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Conserved domains on  [gi|1881766203|ref|NP_001372678|]
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zinc finger protein 384 isoform f [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11472214)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-470 1.07e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 268 TKPHKCPHCSKTFANSSYLAQHIRIHSGAKPYSCNFCEKSFRQLSHlqqhTRIHSKMHTETIKPHKCPHCSKTFANTSYL 347
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSP----NESDSSSEKGFSLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 348 AQHLR--IHSG--AKPYNC--SYCQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSN-----LQSHRRQHNKDK 416
Cdd:COG5048   306 TRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqSLQQYKDLKNDK 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1881766203 417 PFKC--HNCHRAYTDAASLEVHLSTHTVKHAKVYTCTICSRAYTSETYLMKHMRKH 470
Cdd:COG5048   386 KSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-470 1.07e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 268 TKPHKCPHCSKTFANSSYLAQHIRIHSGAKPYSCNFCEKSFRQLSHlqqhTRIHSKMHTETIKPHKCPHCSKTFANTSYL 347
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSP----NESDSSSEKGFSLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 348 AQHLR--IHSG--AKPYNC--SYCQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSN-----LQSHRRQHNKDK 416
Cdd:COG5048   306 TRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqSLQQYKDLKNDK 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1881766203 417 PFKC--HNCHRAYTDAASLEVHLSTHTVKHAKVYTCTICSRAYTSETYLMKHMRKH 470
Cdd:COG5048   386 KSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-310 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 1881766203 285 YLAQHIRIHSGAKPYSCNFCEKSFRQ 310
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 395-439 2.62e-03

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: 37.15  E-value: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1881766203 395 CEKAFTQLSNLQshrrQHNKDKPFKCHNCHRAYTDAASLEVHLST 439
Cdd:cd20908     7 CDREFDDEKILI----QHQKAKHFKCHICHKKLYTAGGLAVHCLQ 47
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-470 1.07e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 268 TKPHKCPHCSKTFANSSYLAQHIRIHSGAKPYSCNFCEKSFRQLSHlqqhTRIHSKMHTETIKPHKCPHCSKTFANTSYL 347
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSP----NESDSSSEKGFSLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 348 AQHLR--IHSG--AKPYNC--SYCQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSN-----LQSHRRQHNKDK 416
Cdd:COG5048   306 TRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqSLQQYKDLKNDK 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1881766203 417 PFKC--HNCHRAYTDAASLEVHLSTHTVKHAKVYTCTICSRAYTSETYLMKHMRKH 470
Cdd:COG5048   386 KSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-423 1.31e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 268 TKPHKCPHCSKTFANSSYLAQHIR--IHSG--AKPYSCNF--CEKSFRQLSHLQQHTRIHSKMHTETIKPHKCPHcSKTF 341
Cdd:COG5048   287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSS-KFSP 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881766203 342 ANTSYLAQHLRIHSGAKPYNCSY-----CQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSNLQSHRRQHNKDK 416
Cdd:COG5048   366 LLNNEPPQSLQQYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHA 445


                  ....*..
gi 1881766203 417 PFKCHNC 423
Cdd:COG5048   446 PLLCSIL 452
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-310 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 1881766203 285 YLAQHIRIHSGAKPYSCNFCEKSFRQ 310
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-401 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*...
gi 1881766203 374 HLQQHTRIHTGDRPYKCahPGCEKAFTQ 401
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 271-293 1.80e-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: 36.12  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|...
gi 1881766203 271 HKCPHCSKTFANSSYLAQHIRIH 293
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
257-282 1.83e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.83e-03
                          10        20
                  ....*....|....*....|....*.
gi 1881766203 257 EMQIHSKSHTETKPHKCPHCSKTFAN 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 395-439 2.62e-03

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: 37.15  E-value: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1881766203 395 CEKAFTQLSNLQshrrQHNKDKPFKCHNCHRAYTDAASLEVHLST 439
Cdd:cd20908     7 CDREFDDEKILI----QHQKAKHFKCHICHKKLYTAGGLAVHCLQ 47
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 384-436 2.75e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1881766203 384 GDRPYKCAHPGCEKAFTQLSNLQSHRRQ---------------HN----KDKPFKCHNCHRAYTDAASLEVH 436
Cdd:COG5189   346 DGKPYKCPVEGCNKKYKNQNGLKYHMLHghqnqklhenpspekMNifsaKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
346-371 2.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....*.
gi 1881766203 346 YLAQHLRIHSGAKPYNCSYCQKAFRQ 371
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 299-321 4.36e-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: 4.36e-03
                          10        20
                  ....*....|....*....|...
gi 1881766203 299 YSCNFCEKSFRQLSHLQQHTRIH 321
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 360-382 5.26e-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: 34.58  E-value: 5.26e-03
                          10        20
                  ....*....|....*....|...
gi 1881766203 360 YNCSYCQKAFRQLSHLQQHTRIH 382
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 297-354 7.56e-03

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: 35.61  E-value: 7.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1881766203 297 KPYsCNFCEKSFRQLSHLQQHTRIHskmhtetikpH-KCPHCSKTFantsYLAQHLRIH 354
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAK----------HfKCHICHKKL----YTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 332-354 8.51e-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: 34.20  E-value: 8.51e-03
                          10        20
                  ....*....|....*....|...
gi 1881766203 332 HKCPHCSKTFANTSYLAQHLRIH 354
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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