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Conserved domains on  [gi|221378820|ref|NP_650092|]
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uncharacterized protein Dmel_CG14710 [Drosophila melanogaster]

Protein Classification

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 ...
 9-84 2.30e-14

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: 67.87  E-value: 2.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221378820    9 QCRICLgdFEESQMICLFGDKGES-DLRKKLELCCRIRVRQSPQLPEKACNSCCEFVQMWFNFRQMCLNSQVYWETS 84
Cdd:pfam07776   1 VCRLCL--DESDELIPIFDPSDSEkTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
261-395 4.71e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378820 261 KFMCILCGNVFYKKSVFTAHM----MTHSEYKPHQC--EICNKSFRQMGELRAHIRRHTGDRPYKCMYCDRHFYDRS--- 331
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLrsvnHSGESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221378820 332 ----ERVRHERVHTNTRPYAC--QECGKTFTHTAILKNHILSHSAQ--KNYNCGICCKSFTLLHQLKAHLQT 395
Cdd:COG5048  369 neppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFrpYNCKNPPCSKSFNRHYNLIPHKKI 440
 
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 ...
 9-84 2.30e-14

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: 67.87  E-value: 2.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221378820    9 QCRICLgdFEESQMICLFGDKGES-DLRKKLELCCRIRVRQSPQLPEKACNSCCEFVQMWFNFRQMCLNSQVYWETS 84
Cdd:pfam07776   1 VCRLCL--DESDELIPIFDPSDSEkTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 9-78 2.10e-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: 214871  Cd Length: 73  Bit Score: 59.45  E-value: 2.10e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378820     9 QCRICLGDFEEsqMICLFGDKGESDLRKKLELCCRIRVRQSPQLPEKACNSCCEFVQMWFNFRQMCLNSQ 78
Cdd:smart00868   1 VCRLCLSESEN--LVSIFDESSEASLAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESD 68
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
261-395 4.71e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378820 261 KFMCILCGNVFYKKSVFTAHM----MTHSEYKPHQC--EICNKSFRQMGELRAHIRRHTGDRPYKCMYCDRHFYDRS--- 331
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLrsvnHSGESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221378820 332 ----ERVRHERVHTNTRPYAC--QECGKTFTHTAILKNHILSHSAQ--KNYNCGICCKSFTLLHQLKAHLQT 395
Cdd:COG5048  369 neppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFrpYNCKNPPCSKSFNRHYNLIPHKKI 440
zf-H2C2_2 pfam13465
Zinc-finger double domain;
304-327 3.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.40e-04
                          10        20
                  ....*....|....*....|....
gi 221378820  304 ELRAHIRRHTGDRPYKCMYCDRHF 327
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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 ...
 9-84 2.30e-14

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: 67.87  E-value: 2.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221378820    9 QCRICLgdFEESQMICLFGDKGES-DLRKKLELCCRIRVRQSPQLPEKACNSCCEFVQMWFNFRQMCLNSQVYWETS 84
Cdd:pfam07776   1 VCRLCL--DESDELIPIFDPSDSEkTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 9-78 2.10e-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: 214871  Cd Length: 73  Bit Score: 59.45  E-value: 2.10e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378820     9 QCRICLGDFEEsqMICLFGDKGESDLRKKLELCCRIRVRQSPQLPEKACNSCCEFVQMWFNFRQMCLNSQ 78
Cdd:smart00868   1 VCRLCLSESEN--LVSIFDESSEASLAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESD 68
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
261-395 4.71e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378820 261 KFMCILCGNVFYKKSVFTAHM----MTHSEYKPHQC--EICNKSFRQMGELRAHIRRHTGDRPYKCMYCDRHFYDRS--- 331
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLrsvnHSGESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221378820 332 ----ERVRHERVHTNTRPYAC--QECGKTFTHTAILKNHILSHSAQ--KNYNCGICCKSFTLLHQLKAHLQT 395
Cdd:COG5048  369 neppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFrpYNCKNPPCSKSFNRHYNLIPHKKI 440
zf-H2C2_2 pfam13465
Zinc-finger double domain;
304-327 3.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.40e-04
                          10        20
                  ....*....|....*....|....
gi 221378820  304 ELRAHIRRHTGDRPYKCMYCDRHF 327
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 290-312 8.63e-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: 8.63e-04
                          10        20
                  ....*....|....*....|...
gi 221378820  290 HQCEICNKSFRQMGELRAHIRRH 312
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
335-357 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|...
gi 221378820  335 RHERVHTNTRPYACQECGKTFTH 357
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
 
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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