NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1582630785|gb|TBE11259|]
View 

transcriptional repressor LexA [Rhizobium ruizarguesonis]

Protein Classification

LexA family protein( domain architecture ID 11449429)

LexA family protein may function as a transcriptional regulator involved in the repression of one or more genes involved in the response to DNA damage (SOS response), including recA and lexA and/or may contain a S24 peptidase domain such as in the translesion error-prone DNA polymerase V autoproteolytic subunit

Gene Ontology:  GO:0003677|GO:0045892
PubMed:  10679470|10908318

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 2-238 1.76e-75

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 227.10  E-value: 1.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASkSGIHRLITALEERGFIRRLPNRARALEVIKLPEayspsiqprr 81
Cdd:COG1974     4 LTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPASP---------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785  82 gfspsviegslgkpqpvaapaaakpvadngNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLG-SGEHYALEVKGDSM 160
Cdd:COG1974    73 ------------------------------EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSM 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582630785 161 IDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRY 238
Cdd:COG1974   123 IDAGILDGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL 199
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 2-238 1.76e-75

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 227.10  E-value: 1.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASkSGIHRLITALEERGFIRRLPNRARALEVIKLPEayspsiqprr 81
Cdd:COG1974     4 LTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPASP---------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785  82 gfspsviegslgkpqpvaapaaakpvadngNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLG-SGEHYALEVKGDSM 160
Cdd:COG1974    73 ------------------------------EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSM 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582630785 161 IDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRY 238
Cdd:COG1974   123 IDAGILDGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 2-239 1.06e-51

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: 166.43  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAyspsiqprr 81
Cdd:TIGR00498   4 LTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPK--------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785  82 gfspsviegslgkpqpvaapaaakpvadngnsvSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEH-YALEVKGDSM 160
Cdd:TIGR00498  75 ---------------------------------GVPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAvFLLKVMGDSM 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582630785 161 IDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH 239
Cdd:TIGR00498 122 VDAGICDGDLLIVRSQKDARNGEIVAAMIDG-EVTVKRFYKDGTKVELKPENPEFDPIVLNAEDVTILGKVVGVIRNFQ 199
Peptidase_S24 pfam00717
Peptidase S24-like;
117-232 5.83e-35

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 120.77  E-value: 5.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 117 PVMGRIAAGVPISAIQNNTHDIVVPADML-GSGEHYALEVKGDSMIdAGIFDGDTVIIRNGSTASPGDIVVALVDDeEAT 195
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLsPPGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVARLDG-EAT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1582630785 196 LKRFRRKGASIALEAANPAYETRIFGP-DRVKVQGKLV 232
Cdd:pfam00717  79 VKRLYRDGGGIRLISLNPEYPPIELPAeDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 151-232 5.35e-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: 81.07  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 151 YALEVKGDSMIDAgIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGAS-IALEAANPAYETRIFGPDRVKVQG 229
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDG-ELTVKRLQRRGGGrLRLISDNPAYPPIEIDEEELEIVG 78


                  ...
gi 1582630785 230 KLV 232
Cdd:cd06529    79 VVG 81
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
151-221 4.37e-12

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 61.74  E-value: 4.37e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582630785 151 YALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKgASIALEAANPAYETRIFG 221
Cdd:PRK10276   52 YFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDG-EFTVKKLQLR-PTVQLIPMNSAYSPITIS 120
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
2-60 6.59e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.96  E-value: 6.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582630785    2 LTRKQQELLLFIHErmkeSGvPPSFDEMKDALDLaSKSGIHRLITALEERGFIRRLPNR 60
Cdd:smart00347   8 LTPTQFLVLRILYE----EG-PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREPSP 60
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 2-238 1.76e-75

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 227.10  E-value: 1.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASkSGIHRLITALEERGFIRRLPNRARALEVIKLPEayspsiqprr 81
Cdd:COG1974     4 LTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPASP---------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785  82 gfspsviegslgkpqpvaapaaakpvadngNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLG-SGEHYALEVKGDSM 160
Cdd:COG1974    73 ------------------------------EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSM 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582630785 161 IDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRY 238
Cdd:COG1974   123 IDAGILDGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 2-239 1.06e-51

