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Conserved domains on  [gi|618466999|ref|NP_037388|]
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zinc finger protein 180 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
332-692 1.22e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 332 SETSHSSSLTQNMRNNSEE---KPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECS--ECGKSFSRSSHLVSHQRTHTGE 406
Cdd:COG5048   10 SSNNSVLSSTPKSTLKSLSnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 407 KPYRCNQC-----------------------------GKSFSQSYVLVVHQRTHTGEKPYECNQCGKSFRQSYK------ 451
Cdd:COG5048   90 PSDLNSKSlplsnskasssslsssssnsndnnllsshSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhp 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 452 ----------------LIAHQRTHTGEKPYECNQCGKSFIQSYKLIAHQRIHTGEKPYECNQCGKSFSQSYKLVAHQRTH 515
Cdd:COG5048  170 plpanslskdpssnlsLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 516 TGEKPFECNQCGKSFSWSSQLVAHQRTHTGE-------KPYECSECGKSFNRSSHLVMHQR--IHTGE--KPYEC--NQC 582
Cdd:COG5048  250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLC 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 583 GKSFSQSYVLVVHQRTHTGEKPYECSQCGKSFRQSSCLT-------QHQRTHTGEKPFEC--NQCGKTFSLSARLIVHQR 653
Cdd:COG5048  330 GKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 618466999 654 THTGEKP--FTCIQCGKAFINSYKLIRHQATHTEEKLYECN 692
Cdd:COG5048  410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 72-112 2.25e-14

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: 67.50  E-value: 2.25e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 618466999   72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSWD 112
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
332-692 1.22e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 332 SETSHSSSLTQNMRNNSEE---KPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECS--ECGKSFSRSSHLVSHQRTHTGE 406
Cdd:COG5048   10 SSNNSVLSSTPKSTLKSLSnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 407 KPYRCNQC-----------------------------GKSFSQSYVLVVHQRTHTGEKPYECNQCGKSFRQSYK------ 451
Cdd:COG5048   90 PSDLNSKSlplsnskasssslsssssnsndnnllsshSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhp 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 452 ----------------LIAHQRTHTGEKPYECNQCGKSFIQSYKLIAHQRIHTGEKPYECNQCGKSFSQSYKLVAHQRTH 515
Cdd:COG5048  170 plpanslskdpssnlsLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 516 TGEKPFECNQCGKSFSWSSQLVAHQRTHTGE-------KPYECSECGKSFNRSSHLVMHQR--IHTGE--KPYEC--NQC 582
Cdd:COG5048  250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLC 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 583 GKSFSQSYVLVVHQRTHTGEKPYECSQCGKSFRQSSCLT-------QHQRTHTGEKPFEC--NQCGKTFSLSARLIVHQR 653
Cdd:COG5048  330 GKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 618466999 654 THTGEKP--FTCIQCGKAFINSYKLIRHQATHTEEKLYECN 692
Cdd:COG5048  410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 72-112 2.25e-14

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: 67.50  E-value: 2.25e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 618466999   72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSWD 112
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 72-111 1.56e-11

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: 59.10  E-value: 1.56e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 618466999  72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSW 111
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB smart00349
krueppel associated box;
72-133 1.01e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 57.60  E-value: 1.01e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618466999    72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSwdLATAVGKKDSTSKQRIfDEEP 133
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVS--LGFQVPKPDLISQLEQ-GEEP 59
zf-H2C2_2 pfam13465
Zinc-finger double domain;
395-420 4.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 618466999  395 HLVSHQRTHTGEKPYRCNQCGKSFSQ 420
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 379-427 2.83e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.15  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 618466999 379 KPYeCSECGKSFSRSSHLVSHQRTHTgekpYRCNQCGKSFSQSYVLVVH 427
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
332-692 1.22e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 332 SETSHSSSLTQNMRNNSEE---KPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECS--ECGKSFSRSSHLVSHQRTHTGE 406
Cdd:COG5048   10 SSNNSVLSSTPKSTLKSLSnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 407 KPYRCNQC-----------------------------GKSFSQSYVLVVHQRTHTGEKPYECNQCGKSFRQSYK------ 451
Cdd:COG5048   90 PSDLNSKSlplsnskasssslsssssnsndnnllsshSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhp 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 452 ----------------LIAHQRTHTGEKPYECNQCGKSFIQSYKLIAHQRIHTGEKPYECNQCGKSFSQSYKLVAHQRTH 515
Cdd:COG5048  170 plpanslskdpssnlsLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 516 TGEKPFECNQCGKSFSWSSQLVAHQRTHTGE-------KPYECSECGKSFNRSSHLVMHQR--IHTGE--KPYEC--NQC 582
Cdd:COG5048  250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLC 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 583 GKSFSQSYVLVVHQRTHTGEKPYECSQCGKSFRQSSCLT-------QHQRTHTGEKPFEC--NQCGKTFSLSARLIVHQR 653
Cdd:COG5048  330 GKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 618466999 654 THTGEKP--FTCIQCGKAFINSYKLIRHQATHTEEKLYECN 692
Cdd:COG5048  410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 72-112 2.25e-14

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: 67.50  E-value: 2.25e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 618466999   72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSWD 112
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 72-111 1.56e-11

