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Conserved domains on  [gi|403273388|ref|XP_003928498|]
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LOW QUALITY PROTEIN: zinc finger protein 205 [Saimiri boliviensis boliviensis]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

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

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  22803940|14519192|8183940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 4.40e-16

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 72.63  E-value: 4.40e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 403273388   124 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQK--RNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
307-487 4.44e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 307 KSYQCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 377 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicgkcftqssalvthqrthtgvkpypC 451
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 403273388 452 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 487
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 477-499 2.46e-05

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: 41.13  E-value: 2.46e-05
                          10        20
                  ....*....|....*....|...
gi 403273388  477 YHCLDCGKSFSHSSHLTAHQRTH 499
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 505-527 1.43e-04

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: 38.82  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|...
gi 403273388  505 YACPLCGKSFSRRSNLHRHEKIH 527
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 194-336 4.31e-04

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 42.93  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 194 CRGECTGPIQEGQVVPTPPVAALGDVKPF---RIRAGKVQGAVPQCAQEAACGRSSGLARDAGQPGDPDSTPGAAPPDP- 269
Cdd:cd23959  128 ETHKTAQVAPPKAEPQTAPVTPFGQLPMFgqhPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDTAPSSg 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 403273388 270 -SPPEAQEGRVPGKpieeeKGTPESGEEGLAPD---GEAGRKSYQCEQCGKGFSWHSHLVTHRRTHTGEKP 336
Cdd:cd23959  208 aPDGFPAEASAPSP-----FAAPASAASFPAAPvanGEAATPTHACTICGKAFSTHEGLRMHSKAKHGVEL 273
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 4.40e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 72.63  E-value: 4.40e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 403273388   124 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQK--RNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 124-161 1.18e-13

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: 64.88  E-value: 1.18e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 403273388 124 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQK--RNGLSL 161
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLEnyENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 123-162 2.36e-13

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: 64.03  E-value: 2.36e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 403273388  123 PVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ--KRNGLSLG 162
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLenYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
307-487 4.44e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 307 KSYQCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 377 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicgkcftqssalvthqrthtgvkpypC 451
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 403273388 452 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 487
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
435-460 1.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 403273388  435 ALVTHQRTHTGVKPYPCPECGKCFSQ 460
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 477-499 2.46e-05

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: 41.13  E-value: 2.46e-05
                          10        20
                  ....*....|....*....|...
gi 403273388  477 YHCLDCGKSFSHSSHLTAHQRTH 499
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 505-527 1.43e-04

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: 38.82  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|...
gi 403273388  505 YACPLCGKSFSRRSNLHRHEKIH 527
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 194-336 4.31e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 42.93  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 194 CRGECTGPIQEGQVVPTPPVAALGDVKPF---RIRAGKVQGAVPQCAQEAACGRSSGLARDAGQPGDPDSTPGAAPPDP- 269
Cdd:cd23959  128 ETHKTAQVAPPKAEPQTAPVTPFGQLPMFgqhPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDTAPSSg 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 403273388 270 -SPPEAQEGRVPGKpieeeKGTPESGEEGLAPD---GEAGRKSYQCEQCGKGFSWHSHLVTHRRTHTGEKP 336
Cdd:cd23959  208 aPDGFPAEASAPSP-----FAAPASAASFPAAPvanGEAATPTHACTICGKAFSTHEGLRMHSKAKHGVEL 273
PHA00733 PHA00733
hypothetical protein
 364-411 4.56e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.24  E-value: 4.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 403273388 364 PYTCPACRKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 411
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 363-411 7.48e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 7.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 403273388 363 KPYtCPACRKSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 411
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
ZnF_C2H2 smart00355
zinc finger;
421-443 5.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 5.85e-03
                           10        20
                   ....*....|....*....|...
gi 403273388   421 HKCPICGKCFTQSSALVTHQRTH 443
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
505-527 9.19e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 9.19e-03
                           10        20
                   ....*....|....*....|...
gi 403273388   505 YACPLCGKSFSRRSNLHRHEKIH 527
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 4.40e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 72.63  E-value: 4.40e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 403273388   124 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQK--RNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 124-161 1.18e-13

