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Conserved domains on  [gi|2430216817|gb|WBY54302|]
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cucoid [Chironomus riparius]

Protein Classification

C2H2-type zinc finger protein; C2H2-type zinc finger protein; zf-AD domain-containing protein; zinc-finger associated domain-containing protein; C2H2-type zinc finger protein; zf-AD domain-containing protein; zinc-finger associated domain-containing protein; C2H2-type zinc finger protein; zinc-finger associated domain-containing protein( domain architecture ID 12083238)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Homo sapiens DNA-binding protein Ikaros, a transcription regulator of hematopoietic cell differentiation; Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Homo sapiens DNA-binding protein Ikaros, a transcription regulator of hematopoietic cell differentiation; zf-AD domain-containing protein; zinc-finger associated domain (ZAD)-containing protein similar to Drosophila melanogaster CG2712 protein; Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Homo sapiens DNA-binding protein Ikaros, a transcription regulator of hematopoietic cell differentiation; zf-AD domain-containing protein; zinc-finger associated domain (ZAD)-containing protein similar to Drosophila melanogaster CG2712 protein; Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Homo sapiens DNA-binding protein Ikaros, a transcription regulator of hematopoietic cell differentiation; zinc-finger associated domain (ZAD)-containing protein similar to Drosophila melanogaster CG2712 protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 21-96 7.97e-11

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 462262  Cd Length: 75  Bit Score: 57.08  E-value: 7.97e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2430216817  21 VCRICLQD-GDLMSVYDKSiDSEFSYAEKIVQVVNsINLKKKGNLPQQICASCINDLESAYRFKMNCESTEAILQTY 96
Cdd:pfam07776   1 VCRLCLDEsDELIPIFDPS-DSEKTLAEILEDCTG-IELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 70-276 1.01e-07

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: 52.80  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817  70 ASCINDLESAYRFKMNCEST---EAILQTYITPNSEGSEEIDEQELPVDD-FYTYKSEIIDTEIVVPDNNDHLDKDL--- 142
Cdd:COG5189   194 STSHNSNMGSKNAKMNDSSKlkkLSLIEEKKFPERVRSRYIDIGHMMDTHqFYLEDVDLMDDDILGPSNEEMLYKYIsps 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 143 --------DDVLG-------KSEDNEEIISDLIDDIKPPTKAKKESTREKSTRSKRNNQSTIDKE-------QERIHICE 200
Cdd:COG5189   274 qgsaelfeESSLGfdyefihKSVGNKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNIDTPsrmlkvkDGKPYKCP 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 201 I--CANQYKYRHALEVHMRR-HNNIKPYECP--ECKRSFVIRfelkrhmrvhtgAKPYSCRFCERKFSDFGSrIKHERSH 275
Cdd:COG5189   354 VegCNKKYKNQNGLKYHMLHgHQNQKLHENPspEKMNIFSAK------------DKPYRCEVCDKRYKNLNG-LKYHRKH 420


                  .
gi 2430216817 276 T 276
Cdd:COG5189   421 S 421
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 21-96 7.97e-11

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 57.08  E-value: 7.97e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2430216817  21 VCRICLQD-GDLMSVYDKSiDSEFSYAEKIVQVVNsINLKKKGNLPQQICASCINDLESAYRFKMNCESTEAILQTY 96
Cdd:pfam07776   1 VCRLCLDEsDELIPIFDPS-DSEKTLAEILEDCTG-IELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 21-95 1.38e-09

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 53.67  E-value: 1.38e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2430216817   21 VCRICLQDGDLMSVYDkSIDSEFSYAEKIVQVVnSINLKKKGNLPQQICASCINDLESAYRFKMNCESTEAILQT 95
Cdd:smart00868   1 VCRLCLSESENLVSIF-DESSEASLAEKIEECT-GIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 70-276 1.01e-07