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: 59.10  E-value: 1.56e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 618466999  72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSW 111
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
236-645 9.32e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 9.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 236 HQKINENETLYENNEC-GKPPQSIHLIQFTRTQTKDKSYG--FSDRIQSFCHGTPLHIHEKIHGGGKTFDFKECGQVLNP 312
Cdd:COG5048   24 LKSLSNAPRPDSCPNCtDSFSRLEHLTRHIRSHTGEKPSQcsYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 313 KISHNEQQRIPFEeSQYKCSETSHSSSLTQNMRNNSEEKP---FECNQCGKSFSWSSHLVAHQRTHtGEKPYECSECGKS 389
Cdd:COG5048  104 KASSSSLSSSSSN-SNDNNLLSSHSLPPSSRDPQLPDLLSisnLRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 390 FSRSSHLvsHQRTHTGEKPYRCNQCGKSFSQSYVLVVHQRTHTGEKPYECNQCgkSFRQSYKLIAHQRTHTGeKPYECNQ 469
Cdd:COG5048  182 SNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLS-SSDSSSS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 470 CGKSFIQSYKLIAHQRIH----------TGEKPYECNQCGKSFSQSYKLVAHQRT--HTGE--KPFEC--NQCGKSFSWS 533
Cdd:COG5048  257 ASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRN 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 534 SQLVAHQRTHTGEKPYEC--SECGKSFNRSSH-----LVMHQRIHTGEKPYEC--NQCGKSFSQSYVLVVHQRTHTGEKP 604
Cdd:COG5048  337 DALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP 416

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 618466999 605 YEC--SQCGKSFRQSSCLTQHQRTHTGEKPFECNQCGKTFSLS 645
Cdd:COG5048  417 YNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
KRAB smart00349
krueppel associated box;
72-133 1.01e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 57.60  E-value: 1.01e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618466999    72 VNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSwdLATAVGKKDSTSKQRIfDEEP 133
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVS--LGFQVPKPDLISQLEQ-GEEP 59
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
234-619 1.19e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 234 NSHQKINENETLYENNECGKPPQSIHLIQFTRTQTKDKSYGFSDRIQSFCHGTPLHIHEKIHGGGKTFDFKECGQVLNPK 313
Cdd:COG5048   50 TRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 314 ISHNEQQRIPFE--ESQYKCSETSHSSSLTQNMRNNSEEKPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECSECGKSFS 391
Cdd:COG5048  130 PSSRDPQLPDLLsiSNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSY 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 392 RSSHLVSHQRTHTGEKPYRCNQCGKSFSQSYVLVVHQRTHtgeKPYECNQCGKSFRQSYKLIAHQRTH----------TG 461
Cdd:COG5048  210 SIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS---SSDSSSSASESPRSSLPTASSQSSSpnesdsssekGF 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 462 EKPYECNQCGKSFIQSYKLIAHQR--IHTGE--KPYEC--NQCGKSFSQSYKLVAHQRTHTGEKPFEC--NQCGKSFS-- 531
Cdd:COG5048  287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpl 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618466999 532 ---WSSQLVAHQRTHTGEKPYEC--SECGKSFNRSSHLVMHQRIHTGEKPYECN--QCGKSFSQSYVLVVHQRTHTGEKP 604
Cdd:COG5048  367 lnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAP 446

                        410
                 ....*....|....*
gi 618466999 605 YECSQCGKSFRQSSC 619
Cdd:COG5048  447 LLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
395-420 4.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 618466999  395 HLVSHQRTHTGEKPYRCNQCGKSFSQ 420
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
563-588 5.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.65e-05
                          10        20
                  ....*....|....*....|....*.
gi 618466999  563 HLVMHQRIHTGEKPYECNQCGKSFSQ 588
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-392 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 618466999  367 HLVAHQRTHTGEKPYECSECGKSFSR 392
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-448 2.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|....*
gi 618466999  424 LVVHQRTHTGEKPYECNQCGKSFRQ 448
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-560 2.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.51e-04
                          10        20
                  ....*....|....*....|....*
gi 618466999  536 LVAHQRTHTGEKPYECSECGKSFNR 560
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-616 2.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|....*
gi 618466999  592 LVVHQRTHTGEKPYECSQCGKSFRQ 616
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
620-643 2.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.88e-04
                          10        20
                  ....*....|....*....|....
gi 618466999  620 LTQHQRTHTGEKPFECNQCGKTFS 643
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 381-403 3.60e-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: 38.05  E-value: 3.60e-04
                          10        20
                  ....*....|....*....|...
gi 618466999  381 YECSECGKSFSRSSHLVSHQRTH 403
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-504 3.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.98e-04
                          10        20
                  ....*....|....*....|..
gi 618466999  483 HQRIHTGEKPYECNQCGKSFSQ 504
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
455-476 5.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|..
gi 618466999  455 HQRTHTGEKPYECNQCGKSFIQ 476
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-531 7.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.17e-04
                          10        20
                  ....*....|....*....|....
gi 618466999  508 LVAHQRTHTGEKPFECNQCGKSFS 531
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
647-672 9.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 618466999  647 RLIVHQRTHTGEKPFTCIQCGKAFIN 672
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 549-571 1.60e-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: 36.12  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|...
gi 618466999  549 YECSECGKSFNRSSHLVMHQRIH 571
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 1.80e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|...
gi 618466999  437 YECNQCGKSFRQSYKLIAHQRTH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 605-627 1.80e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|...
gi 618466999  605 YECSQCGKSFRQSSCLTQHQRTH 627
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 379-427 2.83e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.15  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 618466999 379 KPYeCSECGKSFSRSSHLVSHQRTHTgekpYRCNQCGKSFSQSYVLVVH 427
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 ...
 493-515 2.91e-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: 35.35  E-value: 2.91e-03
                          10        20
                  ....*....|....*....|...
gi 618466999  493 YECNQCGKSFSQSYKLVAHQRTH 515
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 519-571 5.62e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 5.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 618466999 519 KPFeCNQCGKSFSWSSQLVAHQRTHTgekpYECSECGKSFNRSSHLVMH-QRIH 571
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 465-487 6.76e-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: 6.76e-03
                          10        20
                  ....*....|....*....|...
gi 618466999  465 YECNQCGKSFIQSYKLIAHQRIH 487
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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