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Conserved domains on  [gi|1900352444|ref|XP_012725235|]
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zinc finger protein 358 [Fundulus heteroclitus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10604075)

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|30718982
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;
398-423 1.57e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 398 ALEQHQQVHTGERPYTCPHCGKGFAQ 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 ...
 440-462 6.97e-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: 39.59  E-value: 6.97e-05
                          10        20
                  ....*....|....*....|...
gi 1900352444 440 YRCTLCGKSFISSSHLKRHRTVH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-451 9.72e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 426 NLRVHLLVHTGERRYRCTLCGKSFIS 451
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 3.19e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.19e-04
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 454 HLKRHRTVHTQEKPYSCSRCGQSFSQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 1.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 398 ALEQHQQVHTGERPYTCPHCGKGFAQ 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 ...
 440-462 6.97e-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: 39.59  E-value: 6.97e-05
                          10        20
                  ....*....|....*....|...
gi 1900352444 440 YRCTLCGKSFISSSHLKRHRTVH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-451 9.72e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 426 NLRVHLLVHTGERRYRCTLCGKSFIS 451
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 3.19e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.19e-04
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 454 HLKRHRTVHTQEKPYSCSRCGQSFSQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
413-494 4.53e-04

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 41.78  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900352444 413 TCPHCGKgfaqpNNLRVHLLVHTGERRYRCTLCGKSFI--SSSHLKRHRtVHTQEKPYSCSRCGQSFSQMC--------S 482
Cdd:COG3677    18 VCPHCGS-----TRIVKNGKTRNGRQRYRCKDCGRTFTvtTGTIFEGSK-LPLWLQAIRLLLNGISLRQIArvlgvsykT 91

                          90
                  ....*....|..
gi 1900352444 483 VRRHRQQSQCGM 494
Cdd:COG3677    92 VWRWLHRIREAL 103
PHA00733 PHA00733
hypothetical protein
 385-431 2.13e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1900352444 385 VCPVCRLVFPSAAALEQHqqVHTGERPYTCPHCGKGFAQPNNLRVHL 431
Cdd:PHA00733   75 VCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
ZnF_C2H2 smart00355
zinc finger;
440-462 4.38e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 4.38e-03
                           10        20
                   ....*....|....*....|...
gi 1900352444  440 YRCTLCGKSFISSSHLKRHRTVH 462
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 1.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 398 ALEQHQQVHTGERPYTCPHCGKGFAQ 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 ...
 440-462 6.97e-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: 39.59  E-value: 6.97e-05
                          10        20
                  ....*....|....*....|...
gi 1900352444 440 YRCTLCGKSFISSSHLKRHRTVH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-451 9.72e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 426 NLRVHLLVHTGERRYRCTLCGKSFIS 451
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 412-434 2.51e-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: 38.05  E-value: 2.51e-04
                          10        20
                  ....*....|....*....|...
gi 1900352444 412 YTCPHCGKGFAQPNNLRVHLLVH 434
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 3.19e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.19e-04
                          10        20
                  ....*....|....*....|....*.
gi 1900352444 454 HLKRHRTVHTQEKPYSCSRCGQSFSQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
413-494 4.53e-04

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 41.78  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900352444 413 TCPHCGKgfaqpNNLRVHLLVHTGERRYRCTLCGKSFI--SSSHLKRHRtVHTQEKPYSCSRCGQSFSQMC--------S 482
Cdd:COG3677    18 VCPHCGS-----TRIVKNGKTRNGRQRYRCKDCGRTFTvtTGTIFEGSK-LPLWLQAIRLLLNGISLRQIArvlgvsykT 91

                          90
                  ....*....|..
gi 1900352444 483 VRRHRQQSQCGM 494
Cdd:COG3677    92 VWRWLHRIREAL 103
PHA00733 PHA00733
hypothetical protein
 385-431 2.13e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1900352444 385 VCPVCRLVFPSAAALEQHqqVHTGERPYTCPHCGKGFAQPNNLRVHL 431
Cdd:PHA00733   75 VCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
ZnF_C2H2 smart00355
zinc finger;
440-462 4.38e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 4.38e-03
                           10        20
                   ....*....|....*....|...
gi 1900352444  440 YRCTLCGKSFISSSHLKRHRTVH 462
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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