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Conserved domains on  [gi|28572159|ref|NP_650859|]
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uncharacterized protein Dmel_CG4424 [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 ...
10-92 7.74e-15

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: 68.64  E-value: 7.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159    10 LCRTCLQDgEAHMVSIFQTADDRlpggVSLCDKIESLSGIQIRataKEEVLPTRICLRCKAFLTLAHKFRQICQRSNEFL 89
Cdd:pfam07776   1 VCRLCLDE-SDELIPIFDPSDSE----KTLAEILEDCTGIELD---PNDLLPKQICERCLSKLQEFYSFRERCLESQELL 72

                  ...
gi 28572159    90 REY 92
Cdd:pfam07776  73 QEL 75
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
210-345 1.24e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 210 NDERPYECEICHKSFHVNYQLKRHIRQHTGAKPYTCQYCQR--NFADRTSLVKHERTHRNERPYAC-KTCGKKFTYASVL 286
Cdd:COG5048  29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSS 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572159 287 KMHYKTHTGEKPHICQLCNKSFARIHNLVAHLQTQQHINDPRLTAYLSTFKVGITVANA 345
Cdd:COG5048 109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSL 167
 
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 ...
10-92 7.74e-15

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: 68.64  E-value: 7.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159    10 LCRTCLQDgEAHMVSIFQTADDRlpggVSLCDKIESLSGIQIRataKEEVLPTRICLRCKAFLTLAHKFRQICQRSNEFL 89
Cdd:pfam07776   1 VCRLCLDE-SDELIPIFDPSDSE----KTLAEILEDCTGIELD---PNDLLPKQICERCLSKLQEFYSFRERCLESQELL 72

                  ...
gi 28572159    90 REY 92
Cdd:pfam07776  73 QEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
10-91 1.00e-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: 59.84  E-value: 1.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159     10 LCRTCLQDGEaHMVSIFQTADDrlpggVSLCDKIESLSGIQIRataKEEVLPTRICLRCKAFLTLAHKFRQICQRSNEFL 89
Cdd:smart00868   1 VCRLCLSESE-NLVSIFDESSE-----ASLAEKIEECTGIEIE---PDDGLPKVICGDCLEKLESFHKFRERCRESDELL 71

                   ..
gi 28572159     90 RE 91
Cdd:smart00868  72 RE 73
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
210-345 1.24e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 210 NDERPYECEICHKSFHVNYQLKRHIRQHTGAKPYTCQYCQR--NFADRTSLVKHERTHRNERPYAC-KTCGKKFTYASVL 286
Cdd:COG5048  29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSS 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572159 287 KMHYKTHTGEKPHICQLCNKSFARIHNLVAHLQTQQHINDPRLTAYLSTFKVGITVANA 345
Cdd:COG5048 109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSL 167
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
241-289 2.46e-04

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 2.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 28572159 241 KPYtCQYCQRNFADRTSLVKHERTHRnerpYACKTCGKKFTYASVLKMH 289
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
257-282 6.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.24e-04
                          10        20
                  ....*....|....*....|....*.
gi 28572159   257 SLVKHERTHRNERPYACKTCGKKFTY 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
214-261 4.19e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 28572159  214 PYECEICHKSFHVNYQLKRHIRQHTGAKpyTCQYCQRNFADRTSLVKH 261
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
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 ...
10-92 7.74e-15

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: 68.64  E-value: 7.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159    10 LCRTCLQDgEAHMVSIFQTADDRlpggVSLCDKIESLSGIQIRataKEEVLPTRICLRCKAFLTLAHKFRQICQRSNEFL 89
Cdd:pfam07776   1 VCRLCLDE-SDELIPIFDPSDSE----KTLAEILEDCTGIELD---PNDLLPKQICERCLSKLQEFYSFRERCLESQELL 72

