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Conserved domains on  [gi|190014599|ref|NP_001121695|]
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zinc finger protein 717 isoform a [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
22-82 8.23e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.08  E-value: 8.23e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190014599    22 VSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSLGHYITKPEMIFKLEQGAEPWI 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-689 9.24e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 309 KPYACNWCEKLFSYKSSLIIHQRIHTGEKPYGCN--ECGKTFRRKSFLTLHERTHTGDKPYKC-IECGKTFHCKSLLTLH 385
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 386 HRTHSGEKPYQCSECGKTFSQKSYLTIHHRTHTGEKPYACDHC-------EEAFSHKSRL---------------TVHQR 443
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntPQSNSLHPPLpanslskdpssnlslLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 444 THTGEKPYECNECGKPFINKSNLRLHQRTHTGEKPYECNECGKTFHRKSFLTIHQWTHTGEKPYECNECGKTFRCKSFLT 523
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 524 VHQRTHAGE-------KPYACNECGKTYSHKSYLTVHHRT--HTGE--KPYECNE--CGKSFHCKSFLTIHQRTHAGKKP 590
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 591 YECNECEKTFINKLNLGI-------HKRTHTGERPYEC--NECGKTFRQKSNLSTHQGTHTGEKPYVCN--ECGKTFHRK 659
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410       420       430
                 ....*....|....*....|....*....|
gi 190014599 660 SFLTIHQRTHTGKNRMDVMNVEKLFVRNHT 689
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
561-898 1.76e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 561 KPYECNECGKSFHCKSFLTIHQRTHAGKKPYECN--ECEKTFINKLNLGIHKRTHTGERPYEC----------------N 622
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 623 ECGKTFRQKSNLSTHQGTHTGEKPYVCNECGKTFHRKSFLTIH--------QRTHTGKNRMDVMNVEKLFVRNHTLLYIR 694
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntpQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 695 ELTPGKSPmnvmnveNPFIRRQIFRSIKVFTRGRNPMNVANVEKPCQKSVLTVHH---RTHTGEKPYECNECGKTFCHKS 771
Cdd:COG5048  192 VSTSIPSS-------SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 772 NLSTHQGTHSG-----------EKPYECDECRKTFYDKTVLTIHQRT--HTGE--KPFECKE--CRKTFSQKSKLFVHHR 834
Cdd:COG5048  265 LPTASSQSSSPnesdsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190014599 835 THTGEKPFRC--NECRKTFSQKS-----GLSIHQRTHTGEKPYEC--KECGKTFCQKSHLSRHQQTHIGEKSD 898
Cdd:COG5048  345 LHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
22-82 8.23e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.08  E-value: 8.23e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190014599    22 VSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSLGHYITKPEMIFKLEQGAEPWI 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 21-62 1.47e-21

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: 88.30  E-value: 1.47e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 190014599   21 LVSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSLG 62
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 22-61 9.20e-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: 80.29  E-value: 9.20e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 190014599  22 VSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSL 61
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-689 9.24e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 309 KPYACNWCEKLFSYKSSLIIHQRIHTGEKPYGCN--ECGKTFRRKSFLTLHERTHTGDKPYKC-IECGKTFHCKSLLTLH 385
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 386 HRTHSGEKPYQCSECGKTFSQKSYLTIHHRTHTGEKPYACDHC-------EEAFSHKSRL---------------TVHQR 443
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntPQSNSLHPPLpanslskdpssnlslLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 444 THTGEKPYECNECGKPFINKSNLRLHQRTHTGEKPYECNECGKTFHRKSFLTIHQWTHTGEKPYECNECGKTFRCKSFLT 523
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 524 VHQRTHAGE-------KPYACNECGKTYSHKSYLTVHHRT--HTGE--KPYECNE--CGKSFHCKSFLTIHQRTHAGKKP 590
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 591 YECNECEKTFINKLNLGI-------HKRTHTGERPYEC--NECGKTFRQKSNLSTHQGTHTGEKPYVCN--ECGKTFHRK 659
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410       420       430
                 ....*....|....*....|....*....|
gi 190014599 660 SFLTIHQRTHTGKNRMDVMNVEKLFVRNHT 689
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
561-898 1.76e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 561 KPYECNECGKSFHCKSFLTIHQRTHAGKKPYECN--ECEKTFINKLNLGIHKRTHTGERPYEC----------------N 622
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 623 ECGKTFRQKSNLSTHQGTHTGEKPYVCNECGKTFHRKSFLTIH--------QRTHTGKNRMDVMNVEKLFVRNHTLLYIR 694
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntpQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 695 ELTPGKSPmnvmnveNPFIRRQIFRSIKVFTRGRNPMNVANVEKPCQKSVLTVHH---RTHTGEKPYECNECGKTFCHKS 771
Cdd:COG5048  192 VSTSIPSS-------SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 772 NLSTHQGTHSG-----------EKPYECDECRKTFYDKTVLTIHQRT--HTGE--KPFECKE--CRKTFSQKSKLFVHHR 834
Cdd:COG5048  265 LPTASSQSSSPnesdsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190014599 835 THTGEKPFRC--NECRKTFSQKS-----GLSIHQRTHTGEKPYEC--KECGKTFCQKSHLSRHQQTHIGEKSD 898
Cdd:COG5048  345 LHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
465-488 5.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|....
