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Conserved domains on  [gi|124376394|gb|AAI32366|]
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Growth factor independent 1B [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11815272)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Homo sapiens zinc finger protein Gfi-1b that is necessary for development and differentiation of erythroid and megakaryocytic lineages

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
262-287 8.57e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 8.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 124376394  262 DMKKHTYIHTGEKPHKCQVCGKAFSQ 287
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
230-307 1.42e-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: 40.06  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376394 230 KRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQV--CGKAFSQSSNLITHSRKHTGFKPFSCE 307
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS 95
PHA00733 super family cl26169
hypothetical protein
191-239 4.76e-03

hypothetical protein


The actual alignment was detected with superfamily member PHA00733:

Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 4.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 124376394 191 PFACDVCGKTFGHAVSLEQHthVHSQERSFECRMCGKAFKRSSTLSTHL 239
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
262-287 8.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 8.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 124376394  262 DMKKHTYIHTGEKPHKCQVCGKAFSQ 287
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-307 1.42e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376394 230 KRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQV--CGKAFSQSSNLITHSRKHTGFKPFSCE 307
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS 95
PHA00733 PHA00733
hypothetical protein
191-239 4.76e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 4.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 124376394 191 PFACDVCGKTFGHAVSLEQHthVHSQERSFECRMCGKAFKRSSTLSTHL 239
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
220-242 9.78e-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: 9.78e-03
                          10        20
                  ....*....|....*....|...
gi 124376394  220 FECRMCGKAFKRSSTLSTHLLIH 242
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
262-287 8.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 8.57e-05
                          10        20
                  ....*....|....*....|....*.
gi 124376394  262 DMKKHTYIHTGEKPHKCQVCGKAFSQ 287
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-307 1.42e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376394 230 KRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQV--CGKAFSQSSNLITHSRKHTGFKPFSCE 307
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS 95
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
276-298 2.06e-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: 2.06e-03
                          10        20
                  ....*....|....*....|...
gi 124376394  276 HKCQVCGKAFSQSSNLITHSRKH 298
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
168-299 3.70e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376394 168 CNKVFSTP---HGLEVHVRRSHS-----GTRPFACDVCGktfghavsleqhthvhsqersfecrmCGKAFKRSSTLSTHL 239
Cdd:COG5189  318 CTNSSSNGklaHGGERNIDTPSRmlkvkDGKPYKCPVEG--------------------------CNKKYKNQNGLKYHM 371
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376394 240 LiHSDtrpypcqfCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHsRKHT 299
Cdd:COG5189  372 L-HGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
PHA00733 PHA00733
hypothetical protein
191-239 4.76e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 4.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 124376394 191 PFACDVCGKTFGHAVSLEQHthVHSQERSFECRMCGKAFKRSSTLSTHL 239
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
220-242 9.78e-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: 9.78e-03
                          10        20
                  ....*....|....*....|...
gi 124376394  220 FECRMCGKAFKRSSTLSTHLLIH 242
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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