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Conserved domains on  [gi|695661951|ref|WP_032623258|]
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MULTISPECIES: S24 family peptidase [Enterobacter]

Protein Classification

XRE family transcriptional regulator( domain architecture ID 11443577)

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

Gene Ontology:  GO:0003677

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
91-220 3.01e-34

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


:

Pssm-ID: 442176  Cd Length: 121  Bit Score: 118.91  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951  91 VELLDVSASAGMGHIQGSDvvDVIRSIEynneraaalFGGRTPDTVKVINVRGDSMADTIEPGDLIFVDISINEFDGDGI 170
Cdd:COG2932    1 VPLYDGEASAGGGAFNEVE--EPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695661951 171 YVFGFDDKIYVKRLQMIPD-KILVISDNPKYREWSVDKSNEDRFYVFGKVM 220
Cdd:COG2932   70 YVVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIEIIGRVV 120
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-71 5.68e-18

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


:

Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 75.42  E-value: 5.68e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAELFTPSPNETT 71
Cdd:COG1396    6 KALGERLRELRKARGLTQEELAERLGVSRSTISRIERGR-RNPSLETLLKLAKALGVSLDELLGGADEELP 75
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
91-220 3.01e-34

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 118.91  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951  91 VELLDVSASAGMGHIQGSDvvDVIRSIEynneraaalFGGRTPDTVKVINVRGDSMADTIEPGDLIFVDISINEFDGDGI 170
Cdd:COG2932    1 VPLYDGEASAGGGAFNEVE--EPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695661951 171 YVFGFDDKIYVKRLQMIPD-KILVISDNPKYREWSVDKSNEDRFYVFGKVM 220
Cdd:COG2932   70 YVVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIEIIGRVV 120
Peptidase_S24 pfam00717
Peptidase S24-like;
97-220 1.46e-21

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 86.10  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951   97 SASAGMGHIQGSDVVDVIRSIEYNNERAAALFggrtpdtvkVINVRGDSMADTIEPGDLIFVDISINEFDGDgIYVFGFD 176
Cdd:pfam00717   5 RVAAGAPILAEEEIEGYLPLPESLLSPPGNLF---------ALRVKGDSMEPGIPDGDLVLVDPSREARNGD-IVVARLD 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695661951  177 DKIYVKRLQMIPDKILVISDNPKYREWSVDKsnEDRFYVFGKVM 220
Cdd:pfam00717  75 GEATVKRLYRDGGGIRLISLNPEYPPIELPA--EDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
138-217 1.25e-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: 82.22  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 138 VINVRGDSMADTIEPGDLIFVDISINEFDGDgIYVFGFDDKIYVKRLQMIPD-KILVISDNPKYREWSVDKSNEDRFYVF 216
Cdd:cd06529    2 ALRVKGDSMEPTIPDGDLVLVDPSDTPRDGD-IVVARLDGELTVKRLQRRGGgRLRLISDNPAYPPIEIDEEELEIVGVV 80

                 .
gi 695661951 217 G 217
Cdd:cd06529   81 G 81
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-71 5.68e-18

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


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 75.42  E-value: 5.68e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAELFTPSPNETT 71
Cdd:COG1396    6 KALGERLRELRKARGLTQEELAERLGVSRSTISRIERGR-RNPSLETLLKLAKALGVSLDELLGGADEELP 75
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
6-62 2.70e-13

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 62.54  E-value: 2.70e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 695661951     6 RIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKsFTEQSLSKYATALGVSVAEL 62
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVSLDEL 56
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
4-62 3.70e-13

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: 62.19  E-value: 3.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695661951   4 GNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAEL 62
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGK-RNPSLETLEKLAKALGVSLDEL 58
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
6-67 5.81e-12

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: 59.09  E-value: 5.81e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695661951    6 RIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKSFTEQSLSKYATALGVSVAELFTPSP 67
Cdd:pfam13443   1 KLRKLMADRGISKSDLARATGISRATLSRLRKGKPKRVSLDTLDKICDALGCQPGDLLEYVP 62
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
133-219 1.27e-07

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 49.41  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 133 PDTVKVINVRGDSMADT-IEPGDLIFVDISINEFDGDgIYVFGFDDKIYVKRLQMIPdKILVISDNPKYREWSVdkSNED 211
Cdd:PRK10276  48 PSATYFVKASGDSMIDAgISDGDLLIVDSAITASHGD-IVIAAVDGEFTVKKLQLRP-TVQLIPMNSAYSPITI--SSED 123

                 ....*...
gi 695661951 212 RFYVFGKV 219
Cdd:PRK10276 124 TLDVFGVV 131
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
102-220 2.20e-03

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: 37.77  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951  102 MGHIQGSDVVDVIRSIEYNNERAAALFGgrTPDTVKVINVRGDSMADT-IEPGDLIFVDiSINEFDGDGIYVFGFDDKIY 180
Cdd:TIGR00498  79 IGRVAAGEPILAEQHIEEYFPIDFSLLK--KPSAVFLLKVMGDSMVDAgICDGDLLIVR-SQKDARNGEIVAAMIDGEVT 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 695661951  181 VKRLQMIPDKILVISDNPKYREWSVDKSNedrFYVFGKVM 220
Cdd:TIGR00498 156 VKRFYKDGTKVELKPENPEFDPIVLNAED---VTILGKVV 192
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
91-220 3.01e-34

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 118.91  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951  91 VELLDVSASAGMGHIQGSDvvDVIRSIEynneraaalFGGRTPDTVKVINVRGDSMADTIEPGDLIFVDISINEFDGDGI 170
Cdd:COG2932    1 VPLYDGEASAGGGAFNEVE--EPVDKLE---------FPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695661951 171 YVFGFDDKIYVKRLQMIPD-KILVISDNPKYREWSVDKSNEDRFYVFGKVM 220
Cdd:COG2932   70 YVVRTDGELLVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIEIIGRVV 120
Peptidase_S24 pfam00717
Peptidase S24-like;
97-220 1.46e-21

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 86.10  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951   97 SASAGMGHIQGSDVVDVIRSIEYNNERAAALFggrtpdtvkVINVRGDSMADTIEPGDLIFVDISINEFDGDgIYVFGFD 176
Cdd:pfam00717   5 RVAAGAPILAEEEIEGYLPLPESLLSPPGNLF---------ALRVKGDSMEPGIPDGDLVLVDPSREARNGD-IVVARLD 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695661951  177 DKIYVKRLQMIPDKILVISDNPKYREWSVDKsnEDRFYVFGKVM 220
Cdd:pfam00717  75 GEATVKRLYRDGGGIRLISLNPEYPPIELPA--EDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
138-217 1.25e-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: 82.22  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 138 VINVRGDSMADTIEPGDLIFVDISINEFDGDgIYVFGFDDKIYVKRLQMIPD-KILVISDNPKYREWSVDKSNEDRFYVF 216
Cdd:cd06529    2 ALRVKGDSMEPTIPDGDLVLVDPSDTPRDGD-IVVARLDGELTVKRLQRRGGgRLRLISDNPAYPPIEIDEEELEIVGVV 80

                 .
gi 695661951 217 G 217
Cdd:cd06529   81 G 81
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-71 5.68e-18

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


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 75.42  E-value: 5.68e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAELFTPSPNETT 71
Cdd:COG1396    6 KALGERLRELRKARGLTQEELAERLGVSRSTISRIERGR-RNPSLETLLKLAKALGVSLDELLGGADEELP 75
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
138-219 6.11e-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: 70.37  E-value: 6.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 138 VINVRGDSMADTIEPGDLIFVDISINEFDGDGIYVFGFDD-KIYVKRLQMIP--DKILVISDNPKYREWSVDKSNEDRfy 214
Cdd:cd06462    2 ALRVEGDSMEPTIPDGDLVLVDKSSYEPKRGDIVVFRLPGgELTVKRVIGLPgeGHYFLLGDNPNSPDSRIDGPPELD-- 79

                 ....*
gi 695661951 215 VFGKV 219
Cdd:cd06462   80 IVGVV 84
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-67 5.02e-14

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


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 64.48  E-value: 5.02e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKsFTEQSLSKYATALGVSVAELFTPSP 67
Cdd:COG1476    3 KKLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYN-PSLELALKIARALGVSLEELFSLEE 68
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
6-62 2.70e-13

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 62.54  E-value: 2.70e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 695661951     6 RIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKsFTEQSLSKYATALGVSVAEL 62
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVSLDEL 56
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
4-62 3.70e-13

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: 62.19  E-value: 3.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695661951   4 GNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAEL 62
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGK-RNPSLETLEKLAKALGVSLDEL 58
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
6-67 5.81e-12

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: 59.09  E-value: 5.81e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695661951    6 RIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKSFTEQSLSKYATALGVSVAELFTPSP 67
Cdd:pfam13443   1 KLRKLMADRGISKSDLARATGISRATLSRLRKGKPKRVSLDTLDKICDALGCQPGDLLEYVP 62
YozG COG3655
DNA-binding transcriptional regulator, XRE family [Transcription];
3-70 7.95e-12

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


Pssm-ID: 442872 [Multi-domain]  Cd Length: 69  Bit Score: 58.62  E-value: 7.95e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695661951   3 IGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKSFTEQSLSKYATALGVSVAELFTPSPNET 70
Cdd:COG3655    2 IYVKLDELLAERGMTKKELAEATGISRATLSRLKNGKAKAVRLDTLEKICKALDCQPGDLLEYVPDEE 69
HTH_31 pfam13560
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
3-62 1.14e-10

