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Conserved domains on  [gi|1034644757|ref|XP_016864898|]
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zinc finger protein 354C isoform X1 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-72 1.09e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.76  E-value: 1.09e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644757   12 VTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLGIPFSMPKLIHQLQQGEDPCM 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
242-541 1.10e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.95  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 242 KPYKCNECEKTFSHRSSLLSHQRIHTGEKPYKCN--ECEKAFSNSSTLIKHLRVHTGEKPYRC------RECGKAFSQCS 313
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 314 TLTVHQRIHTGEKLYKCGECEK-------AFNCRAKLHRHQRIHTGEKPYKCS----------ECGKGYSQFTSLAEHQR 376
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRdpqlpdlLSISNLRNNPLPGNNSSSVNTPQSnslhpplpanSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 377 FHTGEQLYTCLECGRTFTRIVTLIEHQRIHTGQKPYQCNECEKAFNQYSSFNEHRKIHTGEKLYTCEECGKAFGCKSNLY 456
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 457 RHQRIHTGE-------KPYQCNQCGKAFSQYSFLTEHER--IHTGEKL--YKCME--CGKAYSYRSNLCRHKKVHTKEKL 523
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330
                  ....*....|....*...
gi 1034644757 524 YKWkeygKPFICSSSLTQ 541
Cdd:COG5048   352 AKE----KLLNSSSKFSP 365
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-72 1.09e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.76  E-value: 1.09e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644757   12 VTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLGIPFSMPKLIHQLQQGEDPCM 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 2.98e-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: 92.15  E-value: 2.98e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034644757  11 PVTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-51 1.32e-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: 81.83  E-value: 1.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034644757  12 VTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSL 51
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
242-541 1.10e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.95  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 242 KPYKCNECEKTFSHRSSLLSHQRIHTGEKPYKCN--ECEKAFSNSSTLIKHLRVHTGEKPYRC------RECGKAFSQCS 313
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 314 TLTVHQRIHTGEKLYKCGECEK-------AFNCRAKLHRHQRIHTGEKPYKCS----------ECGKGYSQFTSLAEHQR 376
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRdpqlpdlLSISNLRNNPLPGNNSSSVNTPQSnslhpplpanSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 377 FHTGEQLYTCLECGRTFTRIVTLIEHQRIHTGQKPYQCNECEKAFNQYSSFNEHRKIHTGEKLYTCEECGKAFGCKSNLY 456
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 457 RHQRIHTGE-------KPYQCNQCGKAFSQYSFLTEHER--IHTGEKL--YKCME--CGKAYSYRSNLCRHKKVHTKEKL 523
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330
                  ....*....|....*...
gi 1034644757 524 YKWkeygKPFICSSSLTQ 541
Cdd:COG5048   352 AKE----KLLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.25e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.25e-05
                          10        20
                  ....*....|....*....|....*.
gi 1034644757 454 NLYRHQRIHTGEKPYQCNQCGKAFSQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 242-294 1.67e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 1.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034644757 242 KPYkCNECEKTFSHRSSLLSHQRIHTgekpYKCNECEKAFSNSSTLIKH-LRVH 294
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-72 1.09e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.76  E-value: 1.09e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644757   12 VTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLGIPFSMPKLIHQLQQGEDPCM 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 2.98e-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: 92.15  E-value: 2.98e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034644757  11 PVTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-51 1.32e-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: 81.83  E-value: 1.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034644757  12 VTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSL 51
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
242-541 1.10e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.95  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 242 KPYKCNECEKTFSHRSSLLSHQRIHTGEKPYKCN--ECEKAFSNSSTLIKHLRVHTGEKPYRC------RECGKAFSQCS 313
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 314 TLTVHQRIHTGEKLYKCGECEK-------AFNCRAKLHRHQRIHTGEKPYKCS----------ECGKGYSQFTSLAEHQR 376
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRdpqlpdlLSISNLRNNPLPGNNSSSVNTPQSnslhpplpanSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 377 FHTGEQLYTCLECGRTFTRIVTLIEHQRIHTGQKPYQCNECEKAFNQYSSFNEHRKIHTGEKLYTCEECGKAFGCKSNLY 456
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 457 RHQRIHTGE-------KPYQCNQCGKAFSQYSFLTEHER--IHTGEKL--YKCME--CGKAYSYRSNLCRHKKVHTKEKL 523
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330
                  ....*....|....*...
gi 1034644757 524 YKWkeygKPFICSSSLTQ 541
Cdd:COG5048   352 AKE----KLLNSSSKFSP 365
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
214-538 1.99e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 214 KPHICNECGKSFKQNLHLIEHQRIHTGEKPYKCN--ECEKTFSHRSSLLSHQRIHTGEK-----------PYKCNECEKA 280
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPsdlnskslplsNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 281 FSNSSTLIKHLRVHTGEKP-----------YRCRECGKAFSQCSTLTVHQRIHTGEKLYKCGECEKAFNCRAK-LHRHQR 348
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPssrdpqlpdllSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLsLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 349 IHTGEKPYKCSECGKGYSQFTSLAEHQRFHTGEQLYTCLECGRTFTRIVTLIEHQRIHTGQKPYQCNECEKAFNQYSSFN 428
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 429 EHRKIHTGE-------KLYTCEECGKAFGCKSNLYRHQR--IHTGE--KPYQC--NQCGKAFSQYSFLTEHERIHTGEKL 495
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1034644757 496 YKCMECGKAYSYRSNLcrHKKVHTKEKLYKWKEYGKPFICSSS 538
Cdd:COG5048   352 AKEKLLNSSSKFSPLL--NNEPPQSLQQYKDLKNDKKSETLSN 392
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-346 3.61e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 192 TFGKDFKQNFDLMK----CFQIYPGGKPHICNE--CGKSFKQNLHLIEHQRIHTGEKPYKCNECEKTFSHRSSL------ 259
Cdd:COG5048   294 QCNISFSRSSPLTRhlrsVNHSGESLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppq 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 260 -LSHQRIHTGEKPYKC--NECEKAFSNSSTLIKHLRVHTGEKPYRCR--ECGKAFSQCSTLTVHQRIHTgEKLYKCGECE 334
Cdd:COG5048   374 sLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT-NHAPLLCSIL 452