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: 64.88  E-value: 1.18e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 403273388 124 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQK--RNGLSL 161
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLEnyENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 123-162 2.36e-13

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: 64.03  E-value: 2.36e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 403273388  123 PVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ--KRNGLSLG 162
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLenYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
307-487 4.44e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 307 KSYQCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 377 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicgkcftqssalvthqrthtgvkpypC 451
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 403273388 452 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 487
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
370-529 1.84e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 370 CRKSFSHHSTLiQHQRIHTgekPYVCDRCAKRFTRRSDLVTHQGT--HTG--AKPHKCPI--CGKCFTQSSALVTHQRTH 443
Cdd:COG5048  271 QSSSPNESDSS-SEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 444 TGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD---------CGKSFSHSSHLTAHQRTHRGVRPYAC--PLCGK 512
Cdd:COG5048  347 TSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSK 426

                        170
                 ....*....|....*..
gi 403273388 513 SFSRRSNLHRHEKIHTT 529
Cdd:COG5048  427 SFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
363-524 4.40e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 363 KPYTCPACRKSFSHHSTLIQHQR--IHTGE--KPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPICGKCFTQSSAL 436
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 437 VT-------HQRTHTGVKPYPC--PECGKCFSQRSNLIAHNRTHTGEKPYHC--LDCGKSFSHSSHLTAHQRTHRGVRPY 505
Cdd:COG5048  368 NNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*....
gi 403273388 506 ACPLCGKSFSRRSNLHRHE 524
Cdd:COG5048  448 LCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
307-528 6.15e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 6.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 307 KSYQCEQCGKGFSWHSHLVTHRRTHTGEKPYACTD--CGKRFGRSSHLIQHQIIHTGEKPYTCPACRKS----------- 373
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 374 ---------------------------FSHHSTLIQHQRIHTGEKPYVCDRCA-------------KRFTRRSDLVTHQG 413
Cdd:COG5048  112 ssssnsndnnllsshslppssrdpqlpDLLSISNLRNNPLPGNNSSSVNTPQSnslhpplpanslsKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 414 THTGAKPHKCPICGKCFTQSSALVTHQRTHTGVKPYPCPECGKCF---------------------------------SQ 460
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsqspsslsssdssssasesprsslptasSQ 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 403273388 461 RSNLIAHN-RTHTG-EKPYHCLDCGKSFSHSSHLTAHQRTH----RGVRPYACP--LCGKSFSRRSNLHRHEKIHT 528
Cdd:COG5048  272 SSSPNESDsSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSVnhsgESLKPFSCPysLCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
342-527 1.56e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.56  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 342 CGKRFGRSSHLIQHQIIHTGeKPYTCPACRKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPH 421
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSI-PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 422 KCPICGKCFTQSSALVTHQRTHTGV-------KPYPCPECGKCFSQRSNLIAHNRT--HTGE--KPYHC--LDCGKSFSH 488
Cdd:COG5048  256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSR 335

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 403273388 489 SSHLTAHQRTHRGVRPYACPL--CGKSFSRRSNLHRHEKIH 527
Cdd:COG5048  336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
431-499 2.05e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 2.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 403273388 431 TQSSALVTHQRTHTGV----KPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD--CGKSFSHSSHLTAHQRTH 499
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
435-460 1.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 403273388  435 ALVTHQRTHTGVKPYPCPECGKCFSQ 460
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 477-499 2.46e-05

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: 41.13  E-value: 2.46e-05
                          10        20
                  ....*....|....*....|...
gi 403273388  477 YHCLDCGKSFSHSSHLTAHQRTH 499
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
351-376 3.49e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.49e-05
                          10        20
                  ....*....|....*....|....*.
gi 403273388  351 HLIQHQIIHTGEKPYTCPACRKSFSH 376
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 421-443 3.74e-05