                  ...
gi 28572159    90 REY 92
Cdd:pfam07776  73 QEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
10-91 1.00e-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: 59.84  E-value: 1.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159     10 LCRTCLQDGEaHMVSIFQTADDrlpggVSLCDKIESLSGIQIRataKEEVLPTRICLRCKAFLTLAHKFRQICQRSNEFL 89
Cdd:smart00868   1 VCRLCLSESE-NLVSIFDESSE-----ASLAEKIEECTGIEIE---PDDGLPKVICGDCLEKLESFHKFRERCRESDELL 71

                   ..
gi 28572159     90 RE 91
Cdd:smart00868  72 RE 73
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
210-345 1.24e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 210 NDERPYECEICHKSFHVNYQLKRHIRQHTGAKPYTCQYCQR--NFADRTSLVKHERTHRNERPYAC-KTCGKKFTYASVL 286
Cdd:COG5048  29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSS 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572159 287 KMHYKTHTGEKPHICQLCNKSFARIHNLVAHLQTQQHINDPRLTAYLSTFKVGITVANA 345
Cdd:COG5048 109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSL 167
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
182-310 7.81e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 7.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 182 VKGKLHVCAICGNGYPRKSTLDTHMRRHNDE----RPYEC--EICHKSFHVNYQLKRHIRQHTGAKPYTCQY-------- 247
Cdd:COG5048 285 GFSLPIKSKQCNISFSRSSPLTRHLRSVNHSgeslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLlnssskfs 364
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 248 -----------------------------CQRNFADRTSLVKHERTHRNERPYACK--TCGKKFTYASVLKMHYKTHTGE 296
Cdd:COG5048 365 pllnneppqslqqykdlkndkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNH 444
                       170
                ....*....|....
gi 28572159 297 KPHICQLCNKSFAR 310
Cdd:COG5048 445 APLLCSILKSFRRD 458
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
201-294 2.94e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 2.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 201 TLDTHMRRHN--DERPYECEI--CHKSFHVNYQLKRHiRQHTgakpytcqYCQRNFADRTSLVKHERTHRNERPYACKTC 276
Cdd:COG5189 334 NIDTPSRMLKvkDGKPYKCPVegCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVC 404
                        90
                ....*....|....*...
gi 28572159 277 GKKFTYASVLKMHYKTHT 294
Cdd:COG5189 405 DKRYKNLNGLKYHRKHSH 422
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
241-289 2.46e-04

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 2.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 28572159 241 KPYtCQYCQRNFADRTSLVKHERTHRnerpYACKTCGKKFTYASVLKMH 289
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
257-282 6.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.24e-04
                          10        20
                  ....*....|....*....|....*.
gi 28572159   257 SLVKHERTHRNERPYACKTCGKKFTY 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
202-224 9.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 9.70e-04
                          10        20
                  ....*....|....*....|...
gi 28572159   202 LDTHMRRHNDERPYECEICHKSF 224
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
241-335 9.80e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 9.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572159 241 KPYTCQYCQRNFADRTSLVKHERTH----RNERPYAC--KTCGKKFTYASVLKMHYKTHTGEKPHICQLCNKSFARIHNL 314
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSVnhsgESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                        90       100
                ....*....|....*....|..
gi 28572159 315 VA-HLQTQQHINDPRLTAYLST 335
Cdd:COG5048 368 NNePPQSLQQYKDLKNDKKSET 389
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
215-237 2.12e-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: 2.12e-03
                          10        20
                  ....*....|....*....|...
gi 28572159   215 YECEICHKSFHVNYQLKRHIRQH 237
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
230-253 3.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.09e-03
                          10        20
                  ....*....|....*....|....
gi 28572159   230 LKRHIRQHTGAKPYTCQYCQRNFA 253
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
PHA00733 PHA00733
hypothetical protein
214-261 4.19e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 28572159  214 PYECEICHKSFHVNYQLKRHIRQHTGAKpyTCQYCQRNFADRTSLVKH 261
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
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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