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Conserved domains on  [gi|42794622|ref|NP_976308|]
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zinc finger protein 784 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11472953)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 252-274 9.46e-05

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: 38.82  E-value: 9.46e-05
                          10        20
                  ....*....|....*....|...
gi 42794622   252 FRCTLCDRTFNNSSNFRKHQRTH 274
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-276 1.26e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794622 194 KPFACRFCAKPFRRSSDMRDHER--VHTGE--RPYHCGI--CGKGFTQSSVLSGHARIHTGERPFRCTL--CDRTFNNSS 265
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90
                ....*....|.
gi 42794622 266 NFRKHQRTHFH 276
Cdd:COG5048 368 NNEPPQSLQQY 378
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 252-274 9.46e-05

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: 38.82  E-value: 9.46e-05
                          10        20
                  ....*....|....*....|...
gi 42794622   252 FRCTLCDRTFNNSSNFRKHQRTH 274
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-276 1.26e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794622 194 KPFACRFCAKPFRRSSDMRDHER--VHTGE--RPYHCGI--CGKGFTQSSVLSGHARIHTGERPFRCTL--CDRTFNNSS 265
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90
                ....*....|.
gi 42794622 266 NFRKHQRTHFH 276
Cdd:COG5048 368 NNEPPQSLQQY 378
zf-H2C2_2 pfam13465
Zinc-finger double domain;
210-235 3.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 3.28e-04
                          10        20
                  ....*....|....*....|....*.
gi 42794622   210 DMRDHERVHTGERPYHCGICGKGFTQ 235
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
252-274 7.98e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 7.98e-03
                           10        20
                   ....*....|....*....|...
gi 42794622    252 FRCTLCDRTFNNSSNFRKHQRTH 274
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 252-274 9.46e-05

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: 38.82  E-value: 9.46e-05
                          10        20
                  ....*....|....*....|...
gi 42794622   252 FRCTLCDRTFNNSSNFRKHQRTH 274
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-276 1.26e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794622 194 KPFACRFCAKPFRRSSDMRDHER--VHTGE--RPYHCGI--CGKGFTQSSVLSGHARIHTGERPFRCTL--CDRTFNNSS 265
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90
                ....*....|.
gi 42794622 266 NFRKHQRTHFH 276
Cdd:COG5048 368 NNEPPQSLQQY 378
zf-H2C2_2 pfam13465
Zinc-finger double domain;
210-235 3.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 3.28e-04
                          10        20
                  ....*....|....*....|....*.
gi 42794622   210 DMRDHERVHTGERPYHCGICGKGFTQ 235
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
242-263 1.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|..
gi 42794622   242 HARIHTGERPFRCTLCDRTFNN 263
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 251-276 1.49e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.61  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*.
gi 42794622   251 PFRCTLCDRTFNNSSNFRKHQRTHFH 276
Cdd:pfam12171   1 QFYCVLCDKYFKSENALQNHLKSKKH 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
222-274 2.97e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 2.97e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794622 222 RPYHCGICGKGFTQSSVLSGHARIHTGERPFRCTL--CDRTFNNSSNFRKHQRTH 274
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
ZnF_C2H2 smart00355
zinc finger;
252-274 7.98e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 7.98e-03
                           10        20
                   ....*....|....*....|...
gi 42794622    252 FRCTLCDRTFNNSSNFRKHQRTH 274
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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