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: 166.43  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAyspsiqprr 81
Cdd:TIGR00498   4 LTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPK--------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785  82 gfspsviegslgkpqpvaapaaakpvadngnsvSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEH-YALEVKGDSM 160
Cdd:TIGR00498  75 ---------------------------------GVPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAvFLLKVMGDSM 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582630785 161 IDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH 239
Cdd:TIGR00498 122 VDAGICDGDLLIVRSQKDARNGEIVAAMIDG-EVTVKRFYKDGTKVELKPENPEFDPIVLNAEDVTILGKVVGVIRNFQ 199
Peptidase_S24 pfam00717
Peptidase S24-like;
117-232 5.83e-35

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 120.77  E-value: 5.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 117 PVMGRIAAGVPISAIQNNTHDIVVPADML-GSGEHYALEVKGDSMIdAGIFDGDTVIIRNGSTASPGDIVVALVDDeEAT 195
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLsPPGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVARLDG-EAT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1582630785 196 LKRFRRKGASIALEAANPAYETRIFGP-DRVKVQGKLV 232
Cdd:pfam00717  79 VKRLYRDGGGIRLISLNPEYPPIELPAeDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 151-232 5.35e-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: 81.07  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 151 YALEVKGDSMIDAgIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKGAS-IALEAANPAYETRIFGPDRVKVQG 229
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDG-ELTVKRLQRRGGGrLRLISDNPAYPPIEIDEEELEIVG 78


                  ...
gi 1582630785 230 KLV 232
Cdd:cd06529    79 VVG 81
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 151-230 2.25e-15

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: 68.83  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 151 YALEVKGDSMIDAgIFDGDTVII-RNGSTASPGDIVVALVDDEEATLKRFRRKGAS--IALEAANPAYET-RIFGPDRVK 226
Cdd:cd06462     1 FALRVEGDSMEPT-IPDGDLVLVdKSSYEPKRGDIVVFRLPGGELTVKRVIGLPGEghYFLLGDNPNSPDsRIDGPPELD 79


                  ....
gi 1582630785 227 VQGK 230
Cdd:cd06462    80 IVGV 83
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 116-233 7.92e-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: 68.45  E-value: 7.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582630785 116 VPVM-GRIAAGVPISAIQNNTHDiVVPADMLGSGEHYALEVKGDSMIDAgIFDGDTVII-RNGSTASPGDIVVaLVDDEE 193
Cdd:COG2932     1 VPLYdGEASAGGGAFNEVEEPVD-KLEFPGLPPDNLFAVRVSGDSMEPT-IRDGDIVLVdPSDTEIRDGGIYV-VRTDGE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1582630785 194 ATLKR-FRRKGASIALEAANPAYETRIFGP---DRVKVQGKLVG 233
Cdd:COG2932    78 LLVKRlQRRPDGKLRLISDNPAYPPIEIPPedaDEIEIIGRVVW 121
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 2-63 7.16e-14

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


Pssm-ID: 396335 [Multi-domain]  Cd Length: 63  Bit Score: 64.33  E-value: 7.16e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582630785   2 LTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARA 63
Cdd:pfam01726   2 LTERQREVLDFIKASIEETGYPPSRREIARALGLRSPNAAEEHLKALERKGYIERDPGKPRA 63
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
151-221 4.37e-12

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 61.74  E-value: 4.37e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582630785 151 YALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDeEATLKRFRRKgASIALEAANPAYETRIFG 221
Cdd:PRK10276   52 YFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDG-EFTVKKLQLR-PTVQLIPMNSAYSPITIS 120
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
2-60 6.59e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.96  E-value: 6.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582630785    2 LTRKQQELLLFIHErmkeSGvPPSFDEMKDALDLaSKSGIHRLITALEERGFIRRLPNR 60
Cdd:smart00347   8 LTPTQFLVLRILYE----EG-PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREPSP 60
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
5-56 1.06e-03

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 39.49  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582630785   5 KQQELLLFIHERmkesgvPPSFDEMKDALDlASKSGIHRLITALEERGFIRR 56
Cdd:COG4742    17 KRKNILLLLAEG------PKTRSELAESLD-VSRSTILRQLKELEERGLIER 61
IclR COG1414
DNA-binding transcriptional regulator, IclR family [Transcription];
19-81 4.06e-03

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


Pssm-ID: 441024 [Multi-domain]  Cd Length: 253  Bit Score: 37.49  E-value: 4.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582630785  19 ESGVPPSFDEMKDALDLaSKSGIHRLITALEERGFIRRLPNRAR---ALEVIKLPEAYSPSIQPRR 81
Cdd:COG1414    20 EAGGGLSLSELARRLGL-PKSTVHRLLATLEEEGYVERDPEGGRyrlGPRLLELGSAALRRLDLRR 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH