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Conserved domains on  [gi|73621290|sp|P07664|]
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RecName: Full=Serendipity locus protein delta; Short=Serendipity-delta

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 1000026)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
205-360 1.63e-03

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 205 SWYQLQKHISEEHSKQPN-HICPICGVIRRDEEYLELHMN--LHEGKTEKQC----RYCPKSFSRPVNTLRHMRMHWDKK 277
Cdd:COG5048 271 QSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFscpySLCGKLFSRNDALKRHILLHTSIS 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 278 KYQCEKCGLRFSQDNLLyNHRLRHEAEENPIIC---------SICNVSFKSRKTFNHHTLIHKENRPRHY-CSVCPKSFT 347
Cdd:COG5048 351 PAKEKLLNSSSKFSPLL-NNEPPQSLQQYKDLKndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCkNPPCSKSFN 429

                       170
                ....*....|...
gi 73621290 348 ERYTLKMHMKTHE 360
Cdd:COG5048 430 RHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-360 1.63e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 205 SWYQLQKHISEEHSKQPN-HICPICGVIRRDEEYLELHMN--LHEGKTEKQC----RYCPKSFSRPVNTLRHMRMHWDKK 277
Cdd:COG5048 271 QSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFscpySLCGKLFSRNDALKRHILLHTSIS 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 278 KYQCEKCGLRFSQDNLLyNHRLRHEAEENPIIC---------SICNVSFKSRKTFNHHTLIHKENRPRHY-CSVCPKSFT 347
Cdd:COG5048 351 PAKEKLLNSSSKFSPLL-NNEPPQSLQQYKDLKndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCkNPPCSKSFN 429

                       170
                ....*....|...
gi 73621290 348 ERYTLKMHMKTHE 360
Cdd:COG5048 430 RHYNLIPHKKIHT 442
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-359 5.47e-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: 34.20  E-value: 5.47e-03
                          10        20
                  ....*....|....*....|...
gi 73621290   337 HYCSVCPKSFTERYTLKMHMKTH 359
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-360 1.63e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 205 SWYQLQKHISEEHSKQPN-HICPICGVIRRDEEYLELHMN--LHEGKTEKQC----RYCPKSFSRPVNTLRHMRMHWDKK 277
Cdd:COG5048 271 QSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFscpySLCGKLFSRNDALKRHILLHTSIS 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621290 278 KYQCEKCGLRFSQDNLLyNHRLRHEAEENPIIC---------SICNVSFKSRKTFNHHTLIHKENRPRHY-CSVCPKSFT 347
Cdd:COG5048 351 PAKEKLLNSSSKFSPLL-NNEPPQSLQQYKDLKndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCkNPPCSKSFN 429

                       170
                ....*....|...
gi 73621290 348 ERYTLKMHMKTHE 360
Cdd:COG5048 430 RHYNLIPHKKIHT 442
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-359 5.47e-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: 34.20  E-value: 5.47e-03
                          10        20
                  ....*....|....*....|...
gi 73621290   337 HYCSVCPKSFTERYTLKMHMKTH 359
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 252-273 9.76e-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: 33.43  E-value: 9.76e-03
                          10        20
                  ....*....|....*....|..
gi 73621290   252 QCRYCPKSFSRPVNTLRHMRMH 273
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 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.
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