gi 190014599  465 NLRLHQRTHTGEKPYECNECGKTF 488
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 812-860 2.63e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 190014599 812 KPFeCKECRKTFSQKSKLFVHHRTHTgekpFRCNECRKTFSQKSGLSIH 860
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 ...
 870-892 3.33e-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: 3.33e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  870 YECKECGKTFCQKSHLSRHQQTH 892
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
22-82 8.23e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.08  E-value: 8.23e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190014599    22 VSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSLGHYITKPEMIFKLEQGAEPWI 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 21-62 1.47e-21

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: 88.30  E-value: 1.47e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 190014599   21 LVSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSLG 62
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 22-61 9.20e-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: 80.29  E-value: 9.20e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 190014599  22 VSFEEVAVHFTWEEWQDLDDAQRTLYRDVMLETYSSLVSL 61
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-689 9.24e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 309 KPYACNWCEKLFSYKSSLIIHQRIHTGEKPYGCN--ECGKTFRRKSFLTLHERTHTGDKPYKC-IECGKTFHCKSLLTLH 385
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 386 HRTHSGEKPYQCSECGKTFSQKSYLTIHHRTHTGEKPYACDHC-------EEAFSHKSRL---------------TVHQR 443
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntPQSNSLHPPLpanslskdpssnlslLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 444 THTGEKPYECNECGKPFINKSNLRLHQRTHTGEKPYECNECGKTFHRKSFLTIHQWTHTGEKPYECNECGKTFRCKSFLT 523
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 524 VHQRTHAGE-------KPYACNECGKTYSHKSYLTVHHRT--HTGE--KPYECNE--CGKSFHCKSFLTIHQRTHAGKKP 590
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 591 YECNECEKTFINKLNLGI-------HKRTHTGERPYEC--NECGKTFRQKSNLSTHQGTHTGEKPYVCN--ECGKTFHRK 659
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410       420       430
                 ....*....|....*....|....*....|
gi 190014599 660 SFLTIHQRTHTGKNRMDVMNVEKLFVRNHT 689
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
364-799 2.24e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 364 DKPYKCIECGKTFHCKSLLTLHHRTHSGEKPYQCS--ECGKTFSQKSYLTIHHRTHTGEK-----------PYACDHCEE 430
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPsdlnskslplsNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 431 AFSHKSRLTVhqrthtgeKPYECNECGKPFINKSNLRLHQRTHTGEKPYE-CNecGKTFHRKSFLTIHQWTHTGekpyec 509
Cdd:COG5048  111 SSSSSNSNDN--------NLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPgNN--SSSVNTPQSNSLHPPLPAN------ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 510 NECGKTFRCKSFLTVHQRTHAGEKPYACNECGKTYSHKSYLTVHHRTHTgEKPYECNECGKSFHC------KSFLTIHQR 583
Cdd:COG5048  175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKsllsqsPSSLSSSDS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 584 THAGKKPYECNECEKTFINKLNLGIHKRTHTGER-PYECNECGKTFRQKSNLSTHQGT--HTGE--KPYVCNE--CGKTF 656
Cdd:COG5048  254 SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 657 HRKSFLTIHQRTHTGKNRmdvmNVEKLFVRNHTllyireltpgKSPMNVMNVENPFIRRQIFRSIKVFTRGRNPMNVANV 736
Cdd:COG5048  334 SRNDALKRHILLHTSISP----AKEKLLNSSSK----------FSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFK 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190014599 737 EKPCQKSvltvHHRTHTGEKPYECN--ECGKTFCHKSNLSTHQGTHSGEKPYECDECRKTFYDKT 799
Cdd:COG5048  400 RDSNLSL----HIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
154-577 2.69e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 154 MKPGQFNDCQNMLFPIKPGETQSGE----KPHVCDITRRSHRHHEHLTQHHKIQTLLQTFQCNEQGKTFN-------TEA 222
Cdd:COG5048    3 LTSSQSSSSNNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSfsrplelSRH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 223 MFFIHKRVHIVQTFGKYNEYEKACNNSAVIVQVITQVGQPTCCRKSDFTK-HQQTHTGEKPYECVECEKPSISKSDLMLQ 301
Cdd:COG5048   83 LRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSrDPQLPDLLSISNLRNNPLPGNNSSSVNTP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 302 CKMPTeEKPYACNWCEKLFSYKSSLIIHQRIHTGEKPYGCNECGKTFRRKSFLTLHERTHTGDKPYKCIECGKTFHCKSL 381
