NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622847849|ref|XP_028686079|]
View 

zinc finger protein 84 isoform X1 [Macaca mulatta]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204726)

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|1.10.287.1360
Gene Ontology:  GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 2.37e-34

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 125.01  E-value: 2.37e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849   32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLGYEVMKPDVIFKLEQGEEPWV 91
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-752 2.61e-16

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.44  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 340 KPYGCSECGRAFSEKSNLINHQRIHTGEKPFECR--ECGKAFSRKSQLVTHHRTHTGTKPFGCSDCR-KAFFEKSELIRH 416
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLpLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 417 QTIHTGEKPYECSECRKAFRERSSLINHQRTHTGEKPHGCIQCGKAFSQKSHLISHQMTHTGEkpficSKCGKAFSRKSQ 496
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 497 LVRHQRTHTGEKPYECSECGKAFSEKLSLTNHQRIHTgEKPYVCSECGKAF------CQKSHLISHQRTHTGEKPYECTE 570
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 571 CGKAFGEKSSLATHQRTHTG-EKPYECRDCEKAFSQKSQLNTHQR--IHTGE--KPYEC--SLCRKAFFEKSELIRHLRT 643
Cdd:COG5048   266 PTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 644 HTGEKPYECNECR-------KAFREKSSLINHQRIHTGEKPFEC--SECGKAFSRKSHLIPHQRTHTGEKPYGC--SECR 712
Cdd:COG5048   346 HTSISPAKEKLLNssskfspLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622847849 713 KAFSQKSQLVNHQRIHTgEKPYQCIECGKAFSQKSQLINH 752
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-325 1.08e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*
gi 1622847849 301 LTSHQRTHTGEKPYECGECGKAFSR 325
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 286-308 6.79e-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: 6.79e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 286 YNCSQCGKAFSQKSQLTSHQRTH 308
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 2.37e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 125.01  E-value: 2.37e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849   32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLGYEVMKPDVIFKLEQGEEPWV 91
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 32-71 7.25e-22

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: 88.68  E-value: 7.25e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622847849  32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLG 71
Cdd:pfam01352   3 TFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 32-70 3.66e-19

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: 81.06  E-value: 3.66e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622847849  32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSL 70
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-752 2.61e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.44  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 340 KPYGCSECGRAFSEKSNLINHQRIHTGEKPFECR--ECGKAFSRKSQLVTHHRTHTGTKPFGCSDCR-KAFFEKSELIRH 416
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLpLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 417 QTIHTGEKPYECSECRKAFRERSSLINHQRTHTGEKPHGCIQCGKAFSQKSHLISHQMTHTGEkpficSKCGKAFSRKSQ 496
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 497 LVRHQRTHTGEKPYECSECGKAFSEKLSLTNHQRIHTgEKPYVCSECGKAF------CQKSHLISHQRTHTGEKPYECTE 570
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 571 CGKAFGEKSSLATHQRTHTG-EKPYECRDCEKAFSQKSQLNTHQR--IHTGE--KPYEC--SLCRKAFFEKSELIRHLRT 643
Cdd:COG5048   266 PTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 644 HTGEKPYECNECR-------KAFREKSSLINHQRIHTGEKPFEC--SECGKAFSRKSHLIPHQRTHTGEKPYGC--SECR 712
Cdd:COG5048   346 HTSISPAKEKLLNssskfspLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622847849 713 KAFSQKSQLVNHQRIHTgEKPYQCIECGKAFSQKSQLINH 752
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
497-520 3.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....
gi 1622847849 497 LVRHQRTHTGEKPYECSECGKAFS 520
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-325 1.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*
gi 1622847849 301 LTSHQRTHTGEKPYECGECGKAFSR 325
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 340-388 4.32e-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: 36.77  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622847849 340 KPYgCSECGRAFSEKSNLINHQRIHTgekpFECRECGKAFSRKSQLVTH 388
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 286-308 6.79e-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: 6.79e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 286 YNCSQCGKAFSQKSQLTSHQRTH 308
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 2.37e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 125.01  E-value: 2.37e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849   32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLGYEVMKPDVIFKLEQGEEPWV 91
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 32-71 7.25e-22

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: 88.68  E-value: 7.25e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622847849  32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLG 71
Cdd:pfam01352   3 TFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 32-70 3.66e-19

