NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1953380878|ref|XP_038518597|]
View 

E3 SUMO-protein ligase EGR2 isoform X2 [Canis lupus familiaris]

Protein Classification

DUF3446 and COG5048 domain-containing protein( domain architecture ID 12112558)

protein containing domains DUF3446, zf-C2H2, and COG5048

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DUF3446 pfam11928
Early growth response N-terminal domain; Proteins containing this domain include early growth ...
112-206 2.26e-10

Early growth response N-terminal domain; Proteins containing this domain include early growth response protein 1/2/3 (EGR1/2/3). EGR1 is a transcriptional regulator that binds specifically to 9-bp target sequences containing two CpG sites that can potentially be methylated at four cytosine bases. EGR2, also known as Krox20, is an E3 ligase that sumoylates its Nab coregulators. This domain has a single completely conserved residue P that may be functionally important. Furthermore, it is found associated with pfam00096.


:

Pssm-ID: 463400  Cd Length: 104  Bit Score: 57.54  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 112 GKFSIDPQYP-GASCYPEGIINIVSaGILQGVTSPASTTASSSVTSASPNplATGPLGVCTMSQTQPDLDHLYSPPPPPP 190
Cdd:pfam11928   1 GKFSIDPQYPgGGSLWPEGLISLVS-GLVGMANPPSSSSSSSPSSSSSPN--SSGPLCTMSCSVQSSEMEHIYSAPPPYP 77
                          90
                  ....*....|....*.
gi 1953380878 191 PySGCtGDLYQDPSAF 206
Cdd:pfam11928  78 S-SGC-GDLYQDPSAF 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
382-438 4.47e-07

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953380878 382 KPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSD--ERKRHTKIHLRQK 438
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNP 90
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-378 6.46e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 6.46e-04
                          10        20
                  ....*....|....*....|....*
gi 1953380878 354 YPCPaeGCDRRFSRSDELTRHIRIH 378
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
DUF3446 pfam11928
Early growth response N-terminal domain; Proteins containing this domain include early growth ...
112-206 2.26e-10

Early growth response N-terminal domain; Proteins containing this domain include early growth response protein 1/2/3 (EGR1/2/3). EGR1 is a transcriptional regulator that binds specifically to 9-bp target sequences containing two CpG sites that can potentially be methylated at four cytosine bases. EGR2, also known as Krox20, is an E3 ligase that sumoylates its Nab coregulators. This domain has a single completely conserved residue P that may be functionally important. Furthermore, it is found associated with pfam00096.


Pssm-ID: 463400  Cd Length: 104  Bit Score: 57.54  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 112 GKFSIDPQYP-GASCYPEGIINIVSaGILQGVTSPASTTASSSVTSASPNplATGPLGVCTMSQTQPDLDHLYSPPPPPP 190
Cdd:pfam11928   1 GKFSIDPQYPgGGSLWPEGLISLVS-GLVGMANPPSSSSSSSPSSSSSPN--SSGPLCTMSCSVQSSEMEHIYSAPPPYP 77
                          90
                  ....*....|....*.
gi 1953380878 191 PySGCtGDLYQDPSAF 206
Cdd:pfam11928  78 S-SGC-GDLYQDPSAF 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
382-438 4.47e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953380878 382 KPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSD--ERKRHTKIHLRQK 438
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNP 90
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 2.11e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.11e-06
                          10        20
                  ....*....|....*....|....*.
gi 1953380878 398 HLTTHIRTHTGEKPFACDYCGRKFAR 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-378 6.46e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 6.46e-04
                          10        20
                  ....*....|....*....|....*
gi 1953380878 354 YPCPaeGCDRRFSRSDELTRHIRIH 378
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
383-430 4.95e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 4.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1953380878 383 PFQCRICMRNFSRSDHLTTHIRTHTGEKpfACDYCGRKFARSDERKRH 430
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
DUF3446 pfam11928
Early growth response N-terminal domain; Proteins containing this domain include early growth ...
112-206 2.26e-10

Early growth response N-terminal domain; Proteins containing this domain include early growth response protein 1/2/3 (EGR1/2/3). EGR1 is a transcriptional regulator that binds specifically to 9-bp target sequences containing two CpG sites that can potentially be methylated at four cytosine bases. EGR2, also known as Krox20, is an E3 ligase that sumoylates its Nab coregulators. This domain has a single completely conserved residue P that may be functionally important. Furthermore, it is found associated with pfam00096.


