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Conserved domains on  [gi|665404741|ref|NP_001285708|]
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uncharacterized protein Dmel_CG4496, isoform C [Drosophila melanogaster]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10443094)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
SCOP:  4003583

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
259-282 1.65e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.65e-05
                          10        20
                  ....*....|....*....|....
gi 665404741  259 NLRRHMMIHTGERPFPCDLCERRF 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
245-267 1.24e-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: 36.51  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  245 YECPDCGKKVQSNYNLRRHMMIH 267
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 1.39e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|..
gi 665404741  445 NLKRHYMIHTGEKPFSCSKCRK 466
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGK 22
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
208-298 2.84e-03

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404741 208 SDQEDEQKTDNVIKRKSSGSRRLVKRRPGANR--RGRHMYECP--DCGKKVQSNYNLRRHMM------------------ 265
Cdd:COG5189  311 IDVRKLPCTNSSSNGKLAHGGERNIDTPSRMLkvKDGKPYKCPveGCNKKYKNQNGLKYHMLhghqnqklhenpspekmn 390
                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404741 266 -IHTGERPFPCDLCERRFREFSDLKKHrRRHSHD 298
Cdd:COG5189  391 iFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHSHD 423
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
431-453 4.45e-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: 34.97  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  431 YPCPLCHRPFGTRHNLKRHYMIH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
259-282 1.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.65e-05
                          10        20
                  ....*....|....*....|....
gi 665404741  259 NLRRHMMIHTGERPFPCDLCERRF 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
245-267 1.24e-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: 36.51  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  245 YECPDCGKKVQSNYNLRRHMMIH 267
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 1.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|..
gi 665404741  445 NLKRHYMIHTGEKPFSCSKCRK 466
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGK 22
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
208-298 2.84e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404741 208 SDQEDEQKTDNVIKRKSSGSRRLVKRRPGANR--RGRHMYECP--DCGKKVQSNYNLRRHMM------------------ 265
Cdd:COG5189  311 IDVRKLPCTNSSSNGKLAHGGERNIDTPSRMLkvKDGKPYKCPveGCNKKYKNQNGLKYHMLhghqnqklhenpspekmn 390
                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404741 266 -IHTGERPFPCDLCERRFREFSDLKKHrRRHSHD 298
Cdd:COG5189  391 iFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHSHD 423
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
431-453 4.45e-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: 34.97  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  431 YPCPLCHRPFGTRHNLKRHYMIH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
424-478 9.23e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 9.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665404741 424 MSRTRRSYPCPLCHRPFGTRHNLKRHymIHTGEKPFSCSKCRKPFRECSTLKKHM 478
Cdd:PHA00733  67 TSKAVSPYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
259-282 1.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.65e-05
                          10        20
                  ....*....|....*....|....
gi 665404741  259 NLRRHMMIHTGERPFPCDLCERRF 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
245-267 1.24e-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: 36.51  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  245 YECPDCGKKVQSNYNLRRHMMIH 267
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 1.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|..
gi 665404741  445 NLKRHYMIHTGEKPFSCSKCRK 466
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGK 22
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
208-298 2.84e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404741 208 SDQEDEQKTDNVIKRKSSGSRRLVKRRPGANR--RGRHMYECP--DCGKKVQSNYNLRRHMM------------------ 265
Cdd:COG5189  311 IDVRKLPCTNSSSNGKLAHGGERNIDTPSRMLkvKDGKPYKCPveGCNKKYKNQNGLKYHMLhghqnqklhenpspekmn 390
                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404741 266 -IHTGERPFPCDLCERRFREFSDLKKHrRRHSHD 298
Cdd:COG5189  391 iFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHSHD 423
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
431-453 4.45e-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: 34.97  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|...
gi 665404741  431 YPCPLCHRPFGTRHNLKRHYMIH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
424-478 9.23e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 9.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665404741 424 MSRTRRSYPCPLCHRPFGTRHNLKRHymIHTGEKPFSCSKCRKPFRECSTLKKHM 478
Cdd:PHA00733  67 TSKAVSPYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
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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