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: 81.06  E-value: 3.66e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622847849  32 SFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSL 70
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-752 2.61e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.44  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 340 KPYGCSECGRAFSEKSNLINHQRIHTGEKPFECR--ECGKAFSRKSQLVTHHRTHTGTKPFGCSDCR-KAFFEKSELIRH 416
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLpLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 417 QTIHTGEKPYECSECRKAFRERSSLINHQRTHTGEKPHGCIQCGKAFSQKSHLISHQMTHTGEkpficSKCGKAFSRKSQ 496
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 497 LVRHQRTHTGEKPYECSECGKAFSEKLSLTNHQRIHTgEKPYVCSECGKAF------CQKSHLISHQRTHTGEKPYECTE 570
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 571 CGKAFGEKSSLATHQRTHTG-EKPYECRDCEKAFSQKSQLNTHQR--IHTGE--KPYEC--SLCRKAFFEKSELIRHLRT 643
Cdd:COG5048   266 PTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 644 HTGEKPYECNECR-------KAFREKSSLINHQRIHTGEKPFEC--SECGKAFSRKSHLIPHQRTHTGEKPYGC--SECR 712
Cdd:COG5048   346 HTSISPAKEKLLNssskfspLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622847849 713 KAFSQKSQLVNHQRIHTgEKPYQCIECGKAFSQKSQLINH 752
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
284-691 7.34e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.81  E-value: 7.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 284 KPYNCSQCGKAFSQKSQLTSHQRTHTGEKPYECG--ECGKAFSRKSHLISHWRTHTgekpygcsecgrafSEKSNLINHQ 361
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH--------------NNPSDLNSKS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 362 RIHTGEKPFEC--RECGKAFSRKSQLVTH---HRTHTGTKPFGCSDC--RKAFFEKSELIRHQTIHTGEKPYECS--ECR 432
Cdd:COG5048    98 LPLSNSKASSSslSSSSSNSNDNNLLSSHslpPSSRDPQLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLPanSLS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 433 KAFRERSSLINHQRTHTGEKPHGCIQCGKAFSQKSHLISHQMTHTGEKPFICSKCGKAFSRKSQLVRHQRTHTGEKPYEC 512
Cdd:COG5048   178 KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 513 SECGKAFSEKLSLTNHQRIHTGE-------KPYVCSECGKAFCQKSHLISHQRT--HTGE--KPYECTE--CGKAFGEKS 579
Cdd:COG5048   258 SESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRND 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 580 SLATHQRTHTGEKPYEC--RDCEKAFSQKS-----QLNTHQRIHTGEKPYECSL--CRKAFFEKSELIRHLRTHTGEKPY 650
Cdd:COG5048   338 ALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPY 417

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1622847849 651 ECN--ECRKAFREKSSLINHQRIHTGEKPFECSECGKAFSRKS 691
Cdd:COG5048   418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
258-668 8.88e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 258 FGCGNCGKTFPQKSQFITHHRTHTGEKPYNCSQ--CGKAFSQKSQLTSHQRTHTGEKPYEC--GECGKAFSRKSHLISHW 333
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 334 RTHTgekPYGCSECGRAFSEKSNLINHQRIHTGEKPFECRECGKAFSRKSQLVTHHRTHTGTKPFGCSDcrkAFFEKSEL 413
Cdd:COG5048   114 SSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKD---PSSNLSLL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 414 IRHQTIHTGEKPYECSECRKAFRERSSLINHQRTHTGE-----KPHGCIQCGKAFSQKSHLISHQMTHTGEKPFICSKCG 488
Cdd:COG5048   188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSslpltTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 489 KAFSRKSQLVRHQRTHTG-EKPYECSECGKAFSEKLSLTNHQR--IHTGE--KPYVCSE--CGKAFCQKSHLISHQRTHT 561
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 562 GEKPYEC--TECGKAFGEKSSLATHQRTH-----TGEKPYEC--RDCEKAFSQKSQLNTHQRIHTGEKPYEC--SLCRKA 630
Cdd:COG5048   348 SISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKS 427

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1622847849 631 FFEKSELIRHLRTHTgEKPYECNECRKAFREKSSLINH 668
Cdd:COG5048   428 FNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
222-642 7.26e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 222 RNRLGEKLYECS--ECRKRFSKKPSLIKHQSRHIRD-IAFGCGNCGKTFPQKSQFITHHRTHTGEKPYNCSQCGKAFSQK 298
Cdd:COG5048    54 RSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNpSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 299 SQLTSHQRTHTgeKPYECGECGKAFSRKSHLISHWRTHTGEKPygcSECGRAFSEKSNLINHQRIHTGekpfecrecgka 378
Cdd:COG5048   134 DPQLPDLLSIS--NLRNNPLPGNNSSSVNTPQSNSLHPPLPAN---SLSKDPSSNLSLLISSNVSTSI------------ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 379 fsrKSQLVTHHRTHTGTKPFGCSDCRKAFFEKSELIRHQTIhtgekpyeCSECRKAFRERSSLINHQRTHTGEKPHGCIQ 458
Cdd:COG5048   197 ---PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ--------LSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 459 CGKAFSQKSHLISHQMTHTG-EKPFICSKCGKAFSRKSQLVRHQRT--HTGE--KPYECSE--CGKAFSEKLSLTNHQRI 531
Cdd:COG5048   266 PTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 532 HTGEKPYVC--SECGKAFCQKSH-----LISHQRTHTGEKPYECT--ECGKAFGEKSSLATHQRTHTGEKPYECRD--CE 600
Cdd:COG5048   346 HTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCS 425

