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Conserved domains on  [gi|1720426971|ref|XP_030099278|]
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zinc finger protein 1 isoform X1 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

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
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-47 9.03e-23

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


:

Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.84  E-value: 9.03e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720426971   7 SVSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSV 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
175-336 2.14e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 175 KIKSLVQPFVCNYCDKTFSFKSLLVSHKR--IHTGE--KPYECDV--CQKTFSHKANLIKHQRIHTGEKPFECP--ECGK 246
Cdd:COG5048   282 SEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSS 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 247 AFTHQSNLIVHQRAHMEK-----KPYGC--SECGKTFAQKFELTTHQRIHTGERPYECN--ECAKTFFKKSNLIIHQKIH 317
Cdd:COG5048   362 KFSPLLNNEPPQSLQQYKdlkndKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIH 441
                         170
                  ....*....|....*....
gi 1720426971 318 TGEKRYECSECGKSFIQNS 336
Cdd:COG5048   442 TNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-390 2.82e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.82e-05
                          10        20
                  ....*....|....*....|....*
gi 1720426971 366 LRLHLRIHTGEKPYECAECGKAFSR 390
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-362 2.37e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.37e-04
                          10        20
                  ....*....|....*....|..
gi 1720426971 341 HRRTHTGEKPYECTECGKTFSQ 362
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-47 9.03e-23

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.84  E-value: 9.03e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720426971   7 SVSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSV 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
8-48 1.76e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 1.76e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720426971    8 VSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSVE 48
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 9.24e-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: 78.75  E-value: 9.24e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720426971   8 VSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
175-336 2.14e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 175 KIKSLVQPFVCNYCDKTFSFKSLLVSHKR--IHTGE--KPYECDV--CQKTFSHKANLIKHQRIHTGEKPFECP--ECGK 246
Cdd:COG5048   282 SEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSS 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 247 AFTHQSNLIVHQRAHMEK-----KPYGC--SECGKTFAQKFELTTHQRIHTGERPYECN--ECAKTFFKKSNLIIHQKIH 317
Cdd:COG5048   362 KFSPLLNNEPPQSLQQYKdlkndKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIH 441
                         170
                  ....*....|....*....
gi 1720426971 318 TGEKRYECSECGKSFIQNS 336
Cdd:COG5048   442 TNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
225-250 5.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 5.83e-06
                          10        20
                  ....*....|....*....|....*.
gi 1720426971 225 NLIKHQRIHTGEKPFECPECGKAFTH 250
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-390 2.82e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.82e-05
                          10        20
                  ....*....|....*....|....*
gi 1720426971 366 LRLHLRIHTGEKPYECAECGKAFSR 390
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-362 2.37e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.37e-04
                          10        20
                  ....*....|....*....|..
gi 1720426971 341 HRRTHTGEKPYECTECGKTFSQ 362
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-382 7.34e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 7.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426971 323 YECSECGKSFIQNSQLIIHRRTHTGEKPYECT--ECGKTFSQRSTLRLHLRIHTGEKPYECA 382
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
PHA00733 PHA00733
hypothetical protein
210-257 2.92e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720426971 210 PYECDVCQKTFSHKANLIKHQRIHTGEKpfECPECGKAFTHQSNLIVH 257
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
209-264 3.22e-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: 3.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426971 209 KPYeCDVCQKTFSHKANLIKHQRIHTgekpFECPECGKAFTHQSNLIVH-QRAHMEK 264
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-47 9.03e-23