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 52.80  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817  70 ASCINDLESAYRFKMNCEST---EAILQTYITPNSEGSEEIDEQELPVDD-FYTYKSEIIDTEIVVPDNNDHLDKDL--- 142
Cdd:COG5189   194 STSHNSNMGSKNAKMNDSSKlkkLSLIEEKKFPERVRSRYIDIGHMMDTHqFYLEDVDLMDDDILGPSNEEMLYKYIsps 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 143 --------DDVLG-------KSEDNEEIISDLIDDIKPPTKAKKESTREKSTRSKRNNQSTIDKE-------QERIHICE 200
Cdd:COG5189   274 qgsaelfeESSLGfdyefihKSVGNKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNIDTPsrmlkvkDGKPYKCP 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 201 I--CANQYKYRHALEVHMRR-HNNIKPYECP--ECKRSFVIRfelkrhmrvhtgAKPYSCRFCERKFSDFGSrIKHERSH 275
Cdd:COG5189   354 VegCNKKYKNQNGLKYHMLHgHQNQKLHENPspEKMNIFSAK------------DKPYRCEVCDKRYKNLNG-LKYHRKH 420


                  .
gi 2430216817 276 T 276
Cdd:COG5189   421 S 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-263 3.04e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 3.04e-05
                          10        20
                  ....*....|....*....|....*
gi 2430216817 239 ELKRHMRVHTGAKPYSCRFCERKFS 263
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 21-96 7.97e-11

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 57.08  E-value: 7.97e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2430216817  21 VCRICLQD-GDLMSVYDKSiDSEFSYAEKIVQVVNsINLKKKGNLPQQICASCINDLESAYRFKMNCESTEAILQTY 96
Cdd:pfam07776   1 VCRLCLDEsDELIPIFDPS-DSEKTLAEILEDCTG-IELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 21-95 1.38e-09

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 53.67  E-value: 1.38e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2430216817   21 VCRICLQDGDLMSVYDkSIDSEFSYAEKIVQVVnSINLKKKGNLPQQICASCINDLESAYRFKMNCESTEAILQT 95
Cdd:smart00868   1 VCRLCLSESENLVSIF-DESSEASLAEKIEECT-GIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 70-276 1.01e-07

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 52.80  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817  70 ASCINDLESAYRFKMNCEST---EAILQTYITPNSEGSEEIDEQELPVDD-FYTYKSEIIDTEIVVPDNNDHLDKDL--- 142
Cdd:COG5189   194 STSHNSNMGSKNAKMNDSSKlkkLSLIEEKKFPERVRSRYIDIGHMMDTHqFYLEDVDLMDDDILGPSNEEMLYKYIsps 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 143 --------DDVLG-------KSEDNEEIISDLIDDIKPPTKAKKESTREKSTRSKRNNQSTIDKE-------QERIHICE 200
Cdd:COG5189   274 qgsaelfeESSLGfdyefihKSVGNKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNIDTPsrmlkvkDGKPYKCP 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2430216817 201 I--CANQYKYRHALEVHMRR-HNNIKPYECP--ECKRSFVIRfelkrhmrvhtgAKPYSCRFCERKFSDFGSrIKHERSH 275
Cdd:COG5189   354 VegCNKKYKNQNGLKYHMLHgHQNQKLHENPspEKMNIFSAK------------DKPYRCEVCDKRYKNLNG-LKYHRKH 420


                  .
gi 2430216817 276 T 276
Cdd:COG5189   421 S 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-263 3.04e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 3.04e-05
                          10        20
                  ....*....|....*....|....*
gi 2430216817 239 ELKRHMRVHTGAKPYSCRFCERKFS 263
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-235 1.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.81e-04
                          10        20
                  ....*....|....*....|....*
gi 2430216817 211 ALEVHMRRHNNIKPYECPECKRSFV 235
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 225-247 6.61e-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: 36.51  E-value: 6.61e-04
                          10        20
                  ....*....|....*....|...
gi 2430216817 225 YECPECKRSFVIRFELKRHMRVH 247
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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