Cdd:COG5048  163 QSNSL-HPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 382 LTLHHRTHSGEKPYQCSECGKTFSQKSYLTIHHRTHTGE-------KPYACDHCEEAFSHKSRLTVHQRT--HTGE--KP 450
Cdd:COG5048  242 SQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 451 YECNE--CGKPFINKSNLRLHQRTHTGEKPYEC--NECGKTFHRKSF-----LTIHQWTHTGEKPYEC--NECGKTFRCK 519
Cdd:COG5048  322 FSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRD 401

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 520 SFLTVHQRTHAGEKPYACN--ECGKTYSHKSYLTVHHRTHTGEKPYECNECGKSFHCKSF 577
Cdd:COG5048  402 SNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
561-898 1.76e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 561 KPYECNECGKSFHCKSFLTIHQRTHAGKKPYECN--ECEKTFINKLNLGIHKRTHTGERPYEC----------------N 622
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 623 ECGKTFRQKSNLSTHQGTHTGEKPYVCNECGKTFHRKSFLTIH--------QRTHTGKNRMDVMNVEKLFVRNHTLLYIR 694
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvntpQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 695 ELTPGKSPmnvmnveNPFIRRQIFRSIKVFTRGRNPMNVANVEKPCQKSVLTVHH---RTHTGEKPYECNECGKTFCHKS 771
Cdd:COG5048  192 VSTSIPSS-------SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 772 NLSTHQGTHSG-----------EKPYECDECRKTFYDKTVLTIHQRT--HTGE--KPFECKE--CRKTFSQKSKLFVHHR 834
Cdd:COG5048  265 LPTASSQSSSPnesdsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190014599 835 THTGEKPFRC--NECRKTFSQKS-----GLSIHQRTHTGEKPYEC--KECGKTFCQKSHLSRHQQTHIGEKSD 898
Cdd:COG5048  345 LHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
465-488 5.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|....
gi 190014599  465 NLRLHQRTHTGEKPYECNECGKTF 488
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
771-855 1.68e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 771 SNLSTHQGTHSGEKPYECDECRKTFYDKTVLTIHQRTHTGEKPFEC--KECRKTFSQKSKLFVHHRTHTGEKPFRCNECR 848
Cdd:COG5048   19 TPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSL 98


                 ....*..
gi 190014599 849 KTFSQKS 855
Cdd:COG5048   99 PLSNSKA 105
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 812-860 2.63e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 190014599 812 KPFeCKECRKTFSQKSKLFVHHRTHTgekpFRCNECRKTFSQKSGLSIH 860
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 ...
 870-892 3.33e-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: 3.33e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  870 YECKECGKTFCQKSHLSRHQQTH 892
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
857-879 3.84e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  857 LSIHQRTHTGEKPYECKECGKTF 879
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
801-825 4.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.07e-03
                          10        20
                  ....*....|....*....|....*
gi 190014599  801 LTIHQRTHTGEKPFECKECRKTFSQ 825
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 391-474 4.21e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014599 391 GEKPYQCS--ECGKTFSQKSYLTiHHRTHtgekpyacDHCEEAFSHKSRLTVHQRTHTGEKPYECNECGKPFINKSNLRL 468
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLK-YHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 190014599 469 HqRTHT 474
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-572 4.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|....
gi 190014599  549 YLTVHHRTHTGEKPYECNECGKSF 572
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 395-417 4.65e-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: 35.35  E-value: 4.65e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  395 YQCSECGKTFSQKSYLTIHHRTH 417
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
354-376 5.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.26e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  354 LTLHERTHTGDKPYKCIECGKTF 376
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 451-473 5.60e-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: 5.60e-03
                          10        20
                  ....*....|....*....|...
gi 190014599  451 YECNECGKPFINKSNLRLHQRTH 473
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-630 5.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.80e-03
                          10        20
                  ....*....|....*....|..
gi 190014599  609 HKRTHTGERPYECNECGKTFRQ 630
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.
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