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Conserved domains on  [gi|152963633|ref|NP_919306|]
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zinc finger protein 30 isoform b [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.76e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 2.76e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152963633    14 VTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSMGHSRSKPHVIALLEQWKEPEV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-623 4.37e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 244 YGKLTRHQSTHTGE----KPFGCEECGKAFSTFSYLVQHQRIHTSEKPYEC--KECGKAFSTSSPLAKHQRIHTGEKPYE 317
Cdd:COG5048   14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 318 CKECGK---------------SFTVYGQLTRHQSI-HTGEKPFECKECGKAFRLSSFLHAHQRIHAEIKPYGCK------ 375
Cdd:COG5048   94 NSKSLPlsnskasssslssssSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpplpa 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 376 --ECGRTFSRASYLVQHGRLHTGEKPYECKECgkaFSTGSY--LVQHQRIHTGEKPYECKECGkaFISRHQLTVHQRVHT 451
Cdd:COG5048  174 nsLSKDPSSNLSLLISSNVSTSIPSSSENSPL---SSSYSIpsSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 452 GEK--PYECKECGKAFRVHVHLTQHRKIHTDV-------KPYECKECGKTFSRASYLVQHSR--IHTGK--KPYECKE-- 516
Cdd:COG5048  249 SSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 517 CGKAFSSGSYLVQHQRIHTGEKPYEC--NKCGKAFTV-----YGQLIGHQSVHTGEKPFEC--KECGKAFRLNSFLTEHQ 587
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 152963633 588 RVHTGEKP--FKCKKCGKTFRYSSALKVHLRKHMSVIP 623
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
96-301 2.62e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633  96 CKEMPTSENCPSFALHQKISRQKPRecqeyGKTLCQDSKPVQH--ERIHSSEKPNRCKECGKNFSNGHQLTIHQR--LHV 171
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSL-----PTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 172 GE--KPY--KYEKCGKAFISGSAFVKHGRIHTGEKPLKCK--QCGKTISG-----SYQLTVHKSIHTGKKPYEC--GECG 238
Cdd:COG5048  316 GEslKPFscPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCI 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152963633 239 KAFLVYGKLTRHQSTHTGEKPFGCE--ECGKAFSTFSYLVQHQRIHTSEKPYECKECGKAFSTSS 301
Cdd:COG5048  396 RNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.76e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 2.76e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152963633    14 VTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSMGHSRSKPHVIALLEQWKEPEV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 4.94e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 91.76  E-value: 4.94e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 152963633   13 SVTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSMG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 3.82e-21

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 86.45  E-value: 3.82e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 152963633  14 VTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSM 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-623 4.37e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 244 YGKLTRHQSTHTGE----KPFGCEECGKAFSTFSYLVQHQRIHTSEKPYEC--KECGKAFSTSSPLAKHQRIHTGEKPYE 317
Cdd:COG5048   14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 318 CKECGK---------------SFTVYGQLTRHQSI-HTGEKPFECKECGKAFRLSSFLHAHQRIHAEIKPYGCK------ 375
Cdd:COG5048   94 NSKSLPlsnskasssslssssSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpplpa 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 376 --ECGRTFSRASYLVQHGRLHTGEKPYECKECgkaFSTGSY--LVQHQRIHTGEKPYECKECGkaFISRHQLTVHQRVHT 451
Cdd:COG5048  174 nsLSKDPSSNLSLLISSNVSTSIPSSSENSPL---SSSYSIpsSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 452 GEK--PYECKECGKAFRVHVHLTQHRKIHTDV-------KPYECKECGKTFSRASYLVQHSR--IHTGK--KPYECKE-- 516
Cdd:COG5048  249 SSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 517 CGKAFSSGSYLVQHQRIHTGEKPYEC--NKCGKAFTV-----YGQLIGHQSVHTGEKPFEC--KECGKAFRLNSFLTEHQ 587
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 152963633 588 RVHTGEKP--FKCKKCGKTFRYSSALKVHLRKHMSVIP 623
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
96-301 2.62e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633  96 CKEMPTSENCPSFALHQKISRQKPRecqeyGKTLCQDSKPVQH--ERIHSSEKPNRCKECGKNFSNGHQLTIHQR--LHV 171
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSL-----PTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 172 GE--KPY--KYEKCGKAFISGSAFVKHGRIHTGEKPLKCK--QCGKTISG-----SYQLTVHKSIHTGKKPYEC--GECG 238
Cdd:COG5048  316 GEslKPFscPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCI 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152963633 239 KAFLVYGKLTRHQSTHTGEKPFGCE--ECGKAFSTFSYLVQHQRIHTSEKPYECKECGKAFSTSS 301
Cdd:COG5048  396 RNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-439 3.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.77e-04
                          10        20
                  ....*....|....*....|....*.
gi 152963633  414 YLVQHQRIHTGEKPYECKECGKAFIS 439
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 258-310 1.02e-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: 38.31  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 152963633 258 KPFgCEECGKAFSTFSYLVQHQRIHTsekpYECKECGKAFSTSSPLAKH-QRIH 310
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.76e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 2.76e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152963633    14 VTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSMGHSRSKPHVIALLEQWKEPEV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 4.94e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 91.76  E-value: 4.94e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 152963633   13 SVTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSMG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 3.82e-21