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.84  E-value: 9.03e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720426971   7 SVSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSV 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
8-48 1.76e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 1.76e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720426971    8 VSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSVE 48
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 9.24e-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: 78.75  E-value: 9.24e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720426971   8 VSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
175-336 2.14e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 175 KIKSLVQPFVCNYCDKTFSFKSLLVSHKR--IHTGE--KPYECDV--CQKTFSHKANLIKHQRIHTGEKPFECP--ECGK 246
Cdd:COG5048   282 SEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSS 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 247 AFTHQSNLIVHQRAHMEK-----KPYGC--SECGKTFAQKFELTTHQRIHTGERPYECN--ECAKTFFKKSNLIIHQKIH 317
Cdd:COG5048   362 KFSPLLNNEPPQSLQQYKdlkndKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIH 441
                         170
                  ....*....|....*....
gi 1720426971 318 TGEKRYECSECGKSFIQNS 336
Cdd:COG5048   442 TNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-401 2.70e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 192 FSFKSLLVSHKRIHTGEKPYECDVCQKTFSHKANLIKHQRIHTGEKPFECPEC-----GKAFTHQSNlivHQRAHMEK-- 264
Cdd:COG5048   208 SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTASSQSSS---PNESDSSSek 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 265 ---KPYGCSECGKTFAQKFELTTHQR--IHTGE--RPYECNE--CAKTFFKKSNLIIHQKIHTGEKRYEC--SECGKSFI 333
Cdd:COG5048   285 gfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFS 364
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426971 334 QNS-----QLIIHRRTHTGEKPYECT--ECGKTFSQRSTLRLHLRIHTGEKPYEC--AECGKAFSRKSRLSVHQRVH 401
Cdd:COG5048   365 PLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
225-250 5.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 5.83e-06
                          10        20
                  ....*....|....*....|....*.
gi 1720426971 225 NLIKHQRIHTGEKPFECPECGKAFTH 250
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-390 2.82e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.82e-05
                          10        20
                  ....*....|....*....|....*
gi 1720426971 366 LRLHLRIHTGEKPYECAECGKAFSR 390
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-270 3.91e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 3.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426971 209 KPYECDVCQKTFSHKANLIKHQRIHTGEKPFEC--PECGKAFTHQSNLIVHQRAHMEKKPYGCS 270
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-402 4.30e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 217 QKTFSHKANLIKHQRIHTGEKPFECPECGKAFTHQSNLIVHQRAHMEKKPYGCSECGKTFAQKFELTTHQRIHTGERPYE 296
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSS 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 297 CNECAKTFFKKSNLIIHQKIHTGE-------KRYECSECGKSFIQNSQLIIHRRT--HTGE--KPYECTE--CGKTFSQR 363
Cdd:COG5048   257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720426971 364 STLRLHLRIHTGEKPYEC--AECGKAFSRKSRLSVHQRVHM 402
Cdd:COG5048   337 DALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQ 377
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-398 5.85e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 196 SLLVSHKRIHTgekPYECDVCQKTFSHKANLIKHQR--IHTGE--KPFECPE--CGKAFTHQSNLIVHQRAHMEKKPYGC 269
Cdd:COG5048   278 SDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 270 --SECGKTFAQKFELTTHQRIHtgerpyecnecaktffkksnliiHQKIHTGEKRYEC--SECGKSFIQNSQLIIHRRTH 345
Cdd:COG5048   355 klLNSSSKFSPLLNNEPPQSLQ-----------------------QYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITH 411
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426971 346 TGEKPYECT--ECGKTFSQRSTLRLHLRIHTGEKPYECAECGKAFSRKSRLSVHQ 398
Cdd:COG5048   412 LSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
198-222 9.15e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.15e-05
                          10        20
                  ....*....|....*....|....*
gi 1720426971 198 LVSHKRIHTGEKPYECDVCQKTFSH 222
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-362 2.37e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.37e-04
                          10        20
                  ....*....|....*....|..
gi 1720426971 341 HRRTHTGEKPYECTECGKTFSQ 362
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
239-261 3.72e-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: 37.28  E-value: 3.72e-04
                          10        20
                  ....*....|....*....|...
gi 1720426971 239 FECPECGKAFTHQSNLIVHQRAH 261
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
309-334 4.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 4.85e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720426971 309 NLIIHQKIHTGEKRYECSECGKSFIQ 334
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
351-373 5.24e-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: 36.89  E-value: 5.24e-04
                          10        20
                  ....*....|....*....|...
gi 1720426971 351 YECTECGKTFSQRSTLRLHLRIH 373
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
323-345 5.89e-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: 36.89  E-value: 5.89e-04
                          10        20
                  ....*....|....*....|...
gi 1720426971 323 YECSECGKSFIQNSQLIIHRRTH 345
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
211-233 6.07e-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: 36.89  E-value: 6.07e-04
                          10        20
                  ....*....|....*....|...
gi 1720426971 211 YECDVCQKTFSHKANLIKHQRIH 233
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-382 7.34e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 7.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426971 323 YECSECGKSFIQNSQLIIHRRTHTGEKPYECT--ECGKTFSQRSTLRLHLRIHTGEKPYECA 382
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-353 8.15e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 8.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426971 293 RPYECNECAKTFFKKSNLIIHQKIHTGEKRYECS--ECGKSFIQNSQLIIHRRTHTGEKPYEC 353
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN 94
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
182-241 9.29e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 9.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426971 182 PFVCNYCDKTFSFKSLLVSHKRIHTGEKPYECDV--CQKTFSHKANLIKHQRIHTGEKPFEC 241
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLN 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
281-304 1.84e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.84e-03
                          10        20
                  ....*....|....*....|....
gi 1720426971 281 ELTTHQRIHTGERPYECNECAKTF 304
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
264-326 2.79e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 2.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426971 264 KKPYGCSECGKTFAQKFELTTHQRIHTGERPYECN--ECAKTFFKKSNLIIHQKIHTGEKRYECS 326
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
PHA00733 PHA00733
hypothetical protein
210-257 2.92e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720426971 210 PYECDVCQKTFSHKANLIKHQRIHTGEKpfECPECGKAFTHQSNLIVH 257
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
209-264 3.22e-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: 3.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426971 209 KPYeCDVCQKTFSHKANLIKHQRIHTgekpFECPECGKAFTHQSNLIVH-QRAHMEK 264
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
379-401 5.41e-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: 34.20  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|...
gi 1720426971 379 YECAECGKAFSRKSRLSVHQRVH 401
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-402 5.42e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 5.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426971 349 KPYECTECGKTFSQRSTLRLHLRIHTGEKPYECA--ECGKAFSRKSRLSVHQRVHM 402
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
183-205 5.74e-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: 34.20  E-value: 5.74e-03
                          10        20
                  ....*....|....*....|...
gi 1720426971 183 FVCNYCDKTFSFKSLLVSHKRIH 205
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
237-346 5.76e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 237 KPFECPECGKAFTHQSNLIVHQRAHMEKKPYGCSECGKTFAQKF--ELTTHQRIHTGERPYECN-ECAKTFFKKSNLIIH 313
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720426971 314 QKIHTGEKRYECSECGKSFIQNSQLIIHRRTHT 346
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS 144
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
157-278 6.98e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426971 157 YNGNGRALSHKDAIFKHRKIKSLVQPFVCNYCDKTFSFKSLL-------VSHKRIHTGEKPYECDV--CQKTFSHKANLI 227
Cdd:COG5048   326 YSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETLSnsCIRNFKRDSNLS 405
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720426971 228 KHQRIHTGEKP--FECPECGKAFTHQSNLIVHQRAHMEKKPYGCSECGKTFAQ 278
Cdd:COG5048   406 LHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
 
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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