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: 55.61  E-value: 1.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951    3 IGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKSFTEQSLSKYATALGVSVAEL 62
Cdd:pfam13560   2 LGARLRRLRERAGLSQEALARRLGVSRSTLSRLETGRRGRPSPAVVERLARALGVDGAER 61
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
2-61 1.55e-10

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: 55.33  E-value: 1.55e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951   2 NIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKsFTEQSLSKYATALGVSVAE 61
Cdd:COG1813   12 DYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEAT-PSLDTLRKLEKALGISLAE 70
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
7-62 1.31e-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: 52.54  E-value: 1.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 695661951    7 IRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAEL 62
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGK-REPSLETLKKLAEALGVSLDEL 55
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
141-219 7.42e-09

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 7.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 141 VRGDSMAD-TIEPGDLIFVDISINEFDGDgIYVFGFDDKIYVKRLQMIPDKILVISDNPKYREWSVDksnEDRFYVFGKV 219
Cdd:COG1974  117 VKGDSMIDaGILDGDLVIVDRQLEAENGD-IVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIIIE---GDDVEILGVV 192
RodZ COG1426
Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell ...
1-63 6.12e-08

Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441035 [Multi-domain]  Cd Length: 71  Bit Score: 48.26  E-value: 6.12e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKS-----FTEQSLSKYATALGVSVAELF 63
Cdd:COG1426    4 ETIGELLRQAREAKGLSLEDVAERTKISVSYLEAIEEGDFDAlpgpvYVRGFLRSYARALGLDPEELL 71
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
133-219 1.27e-07

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 49.41  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 133 PDTVKVINVRGDSMADT-IEPGDLIFVDISINEFDGDgIYVFGFDDKIYVKRLQMIPdKILVISDNPKYREWSVdkSNED 211
Cdd:PRK10276  48 PSATYFVKASGDSMIDAgISDGDLLIVDSAITASHGD-IVIAAVDGEFTVKKLQLRP-TVQLIPMNSAYSPITI--SSED 123

                 ....*...
gi 695661951 212 RFYVFGKV 219
Cdd:PRK10276 124 TLDVFGVV 131
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
4-64 1.38e-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: 44.59  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695661951    4 GNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAELFT 64
Cdd:pfam12844   1 GERLRKAREERGLTQEELAERLGISRSQLSAIENGK-SVPPAETLYKIAELLGVPANWLLQ 60
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
1-62 8.66e-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: 40.39  E-value: 8.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695661951   1 MNIGNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKqKSFTEQSLSKYATALGVSVAEL 62
Cdd:COG3620   16 DTLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGK-RDPTVSTLEKIAEALGKELSAV 76
HTH_37 pfam13744
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain.
6-56 1.20e-04

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain.


Pssm-ID: 433449 [Multi-domain]  Cd Length: 80  Bit Score: 39.52  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 695661951    6 RIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQKSFTEQSLSKYATALG 56
Cdd:pfam13744  22 AIARLIEGRGLSQQEAAALLGIAQPKVSALLKGKLSRFSLDKLLDFLTALG 72
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
141-218 1.43e-04

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 39.49  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951 141 VRGDSMADTIEPGDLIFVD---ISINEFD-GDgIYVF---GFDDKIYVKRLqmIpdKILVISDNpkyREWSVDksneDRF 213
Cdd:cd06530    5 VPGGSMEPTLQPGDLVLVNklsYGFREPKrGD-VVVFkspGDPGKPIIKRV--I--GYFVLGDN---RNNSLD----SRY 72

                 ....*
gi 695661951 214 YVFGK 218
Cdd:cd06530   73 WGPVP 77
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
102-220 2.20e-03

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: 37.77  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695661951  102 MGHIQGSDVVDVIRSIEYNNERAAALFGgrTPDTVKVINVRGDSMADT-IEPGDLIFVDiSINEFDGDGIYVFGFDDKIY 180
Cdd:TIGR00498  79 IGRVAAGEPILAEQHIEEYFPIDFSLLK--KPSAVFLLKVMGDSMVDAgICDGDLLIVR-SQKDARNGEIVAAMIDGEVT 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 695661951  181 VKRLQMIPDKILVISDNPKYREWSVDKSNedrFYVFGKVM 220
Cdd:TIGR00498 156 VKRFYKDGTKVELKPENPEFDPIVLNAED---VTILGKVV 192
YiaG COG2944
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];
4-41 6.50e-03

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


Pssm-ID: 442187 [Multi-domain]  Cd Length: 64  Bit Score: 34.14  E-value: 6.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 695661951   4 GNRIRELRLEKGMKISDLAEAVGIDGANVSRVETGKQK 41
Cdd:COG2944    8 PEEIRALRERLGLSQAEFAALLGVSVSTVRRWEQGRRK 45
 
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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