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 86.45  E-value: 3.82e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 152963633  14 VTFEDVAIAFSQQEWESLDSSQRGLYRDVMLENYRNLVSM 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-623 4.37e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 244 YGKLTRHQSTHTGE----KPFGCEECGKAFSTFSYLVQHQRIHTSEKPYEC--KECGKAFSTSSPLAKHQRIHTGEKPYE 317
Cdd:COG5048   14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 318 CKECGK---------------SFTVYGQLTRHQSI-HTGEKPFECKECGKAFRLSSFLHAHQRIHAEIKPYGCK------ 375
Cdd:COG5048   94 NSKSLPlsnskasssslssssSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpplpa 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 376 --ECGRTFSRASYLVQHGRLHTGEKPYECKECgkaFSTGSY--LVQHQRIHTGEKPYECKECGkaFISRHQLTVHQRVHT 451
Cdd:COG5048  174 nsLSKDPSSNLSLLISSNVSTSIPSSSENSPL---SSSYSIpsSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 452 GEK--PYECKECGKAFRVHVHLTQHRKIHTDV-------KPYECKECGKTFSRASYLVQHSR--IHTGK--KPYECKE-- 516
Cdd:COG5048  249 SSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 517 CGKAFSSGSYLVQHQRIHTGEKPYEC--NKCGKAFTV-----YGQLIGHQSVHTGEKPFEC--KECGKAFRLNSFLTEHQ 587
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 152963633 588 RVHTGEKP--FKCKKCGKTFRYSSALKVHLRKHMSVIP 623
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
96-301 2.62e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633  96 CKEMPTSENCPSFALHQKISRQKPRecqeyGKTLCQDSKPVQH--ERIHSSEKPNRCKECGKNFSNGHQLTIHQR--LHV 171
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSL-----PTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 172 GE--KPY--KYEKCGKAFISGSAFVKHGRIHTGEKPLKCK--QCGKTISG-----SYQLTVHKSIHTGKKPYEC--GECG 238
Cdd:COG5048  316 GEslKPFscPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCI 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152963633 239 KAFLVYGKLTRHQSTHTGEKPFGCE--ECGKAFSTFSYLVQHQRIHTSEKPYECKECGKAFSTSS 301
Cdd:COG5048  396 RNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 536-618 6.00e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.86  E-value: 6.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152963633 536 GEKPYECN--KCGKAFT-----VYGQLIGHQSVHTGEKPFECKecgkafrLNSFLTEhqrvhtgEKPFKCKKCGKTFRYS 608
Cdd:COG5189  346 DGKPYKCPveGCNKKYKnqnglKYHMLHGHQNQKLHENPSPEK-------MNIFSAK-------DKPYRCEVCDKRYKNL 411

                         90
                 ....*....|
gi 152963633 609 SALKVHlRKH 618
Cdd:COG5189  412 NGLKYH-RKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-439 3.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.77e-04
                          10        20
                  ....*....|....*....|....*.
gi 152963633  414 YLVQHQRIHTGEKPYECKECGKAFIS 439
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-523 5.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 152963633  498 YLVQHSRIHTGKKPYECKECGKAFSS 523
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-326 5.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.53e-04
                          10        20
                  ....*....|....*....|....
gi 152963633  303 LAKHQRIHTGEKPYECKECGKSFT 326
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 7.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 152963633  274 YLVQHQRIHTSEKPYECKECGKAFST 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-550 9.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.21e-04
                          10        20
                  ....*....|....*....|....*
gi 152963633  526 YLVQHQRIHTGEKPYECNKCGKAFT 550
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 258-310 1.02e-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: 38.31  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 152963633 258 KPFgCEECGKAFSTFSYLVQHQRIHTsekpYECKECGKAFSTSSPLAKH-QRIH 310
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
583-607 2.53e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.53e-03
                          10        20
                  ....*....|....*....|....*
gi 152963633  583 LTEHQRVHTGEKPFKCKKCGKTFRY 607
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-465 4.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|...
gi 152963633  443 LTVHQRVHTGEKPYECKECGKAF 465
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
331-353 4.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.52e-03
                          10        20
                  ....*....|....*....|...
gi 152963633  331 LTRHQSIHTGEKPFECKECGKAF 353
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 596-618 4.59e-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: 4.59e-03
                          10        20
                  ....*....|....*....|...
gi 152963633  596 FKCKKCGKTFRYSSALKVHLRKH 618
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 398-450 5.18e-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: 36.38  E-value: 5.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 152963633 398 KPYeCKECGKAFSTGSYLVQHQRIHTgekpYECKECGKAFISRHQLTVH-QRVH 450
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 370-422 6.25e-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: 36.00  E-value: 6.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 152963633 370 KPYgCKECGRTFSRASYLVQHGRLHTgekpYECKECGKAFSTGSYLVQH-QRIH 422
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
470-495 7.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 152963633  470 HLTQHRKIHTDVKPYECKECGKTFSR 495
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 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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