NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|281362562|ref|NP_651389|]
View 

uncharacterized protein Dmel_CG11902 [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 6-83 1.34e-10

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: 58.62  E-value: 1.34e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362562     6 VCRTCAVQNSQLLPLStcLDKDSSKSYYAVLQELTQIDLeNTDDNLPQHICSECWRRMESAYTFVQQARKVHGELLAQ 83
Cdd:pfam07776    1 VCRLCLDESDELIPIF--DPSDSEKTLAEILEDCTGIEL-DPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1340-1364 3.35e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-05
                           10        20
                   ....*....|....*....|....*
gi 281362562  1340 LQQHMRIHSGERPYKCTYCEKSFTQ 1364
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 1349-1405 5.61e-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: 43.94  E-value: 5.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362562 1349 GERPYKCTY--CEKSFTQSNDLTLHiRRH--------------------TGERPYQCGVCGERFIQGTALKNHRMQQSH 1405
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHRKHSHD 423
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 673-726 5.64e-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.


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 40.23  E-value: 5.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281362562  673 KLKCDQCEKVFiwhKDlnrHKRLHQPQSAAQFDCPHCHRRFHRKDGLKSH-LKVH 726
Cdd:cd20908     1 KPWCYYCDREF---DD---EKILIQHQKAKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1283-1306 6.36e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 6.36e-04
                           10        20
                   ....*....|....*....|....
gi 281362562  1283 NLIIHMRRHTGEKPFKCEYCTMAF 1306
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 ...
 6-83 1.34e-10

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: 58.62  E-value: 1.34e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362562     6 VCRTCAVQNSQLLPLStcLDKDSSKSYYAVLQELTQIDLeNTDDNLPQHICSECWRRMESAYTFVQQARKVHGELLAQ 83
Cdd:pfam07776    1 VCRLCLDESDELIPIF--DPSDSEKTLAEILEDCTGIEL-DPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-82 5.15e-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: 54.06  E-value: 5.15e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362562      6 VCRTCAVQNSQLLPLStclDKDSSKSYYAVLQELTQIDLENtDDNLPQHICSECWRRMESAYTFVQQARKVHGELLA 82
Cdd:smart00868    1 VCRLCLSESENLVSIF---DESSEASLAEKIEECTGIEIEP-DDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1340-1364 3.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-05
                           10        20
                   ....*....|....*....|....*
gi 281362562  1340 LQQHMRIHSGERPYKCTYCEKSFTQ 1364
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 1349-1405 5.61e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 5.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362562 1349 GERPYKCTY--CEKSFTQSNDLTLHiRRH--------------------TGERPYQCGVCGERFIQGTALKNHRMQQSH 1405
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHRKHSHD 423
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 673-726 5.64e-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: 40.23  E-value: 5.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281362562  673 KLKCDQCEKVFiwhKDlnrHKRLHQPQSAAQFDCPHCHRRFHRKDGLKSH-LKVH 726
Cdd:cd20908     1 KPWCYYCDREF---DD---EKILIQHQKAKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1283-1306 6.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 6.36e-04
                           10        20
                   ....*....|....*....|....
gi 281362562  1283 NLIIHMRRHTGEKPFKCEYCTMAF 1306
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1367-1392 8.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 8.09e-03
                           10        20
                   ....*....|....*....|....*.
gi 281362562  1367 DLTLHIRRHTGERPYQCGVCGERFIQ 1392
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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 ...
 6-83 1.34e-10

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: 58.62  E-value: 1.34e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362562     6 VCRTCAVQNSQLLPLStcLDKDSSKSYYAVLQELTQIDLeNTDDNLPQHICSECWRRMESAYTFVQQARKVHGELLAQ 83
Cdd:pfam07776    1 VCRLCLDESDELIPIF--DPSDSEKTLAEILEDCTGIEL-DPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-82 5.15e-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: 54.06  E-value: 5.15e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362562      6 VCRTCAVQNSQLLPLStclDKDSSKSYYAVLQELTQIDLENtDDNLPQHICSECWRRMESAYTFVQQARKVHGELLA 82
Cdd:smart00868    1 VCRLCLSESENLVSIF---DESSEASLAEKIEECTGIEIEP-DDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1340-1364 3.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-05
                           10        20
                   ....*....|....*....|....*
gi 281362562  1340 LQQHMRIHSGERPYKCTYCEKSFTQ 1364
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 1349-1405 5.61e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 5.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362562 1349 GERPYKCTY--CEKSFTQSNDLTLHiRRH--------------------TGERPYQCGVCGERFIQGTALKNHRMQQSH 1405
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHRKHSHD 423
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 673-726 5.64e-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: 40.23  E-value: 5.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281362562  673 KLKCDQCEKVFiwhKDlnrHKRLHQPQSAAQFDCPHCHRRFHRKDGLKSH-LKVH 726
Cdd:cd20908     1 KPWCYYCDREF---DD---EKILIQHQKAKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1283-1306 6.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 6.36e-04
                           10        20
                   ....*....|....*....|....
gi 281362562  1283 NLIIHMRRHTGEKPFKCEYCTMAF 1306
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1367-1392 8.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 8.09e-03
                           10        20
                   ....*....|....*....|....*.
gi 281362562  1367 DLTLHIRRHTGERPYQCGVCGERFIQ 1392
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1353-1375 8.95e-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: 8.95e-03
                           10        20
                   ....*....|....*....|...
gi 281362562  1353 YKCTYCEKSFTQSNDLTLHIRRH 1375
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH