIKRV-DI 210
Cdd:COG2932    9 SAGGGAFNEVEEPVDKLEF--PGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTeIRDGGIYVVRTDGELLVKRLqRR 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446433235 211 CEDYINLVSLNPKYDDIKVAS--FSNIKVMGKVV 242
Cdd:COG2932   87 PDGKLRLISDNPAYPPIEIPPedADEIEIIGRVV 120
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 162-242 6.71e-16

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: 70.28  E-value: 6.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 162 FCILVNGDSMEPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVDIC-EDYINLVSLNPKYDDIKVaSFSNIKVMGK 240
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRgGGRLRLISDNPAYPPIEI-DEEELEIVGV 79


                 ..
gi 446433235 241 VV 242
Cdd:cd06529   80 VG 81
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 158-242 1.36e-13

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 67.25  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 158 SNADFCILVNGDSM-EPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVDICEDYINLVSLNPKYDDIKVASfSNIK 236
Cdd:COG1974  109 PGATFALRVKGDSMiDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIIIEG-DDVE 187


                 ....*.
gi 446433235 237 VMGKVV 242
Cdd:COG1974  188 ILGVVV 193
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-74 6.30e-13

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


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 61.79  E-value: 6.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446433235   1 MGIGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESN 74
Cdd:COG1476    3 KKLGNRLKELRKERGLTQEELA--------ELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSLEE 68
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 162-241 8.22e-13

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: 62.28  E-value: 8.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235 162 FCILVNGDSMEPMLKQGTYAFIKKED-SIKDGTIALVVLDGVSL-IKRV--DICEDYINLVSLNPKYDDIKVASFSNIKV 237
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSyEPKRGDIVVFRLPGGELtVKRVigLPGEGHYFLLGDNPNSPDSRIDGPPELDI 80


                 ....
gi 446433235 238 MGKV 241
Cdd:cd06462   81 VGVV 84
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-76 2.14e-12

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


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 61.17  E-value: 2.14e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446433235   1 MGIGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESNTT 76
Cdd:COG1396    6 KALGERLRELRKARGLTQEELA--------ERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELLGGADEE 73
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 4-69 4.06e-12

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: 59.49  E-value: 4.06e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446433235   4 GEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:cd00093    1 GERLKELRKEKGLTQEELA--------EKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-69 3.56e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 54.06  E-value: 3.56e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446433235     7 LKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:smart00530   2 LKELREEKGLTQEELA--------EKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 7-69 3.41e-09

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: 51.39  E-value: 3.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446433235    7 LKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:pfam01381   1 LKELREELGLSQEELA--------EKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 4-70 1.48e-08

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: 49.98  E-value: 1.48e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446433235    4 GEGLKKLRKNKNMTMEQLATDLnnkypdlmKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLY 70
Cdd:pfam12844   1 GERLRKAREERGLTQEELAERL--------GISRSQLSAIENGKSVPPAETLYKIAELLGVPANWLL 59
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 3-66 1.94e-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: 47.24  E-value: 1.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446433235   3 IGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKI 66
Cdd:COG1813   13 YGERIREAREARGLSQEELA--------EKLGVSESTIRRIERGEATPSLDTLRKLEKALGISL 68
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 4-85 9.50e-06

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 45.88  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235   4 GEGLKKLRKNKNMTMEQL---ATDLNnkypdlMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDLYSESNTTYKDD 80
Cdd:PRK13355   5 AERLKQAMKARGLKQEDLvhaAEARG------VKLGKSHISQYVSGKTGPRRDVLPFLAAILGVSEDWLLGGESPADQES 78


                 ....*
gi 446433235  81 NDITS 85
Cdd:PRK13355  79 DASAV 83
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 3-69 1.48e-05

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: 42.70  E-value: 1.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446433235   3 IGEGLKKLRKNKNMTMEQLAtdlnnkypDLMKLTKGKISKWENEKEEPRLSTAKILAEYFNVKINDL 69
Cdd:COG3620   18 LGEALRLMRKELGLSQLPVA--------ELVGVSQSDILRIESGKRDPTVSTLEKIAEALGKELSAV 76
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 146-242 9.65e-05

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: 42.01  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446433235  146 HEEVFFKEDETP---SNADFCILVNGDSM-EPMLKQGTYAFIKKEDSIKDGTIALVVLDGVSLIKRVDICEDYINLVSLN 221
Cdd:TIGR00498  93 HIEEYFPIDFSLlkkPSAVFLLKVMGDSMvDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFYKDGTKVELKPEN 172

                          90       100
                  ....*....|....*....|.
gi 446433235  222 PKYDDIkVASFSNIKVMGKVV 242
Cdd:TIGR00498 173 PEFDPI-VLNAEDVTILGKVV 192
 
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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