                         170
                  ....*....|..
gi 1034644757 335 KAFNCRAKLHRH 346
Cdd:COG5048   453 KSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
234-479 4.60e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 234 HQRIHTGEKPYKCNECEKTFSHRSSLLSHQRIHTGEKPYKCNEC------EKAFSNSSTLIKHLRVHTGEKPYRCRECGK 307
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNsqlspkSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 308 AFSQCSTLTVHQRIHTGEKL-YKCGECEKAFNCRAKLHRHQR--IHTGE--KPYKCSE--CGKGYSQFTSLAEHQRFHTG 380
Cdd:COG5048   269 SSQSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 381 EQLYTC--LECGRTFTRIVT-----LIEHQRIHTGQKPYQC--NECEKAFNQYSSFNEHRKIHT--GEKLYTCEECGKAF 449
Cdd:COG5048   349 ISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSF 428

                         250       260       270
                  ....*....|....*....|....*....|
gi 1034644757 450 GCKSNLYRHQRIHTGEKPYQCNQCGKAFSQ 479
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.25e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.25e-05
                          10        20
                  ....*....|....*....|....*.
gi 1034644757 454 NLYRHQRIHTGEKPYQCNQCGKAFSQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
270-430 1.33e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 270 KPYKCNECEKAFSNSSTLIKHLR--VHTGE--KPYRCRE--CGKAFSQCSTLTVHQRIHTGEKLYKC--GECEKAF---- 337
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFspll 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 338 -NCRAKLHRHQRIHTGEKPYKCSecGKGYSQFTSLAEHQRFHT------GEQLYTCLECGRTFTRIVTLIEHQRIHTgQK 410
Cdd:COG5048   368 nNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHIithlsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NH 444

                         170       180
                  ....*....|....*....|
gi 1034644757 411 PYQCNECEKAFNQYSSFNEH 430
Cdd:COG5048   445 APLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
230-255 1.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 1034644757 230 HLIEHQRIHTGEKPYKCNECEKTFSH 255
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
258-283 1.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 1034644757 258 SLLSHQRIHTGEKPYKCNECEKAFSN 283
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
287-311 3.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.56e-04
                          10        20
                  ....*....|....*....|....*
gi 1034644757 287 LIKHLRVHTGEKPYRCRECGKAFSQ 311
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-423 5.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.28e-04
                          10        20
                  ....*....|....*....|....*
gi 1034644757 399 LIEHQRIHTGQKPYQCNECEKAFNQ 423
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
345-367 9.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.60e-04
                          10        20
                  ....*....|....*....|...
gi 1034644757 345 RHQRIHTGEKPYKCSECGKGYSQ 367
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 240-323 1.16e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 240 GEKPYKCN--ECEKTFSHRSSLLSHqRIHtgekpykcNECEKAFSNSSTLIKHLRVHTGEKPYRCRECGKAFSQCSTLTV 317
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1034644757 318 HqRIHT 323
Cdd:COG5189   417 H-RKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 242-294 1.67e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 1.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034644757 242 KPYkCNECEKTFSHRSSLLSHQRIHTgekpYKCNECEKAFSNSSTLIKH-LRVH 294
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 270-322 3.25e-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: 36.77  E-value: 3.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034644757 270 KPYkCNECEKAFSNSSTLIKHLRvhtgEKPYRCRECGKAFSQCSTLTVH-QRIH 322
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 272-294 3.26e-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: 3.26e-03
                          10        20
                  ....*....|....*....|...
gi 1034644757 272 YKCNECEKAFSNSSTLIKHLRVH 294
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 244-266 3.71e-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: 3.71e-03
                          10        20
                  ....*....|....*....|...
gi 1034644757 244 YKCNECEKTFSHRSSLLSHQRIH 266
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-507 6.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.27e-03
                          10        20
                  ....*....|....*....|....*
gi 1034644757 483 LTEHERIHTGEKLYKCMECGKAYSY 507
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 300-322 8.37e-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: 33.81  E-value: 8.37e-03
                          10        20
                  ....*....|....*....|...
gi 1034644757 300 YRCRECGKAFSQCSTLTVHQRIH 322
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
365-491 9.65e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644757 365 YSQFTSLAEHQRFHTGEQLYT----CLECGRTFTRIVTLIEHQRIHTGQKPYQCN--ECEKAFNQYSSFNEHRKIHTGEK 438
Cdd:COG5048    11 SNNSVLSSTPKSTLKSLSNAPrpdsCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNP 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644757 439 LYTCEECG-----KAFGCKSNLYRHQRIhtgeKPYQCNQCGKAFSQYSFLTEHERIHT 491
Cdd:COG5048    91 SDLNSKSLplsnsKASSSSLSSSSSNSN----DNNLLSSHSLPPSSRDPQLPDLLSIS 144
 
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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