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Conserved domains on  [gi|929077093|ref|XP_014048880|]
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zinc finger protein Gfi-1b isoform X1 [Salmo salar]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 208-290 5.17e-04

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: 41.63  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929077093 208 ERSYSCKV--CGKVFKRSSTLSTHLLiHSdtrpypcqYCGKRFHQKSDMKKHTFIHTGEKPHVCQVCGKAFSQSSNLITH 285
Cdd:COG5189  347 GKPYKCPVegCNKKYKNQNGLKYHML-HG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417


                 ....*
gi 929077093 286 sRKHS 290
Cdd:COG5189  418 -RKHS 421
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 208-290 5.17e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929077093 208 ERSYSCKV--CGKVFKRSSTLSTHLLiHSdtrpypcqYCGKRFHQKSDMKKHTFIHTGEKPHVCQVCGKAFSQSSNLITH 285
Cdd:COG5189  347 GKPYKCPVegCNKKYKNQNGLKYHML-HG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417


                 ....*
gi 929077093 286 sRKHS 290
Cdd:COG5189  418 -RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
253-278 1.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*.
gi 929077093  253 DMKKHTFIHTGEKPHVCQVCGKAFSQ 278
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 208-290 5.17e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929077093 208 ERSYSCKV--CGKVFKRSSTLSTHLLiHSdtrpypcqYCGKRFHQKSDMKKHTFIHTGEKPHVCQVCGKAFSQSSNLITH 285
Cdd:COG5189  347 GKPYKCPVegCNKKYKNQNGLKYHML-HG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417


                 ....*
gi 929077093 286 sRKHS 290
Cdd:COG5189  418 -RKHS 421
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
185-316 8.61e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929077093 185 TSAKAPEHPYELKQTLGMYGRPKERSYSckVCGKVFKRSSTLSTHLLIHSDTRPYPCQY--CGKRFHQKSDMKKHTFIH- 261
Cdd:COG5048  300 SRSSPLTRHLRSVNHSGESLKPFSCPYS--LCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQq 377

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929077093 262 ----TGEKPHVCQV--CGKAFSQSSNLITHSRKHSSYWP--FSCTHCQSSFQRRLDLQRHQET 316
Cdd:COG5048  378 ykdlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKI 440
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
221-291 1.08e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929077093 221 KRSSTLSTHLLIHSDTRPYPCQYCGKRFHQKSDMKKHTFIHTGEKPHVCQV--CGKAFSQSSNLITHSRKHSS 291
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
253-278 1.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*.
gi 929077093  253 DMKKHTFIHTGEKPHVCQVCGKAFSQ 278
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 211-233 5.60e-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: 33.81  E-value: 5.60e-03
                          10        20
                  ....*....|....*....|...
gi 929077093  211 YSCKVCGKVFKRSSTLSTHLLIH 233
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 267-289 9.23e-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: 33.04  E-value: 9.23e-03
                          10        20
                  ....*....|....*....|...
gi 929077093  267 HVCQVCGKAFSQSSNLITHSRKH 289
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 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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