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Conserved domains on  [gi|55769568|ref|NP_001007095|]
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zinc finger protein 37A isoform a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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 smart00349
krueppel associated box;
8-68 4.10e-37

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 4.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769568      8 VSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVSVGYCIPKPEVILKLEKGEEPWI 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-421 2.83e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 269 KPYECHECGKTFTQKSAHTRHQRT--HTG--GKPYECHE--CGKTFYKNSDLIKHQRIHTGERPYGCH--ECGKSFSEKS 340
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 341 T-----LTQHQRTHTGEKPYEC--HECGKTFSFKSVLTVHQKTHTGEKPYECY--ACGKAFLRKSDLIKHQRIHTGEKPY 411
Cdd:COG5048 368 NneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|
gi 55769568 412 ECNECGKSFS 421
Cdd:COG5048 448 LCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-448 1.24e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 55769568   426 LTKHLRTHTGEKPYECIQCGKFF 448
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-532 5.70e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.70e-03
                          10        20
                  ....*....|....*....|
gi 55769568   513 HHRTHTGEKPYECNVCGKSF 532
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
492-552 7.06e-03

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 7.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55769568 492 QKPYGCNQCGKSFCVKSKLIAHHRTHTGEKPYECNV--CGKSFYVKSKLTVHQRIHLGRNPIN 552
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL 93
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 4.10e-37

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 4.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769568      8 VSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVSVGYCIPKPEVILKLEKGEEPWI 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 2.03e-24

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: 95.62  E-value: 2.03e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55769568     7 SVSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 4.93e-20

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: 82.98  E-value: 4.93e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55769568   8 VSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVS 46
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-421 2.83e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 269 KPYECHECGKTFTQKSAHTRHQRT--HTG--GKPYECHE--CGKTFYKNSDLIKHQRIHTGERPYGCH--ECGKSFSEKS 340
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 341 T-----LTQHQRTHTGEKPYEC--HECGKTFSFKSVLTVHQKTHTGEKPYECY--ACGKAFLRKSDLIKHQRIHTGEKPY 411
Cdd:COG5048 368 NneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|
gi 55769568 412 ECNECGKSFS 421
Cdd:COG5048 448 LCSILKSFRR 457
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 325-373 2.43e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 55769568 325 RPYgCHECGKSFSEKSTLTQHQRTHTgekpYECHECGKTFSFKSVLTVH 373
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-365 4.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.10e-04
                          10        20
                  ....*....|....*....|....
gi 55769568   342 LTQHQRTHTGEKPYECHECGKTFS 365
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-448 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 55769568   426 LTKHLRTHTGEKPYECIQCGKFF 448
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-532 5.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.70e-03
                          10        20
                  ....*....|....*....|
gi 55769568   513 HHRTHTGEKPYECNVCGKSF 532
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
492-552 7.06e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 7.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55769568 492 QKPYGCNQCGKSFCVKSKLIAHHRTHTGEKPYECNV--CGKSFYVKSKLTVHQRIHLGRNPIN 552
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL 93
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 4.10e-37

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 4.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769568      8 VSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVSVGYCIPKPEVILKLEKGEEPWI 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 2.03e-24

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: 95.62  E-value: 2.03e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55769568     7 SVSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 4.93e-20

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: 82.98  E-value: 4.93e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55769568   8 VSFRDVTVGFTQEEWQHLDPAQRTLYRDVMLENYSHLVS 46
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-421 2.83e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 269 KPYECHECGKTFTQKSAHTRHQRT--HTG--GKPYECHE--CGKTFYKNSDLIKHQRIHTGERPYGCH--ECGKSFSEKS 340
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 341 T-----LTQHQRTHTGEKPYEC--HECGKTFSFKSVLTVHQKTHTGEKPYECY--ACGKAFLRKSDLIKHQRIHTGEKPY 411
Cdd:COG5048 368 NneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|
gi 55769568 412 ECNECGKSFS 421
Cdd:COG5048 448 LCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
185-448 1.57e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 185 MSFFITHQQTHPRENHYGNECGENIFEESILLEHQSVYPFSQklnltPIQRTHSINNIIEYNECGTFFSEKLVLHLQQRT 264
Cdd:COG5048 174 NSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS-----SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSL 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 265 HTGEKPYECHECGKTFTQKSAHTRHQRTHTG-------GKPYECHECGKTFYKNSDLIKHQR--IHTGE--RPYGCHE-- 331
Cdd:COG5048 249 SSSDSSSSASESPRSSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 332 CGKSFSEKSTLTQHQRTHTGEKPYECHECGKTFSFKSVLT-------VHQKTHTGEKPYEC--YACGKAFLRKSDLIKHQ 402
Cdd:COG5048 329 CGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 55769568 403 RIHTGEKPYECN--ECGKSFSEKSTLTKHLRTHTGEKPYECIQCGKFF 448
Cdd:COG5048 409 ITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
145-561 2.16e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 145 SFEYNECGKAFPENSLFLVHKRGYTGQKT--CKYTEHGKT-CDMSFFITHQQTHPRENHYGNE----------CGENIFE 211
Cdd:COG5048  33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPsqCSYSGCDKSfSRPLELSRHLRTHHNNPSDLNSkslplsnskaSSSSLSS 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 212 ES-----ILLEHQSVYPFSQKLNLTPIQRTHSINNIIEYNECGTFFSE-KLVLHLQQRTHTgekpyecHECGKTFTQKSA 285
Cdd:COG5048 113 SSsnsndNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPLPA-------NSLSKDPSSNLS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 286 HTRHQRTHTGGKPYECHECGKTFYKNSDLIKHQRIHTGERPYGCHECGKSFSEKSTLTQHQRTHTGEKPYECHECGKTFS 365
Cdd:COG5048 186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 366 FKSVLTVHQKTHTGE-------KPYECYACGKAFLRKSDLIKHQR--IHTGE--KPYECNE--CGKSFSEKSTLTKHLRT 432
Cdd:COG5048 266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 433 HTGEKPyeciqcgkffcyysgFTEHLRRHTGEKPFGCNECGKTFRQKsalivHQRTHIRQKPYGCNQCGKSFCVKSKLIA 512
Cdd:COG5048 346 HTSISP---------------AKEKLLNSSSKFSPLLNNEPPQSLQQ-----YKDLKNDKKSETLSNSCIRNFKRDSNLS 405

