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MULTISPECIES: transcriptional repressor LexA [Oligella]

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

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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, ...
 4-217 5.18e-81

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 240.20  E-value: 5.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSaNAAEDHLKALAKKGAIILTPGTSRGIRLNPDleattpatasa 83
Cdd:COG1974    3 KLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPA----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  84 aaaelSERLTTLPLIGRVAAGNPILAQAHIEKEIPVDPAMFE-DKADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQ 162
Cdd:COG1974   71 -----SPEVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGD 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738649528 163 IVVARINDDVTVKRFQKGANRITLIAENQHFAPIIVtPQDEFAIEGLAVGLIRSL 217
Cdd:COG1974  146 IVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIII-EGDDVEILGVVVGVIRRL 199
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 4-217 5.18e-81

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 240.20  E-value: 5.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSaNAAEDHLKALAKKGAIILTPGTSRGIRLNPDleattpatasa 83
Cdd:COG1974    3 KLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPA----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  84 aaaelSERLTTLPLIGRVAAGNPILAQAHIEKEIPVDPAMFE-DKADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQ 162
Cdd:COG1974   71 -----SPEVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGD 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738649528 163 IVVARINDDVTVKRFQKGANRITLIAENQHFAPIIVtPQDEFAIEGLAVGLIRSL 217
Cdd:COG1974  146 IVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIII-EGDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 4-217 5.07e-75

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: 224.98  E-value: 5.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528    4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSANAAEDHLKALAKKGAIILTPGTSRGIRLnpdleattpatasa 83
Cdd:TIGR00498   3 PLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRI-------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   84 aaaeLSERLTTLPLIGRVAAGNPILAQAHIEKEIPVDPAMF-EDKADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQ 162
Cdd:TIGR00498  69 ----LDDEPKGVPLIGRVAAGEPILAEQHIEEYFPIDFSLLkKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGE 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 738649528  163 IVVARINDDVTVKRFQKGANRITLIAENQHFAPIIVTPQDeFAIEGLAVGLIRSL 217
Cdd:TIGR00498 145 IVAAMIDGEVTVKRFYKDGTKVELKPENPEFDPIVLNAED-VTILGKVVGVIRNF 198
Peptidase_S24 pfam00717
Peptidase S24-like;
96-211 1.63e-41

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 136.95  E-value: 1.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   96 PLIGRVAAGNPILAQAHIEKEIPVDPAMF-EDKADYLLRVRGESMIDiGIYDGDLLAVKKSQSAHNGQIVVARINDDVTV 174
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLsPPGNLFALRVKGDSMEP-GIPDGDLVLVDPSREARNGDIVVARLDGEATV 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 738649528  175 KRFQKGANRITLIAENQHFAPIIVTPQDEFAIEGLAV 211
Cdd:pfam00717  80 KRLYRDGGGIRLISLNPEYPPIELPAEDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 130-202 3.19e-22

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: 86.07  E-value: 3.19e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649528 130 YLLRVRGESMIDIgIYDGDLLAVKKSQSAHNGQIVVARINDDVTVKRFQK-GANRITLIAENQHFAPIIVTPQD 202
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRrGGGRLRLISDNPAYPPIEIDEEE 73
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
87-216 2.42e-20

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 83.31  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  87 ELSErLTTLPLIGR-VAAGNPILAQAHIEKEIPVDPAMFED-KADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQIV 164
Cdd:PRK10276   8 ELRE-IVTFPLFSDlVQCGFPSPAADYVEQRIDLNELLIQHpSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIV 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738649528 165 VARINDDVTVKRFQKGAnRITLIAENQHFAPIIVTPQDEFAIEGLAVGLIRS 216
Cdd:PRK10276  87 IAAVDGEFTVKKLQLRP-TVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKA 137
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 4-217 5.18e-81

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 240.20  E-value: 5.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSaNAAEDHLKALAKKGAIILTPGTSRGIRLNPDleattpatasa 83
Cdd:COG1974    3 KLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSS-SAVHRHLKALEKKGYLRRDPGKSRAIELLPA----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  84 aaaelSERLTTLPLIGRVAAGNPILAQAHIEKEIPVDPAMFE-DKADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQ 162
Cdd:COG1974   71 -----SPEVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKnPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGD 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738649528 163 IVVARINDDVTVKRFQKGANRITLIAENQHFAPIIVtPQDEFAIEGLAVGLIRSL 217
Cdd:COG1974  146 IVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIII-EGDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 4-217 5.07e-75

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: 224.98  E-value: 5.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528    4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSANAAEDHLKALAKKGAIILTPGTSRGIRLnpdleattpatasa 83
Cdd:TIGR00498   3 PLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRI-------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   84 aaaeLSERLTTLPLIGRVAAGNPILAQAHIEKEIPVDPAMF-EDKADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQ 162
Cdd:TIGR00498  69 ----LDDEPKGVPLIGRVAAGEPILAEQHIEEYFPIDFSLLkKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGE 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 738649528  163 IVVARINDDVTVKRFQKGANRITLIAENQHFAPIIVTPQDeFAIEGLAVGLIRSL 217
Cdd:TIGR00498 145 IVAAMIDGEVTVKRFYKDGTKVELKPENPEFDPIVLNAED-VTILGKVVGVIRNF 198
Peptidase_S24 pfam00717
Peptidase S24-like;
96-211 1.63e-41

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 136.95  E-value: 1.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528   96 PLIGRVAAGNPILAQAHIEKEIPVDPAMF-EDKADYLLRVRGESMIDiGIYDGDLLAVKKSQSAHNGQIVVARINDDVTV 174
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLsPPGNLFALRVKGDSMEP-GIPDGDLVLVDPSREARNGDIVVARLDGEATV 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 738649528  175 KRFQKGANRITLIAENQHFAPIIVTPQDEFAIEGLAV 211
Cdd:pfam00717  80 KRLYRDGGGIRLISLNPEYPPIELPAEDDVEIIGRVV 116
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 4-66 3.93e-26

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: 95.91  E-value: 3.93e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738649528    4 KLTARQQEVFDLIQASIRRTGFPPTRAEIAQSLGFRSANAAEDHLKALAKKGAIILTPGTSRG 66
Cdd:pfam01726   1 PLTERQREVLDFIKASIEETGYPPSRREIARALGLRSPNAAEEHLKALERKGYIERDPGKPRA 63
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 130-202 3.19e-22

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: 86.07  E-value: 3.19e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738649528 130 YLLRVRGESMIDIgIYDGDLLAVKKSQSAHNGQIVVARINDDVTVKRFQK-GANRITLIAENQHFAPIIVTPQD 202
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRrGGGRLRLISDNPAYPPIEIDEEE 73
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
87-216 2.42e-20

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 83.31  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  87 ELSErLTTLPLIGR-VAAGNPILAQAHIEKEIPVDPAMFED-KADYLLRVRGESMIDIGIYDGDLLAVKKSQSAHNGQIV 164
Cdd:PRK10276   8 ELRE-IVTFPLFSDlVQCGFPSPAADYVEQRIDLNELLIQHpSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIV 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738649528 165 VARINDDVTVKRFQKGAnRITLIAENQHFAPIIVTPQDEFAIEGLAVGLIRS 216
Cdd:PRK10276  87 IAAVDGEFTVKKLQLRP-TVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKA 137
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 95-212 1.96e-16

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 72.30  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528  95 LPLI-GRVAAGNPILA-QAHIEKEIPVDPamFEDKADYLLRVRGESMIDIgIYDGDLLAVKKSQSA-HNGQIVVARINDD 171
Cdd:COG2932    1 VPLYdGEASAGGGAFNeVEEPVDKLEFPG--LPPDNLFAVRVSGDSMEPT-IRDGDIVLVDPSDTEiRDGGIYVVRTDGE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 738649528 172 VTVKRFQK-GANRITLIAENQHFAPIIVTPQD--EFAIEGLAVG 212
Cdd:COG2932   78 LLVKRLQRrPDGKLRLISDNPAYPPIEIPPEDadEIEIIGRVVW 121
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 130-208 2.08e-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: 68.44  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738649528 130 YLLRVRGESMIDiGIYDGDLLAVKKSQ-SAHNGQIVVARINDD-VTVKRFQK--GANRITLIAENQHFAPIIVTPQDEFA 205
Cdd:cd06462    1 FALRVEGDSMEP-TIPDGDLVLVDKSSyEPKRGDIVVFRLPGGeLTVKRVIGlpGEGHYFLLGDNPNSPDSRIDGPPELD 79


                 ...
gi 738649528 206 IEG 208
Cdd:cd06462   80 IVG 82
 
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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