Pssm-ID: 463400  Cd Length: 104  Bit Score: 57.54  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 112 GKFSIDPQYP-GASCYPEGIINIVSaGILQGVTSPASTTASSSVTSASPNplATGPLGVCTMSQTQPDLDHLYSPPPPPP 190
Cdd:pfam11928   1 GKFSIDPQYPgGGSLWPEGLISLVS-GLVGMANPPSSSSSSSPSSSSSPN--SSGPLCTMSCSVQSSEMEHIYSAPPPYP 77
                          90
                  ....*....|....*.
gi 1953380878 191 PySGCtGDLYQDPSAF 206
Cdd:pfam11928  78 S-SGC-GDLYQDPSAF 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
382-438 4.47e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953380878 382 KPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSD--ERKRHTKIHLRQK 438
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNP 90
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 2.11e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.11e-06
                          10        20
                  ....*....|....*....|....*.
gi 1953380878 398 HLTTHIRTHTGEKPFACDYCGRKFAR 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
339-432 2.73e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.63  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 339 KYPNRPSKTpVHERPYPCPAEGCDRRFSRSDELTRHiRIHtGHK-----PFQCRICMRNFSRSDhltthirthtgeKPFA 413
Cdd:COG5189   336 DTPSRMLKV-KDGKPYKCPVEGCNKKYKNQNGLKYH-MLH-GHQnqklhENPSPEKMNIFSAKD------------KPYR 400
                          90
                  ....*....|....*....
gi 1953380878 414 CDYCGRKFARSDERKRHTK 432
Cdd:COG5189   401 CEVCDKRYKNLNGLKYHRK 419
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
350-420 6.75e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 6.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953380878 350 HERPYPCPaeGCDRRFSRSDELTRHIRIHTGHKPFQCRICMR--NFSRSDHLTTHIRTHTGEKPFACDYCGRK 420
Cdd:COG5048    30 APRPDSCP--NCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-395 8.09e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.09e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953380878 370 ELTRHIRIHTGHKPFQCRICMRNFSR 395
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-378 6.46e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 6.46e-04
                          10        20
                  ....*....|....*....|....*
gi 1953380878 354 YPCPaeGCDRRFSRSDELTRHIRIH 378
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-438 1.01e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 354 YPCPAEGCDRRFSRSDELTRHIR--IHTG--HKPFQCRI--CMRNFSRSDHLTTHIRTHTGEKPFACDY--CGRKFARSD 425
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367
                          90
                  ....*....|...
gi 1953380878 426 ERKRHTKIHLRQK 438
Cdd:COG5048   368 NNEPPQSLQQYKD 380
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
384-406 1.92e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 1.92e-03
                          10        20
                  ....*....|....*....|...
gi 1953380878 384 FQCRICMRNFSRSDHLTTHIRTH 406
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
412-434 4.29e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 4.29e-03
                          10        20
                  ....*....|....*....|...
gi 1953380878 412 FACDYCGRKFARSDERKRHTKIH 434
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
383-430 4.95e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 4.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1953380878 383 PFQCRICMRNFSRSDHLTTHIRTHTGEKpfACDYCGRKFARSDERKRH 430
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
356-435 7.32e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 38.85  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953380878 356 CPAEGCDRRFSRSDELTRHIRIHtgHKPFQCRICMRN---------FSRSDHLTTHIRTHTGEKPFA----CDYCGRKFA 422
Cdd:COG5236   154 CPKSKCHRRCGSLKELKKHYKAQ--HGFVLCSECIGNkkdfwneirLFRSSTLRDHKNGGLEEEGFKghplCIFCKIYFY 231
                          90
                  ....*....|....*...
gi 1953380878 423 RSDE-----RKRHTKIHL 435
Cdd:COG5236   232 DDDElrrhcRLRHEACHI 249
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
384-406 7.95e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.77  E-value: 7.95e-03
                          10        20
                  ....*....|....*....|...
gi 1953380878 384 FQCRICMRNFSRSDHLTTHIRTH 406
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
 
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