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 55769568 513 HHR-THTGEKPYECN--VCGKSFYVKSKLTVHQRIHLGRNPINVVNEGNYSG 561
Cdd:COG5048 406 LHIiTHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-556 7.93e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 7.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 269 KPYECHECGKTFTQKSAHTRHQRTHTGGKPYECH--ECGKTFYKNSDLIKHQRIHTGERPYGC----------------H 330
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 331 ECGKSFSEKSTLTQHQRTHTGEKPYECHECGKTFSFKSVLTVHQKTHTGEK-------PYECYACGKAFLRKSDLIKHQR 403
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpPLPANSLSKDPSSNLSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 404 IHTGEKPYECNECGKSFSEKSTLTKHLRTHTGEKPYECIQCGKFF------CYYSGFTEHLRRHTGEKPFGCNECGKTFR 477
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 478 QKSALIVHQRTHIRQ-KPYGCNQCGKSFCVKSKLIAHHRT--HTGE--KPYECNV--CGKSFYVKSKLTVHQRIHLGRNP 550
Cdd:COG5048 272 SSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351


                ....*.
gi 55769568 551 INVVNE 556
Cdd:COG5048 352 AKEKLL 357
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 325-373 2.43e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 55769568 325 RPYgCHECGKSFSEKSTLTQHQRTHTgekpYECHECGKTFSFKSVLTVH 373
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-365 4.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.10e-04
                          10        20
                  ....*....|....*....|....
gi 55769568   342 LTQHQRTHTGEKPYECHECGKTFS 365
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
397-421 4.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.94e-04
                          10        20
                  ....*....|....*....|....*
gi 55769568   397 DLIKHQRIHTGEKPYECNECGKSFS 421
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-448 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 55769568   426 LTKHLRTHTGEKPYECIQCGKFF 448
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 411-433 2.21e-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: 2.21e-03
                          10        20
                  ....*....|....*....|...
gi 55769568   411 YECNECGKSFSEKSTLTKHLRTH 433
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 299-321 3.24e-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: 3.24e-03
                          10        20
                  ....*....|....*....|...
gi 55769568   299 YECHECGKTFYKNSDLIKHQRIH 321
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-394 3.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.38e-03
                          10        20
                  ....*....|....*....|....*
gi 55769568   370 LTVHQKTHTGEKPYECYACGKAFLR 394
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-308 3.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.45e-03
                          10        20
                  ....*....|....*....|.
gi 55769568   288 RHQRTHTGGKPYECHECGKTF 308
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 275-378 4.58e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 4.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769568 275 ECGKTFTQKSAH---------TRHQRThTGGKPYECH--ECGKTfYKNSDLIKHQRIHTgerpygchECGKSFSEKSTLT 343
Cdd:COG5189 318 CTNSSSNGKLAHggernidtpSRMLKV-KDGKPYKCPveGCNKK-YKNQNGLKYHMLHG--------HQNQKLHENPSPE 387

                        90       100       110
                ....*....|....*....|....*....|....*
gi 55769568 344 QHQRTHTGEKPYECHECGKTFSFKSVLTVHQKTHT 378
Cdd:COG5189 388 KMNIFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-532 5.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.70e-03
                          10        20
                  ....*....|....*....|
gi 55769568   513 HHRTHTGEKPYECNVCGKSF 532
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
492-552 7.06e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 7.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55769568 492 QKPYGCNQCGKSFCVKSKLIAHHRTHTGEKPYECNV--CGKSFYVKSKLTVHQRIHLGRNPIN 552
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL 93
 
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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