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: 40.75  E-value: 3.74e-05
                          10        20
                  ....*....|....*....|...
gi 403273388  421 HKCPICGKCFTQSSALVTHQRTH 443
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
323-346 5.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.65e-05
                          10        20
                  ....*....|....*....|....
gi 403273388  323 HLVTHRRTHTGEKPYACTDCGKRF 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 449-471 7.00e-05

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: 39.98  E-value: 7.00e-05
                          10        20
                  ....*....|....*....|...
gi 403273388  449 YPCPECGKCFSQRSNLIAHNRTH 471
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
463-488 9.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 403273388  463 NLIAHNRTHTGEKPYHCLDCGKSFSH 488
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 505-527 1.43e-04

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: 38.82  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|...
gi 403273388  505 YACPLCGKSFSRRSNLHRHEKIH 527
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
491-516 1.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.87e-04
                          10        20
                  ....*....|....*....|....*.
gi 403273388  491 HLTAHQRTHRGVRPYACPLCGKSFSR 516
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 361-444 2.89e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 361 GEKPYTCP--ACRKSFSHHSTLIQHqRIHtgekpyvcDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICGKCFTQSSALVT 438
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 403273388 439 HqRTHT 444
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-404 4.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.14e-04
                          10        20
                  ....*....|....*....|....*
gi 403273388  380 LIQHQRIHTGEKPYVCDRCAKRFTR 404
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 194-336 4.31e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 42.93  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 194 CRGECTGPIQEGQVVPTPPVAALGDVKPF---RIRAGKVQGAVPQCAQEAACGRSSGLARDAGQPGDPDSTPGAAPPDP- 269
Cdd:cd23959  128 ETHKTAQVAPPKAEPQTAPVTPFGQLPMFgqhPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDTAPSSg 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 403273388 270 -SPPEAQEGRVPGKpieeeKGTPESGEEGLAPD---GEAGRKSYQCEQCGKGFSWHSHLVTHRRTHTGEKP 336
Cdd:cd23959  208 aPDGFPAEASAPSP-----FAAPASAASFPAAPvanGEAATPTHACTICGKAFSTHEGLRMHSKAKHGVEL 273
PHA00733 PHA00733
hypothetical protein
 364-411 4.56e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.24  E-value: 4.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 403273388 364 PYTCPACRKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 411
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 363-411 7.48e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 7.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 403273388 363 KPYtCPACRKSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 411
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
407-432 9.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 403273388  407 DLVTHQGTHTGAKPHKCPICGKCFTQ 432
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-359 1.08e-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: 36.51  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|...
gi 403273388  337 YACTDCGKRFGRSSHLIQHQIIH 359
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 417-499 1.66e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403273388 417 GAKPHKCPI--CGKCFTQSSALVTHQRT-HTGVKPYPCPecgkcfsqrsNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLT 493
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYHMLHgHQNQKLHENP----------SPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                 ....*.
gi 403273388 494 AHqRTH 499
Cdd:COG5189  416 YH-RKH 420
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 365-387 1.91e-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: 1.91e-03
                          10        20
                  ....*....|....*....|...
gi 403273388  365 YTCPACRKSFSHHSTLIQHQRIH 387
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
421-443 5.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 5.85e-03
                           10        20
                   ....*....|....*....|...
gi 403273388   421 HKCPICGKCFTQSSALVTHQRTH 443
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
PHA00733 PHA00733
hypothetical protein
 336-383 8.45e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 403273388 336 PYACTDCGKRFGRSSHLIQHqiIHTGEKPYTCPACRKSFSHHSTLIQH 383
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDH 118
PHA00733 PHA00733
hypothetical protein
 420-467 8.61e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 403273388 420 PHKCPICGKCFTQSSALVTHQR--THTGVkpypCPECGKCFSQRSNLIAH 467
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV----CPVCGKEFRNTDSTLDH 118
ZnF_C2H2 smart00355
zinc finger;
505-527 9.19e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 9.19e-03
                           10        20
                   ....*....|....*....|...
gi 403273388   505 YACPLCGKSFSRRSNLHRHEKIH 527
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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