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1622847849 601 KAFSQKSQLNTHQRIHTGEKPYECSLCRKaFFEKSELIRHLR 642
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
452-756 1.67e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 452 KPHGCIQCGKAFSQKSHLISHQMTHTGEKPFICSK--CGKAFSRKSQLVRHQRTHTGEKPYECS---------------- 513
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 514 ECGKAFSEKLSLTNH---QRIHTGEKPYVCSEC--GKAFCQKSHLISHQRTHTGEKPYECT---ECGKAFGEKSSLATHQ 585
Cdd:COG5048   112 SSSSNSNDNNLLSSHslpPSSRDPQLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLPansLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 586 RTHTGEKPYECRDCEKAFSQKSQlNTHQRIHTGEKPYECSLCRKAFFEKSELIRHLRTHTGEKPYECNECRKAFREKSSL 665
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSS-SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 666 INHQRIHTGE-------KPFECSECGKAFSRKSHLIPHQRT--HTGE--KPYGCSE--CRKAFSQKSQLVNHQRIHTGEK 732
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                         330       340
                  ....*....|....*....|....*.
gi 1622847849 733 PYQCI--ECGKAFSQKSQLINHQRTH 756
Cdd:COG5048   351 PAKEKllNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
480-761 6.01e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 6.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 480 KPFICSKCGKAFSRKSQLVRHQRTHTGEKPYECS--ECGKAFSEKLSLTNHQRIHTGEKPYVCS-ECGKAFCQKSHLISH 556
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 557 QRTHTGEKPYECTECGKAFGEKSSLA--THQRTHTGEKPYE-----CRDCEKAFSQKSQLNTH----------------Q 613
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPgnnssSVNTPQSNSLHPPLPANslskdpssnlsllissN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 614 RIHTGEKPYECSLCRKAFFEKSELIRHLRTHTgEKPYECNECRKAF------REKSSLINHQRIHTGEKPFECSECGKAF 687
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847849 688 SRKSHLIPHQRTHTG-EKPYGCSECRKAFSQKSQLVNHQR--IHTGE--KPYQC--IECGKAFSQKSQLINHQRTHTVKK 760
Cdd:COG5048   271 QSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350


                  .
gi 1622847849 761 S 761
Cdd:COG5048   351 P 351
zf-H2C2_2 pfam13465
Zinc-finger double domain;
497-520 3.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....
gi 1622847849 497 LVRHQRTHTGEKPYECSECGKAFS 520
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
356-381 4.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622847849 356 NLINHQRIHTGEKPFECRECGKAFSR 381
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
721-745 5.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.69e-04
                          10        20
                  ....*....|....*....|....*
gi 1622847849 721 LVNHQRIHTGEKPYQCIECGKAFSQ 745
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
636-659 6.16e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.16e-04
                          10        20
                  ....*....|....*....|....
gi 1622847849 636 ELIRHLRTHTGEKPYECNECRKAF 659
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
552-575 6.41e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.41e-04
                          10        20
                  ....*....|....*....|....
gi 1622847849 552 HLISHQRTHTGEKPYECTECGKAF 575
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
664-689 9.49e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.49e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622847849 664 SLINHQRIHTGEKPFECSECGKAFSR 689
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-325 1.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*
gi 1622847849 301 LTSHQRTHTGEKPYECGECGKAFSR 325
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
580-605 1.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622847849 580 SLATHQRTHTGEKPYECRDCEKAFSQ 605
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 482-504 2.22e-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: 2.22e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 482 FICSKCGKAFSRKSQLVRHQRTH 504
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
524-547 2.88e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.88e-03
                          10        20
                  ....*....|....*....|....
gi 1622847849 524 SLTNHQRIHTGEKPYVCSECGKAF 547
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 538-560 3.04e-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: 35.74  E-value: 3.04e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 538 YVCSECGKAFCQKSHLISHQRTH 560
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-631 3.98e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.98e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 609 LNTHQRIHTGEKPYECSLCRKAF 631
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 340-388 4.32e-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: 36.77  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622847849 340 KPYgCSECGRAFSEKSNLINHQRIHTgekpFECRECGKAFSRKSQLVTH 388
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 536-584 4.32e-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: 36.77  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622847849 536 KPYvCSECGKAFCQKSHLISHQRTHTgekpYECTECGKAFGEKSSLATH 584
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-435 4.66e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.66e-03
                          10        20
                  ....*....|....*....|....
gi 1622847849 412 ELIRHQTIHTGEKPYECSECRKAF 435
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 314-336 5.01e-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: 5.01e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 314 YECGECGKAFSRKSHLISHWRTH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 286-308 6.79e-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: 6.79e-03
                          10        20
                  ....*....|....*....|...
gi 1622847849 286 YNCSQCGKAFSQKSQLTSHQRTH 308
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
276-297 8.48e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.48e-03
                          10        20
                  ....*....|....*....|..
gi 1622847849 276 HHRTHTGEKPYNCSQCGKAFSQ 297
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH