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Conserved domains on  [gi|157819833|ref|NP_001100478|]
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zinc finger protein 287 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
46-144 5.45e-48

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 165.17  E-value: 5.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833    46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90
                   ....*....|....*....
gi 157819833   126 DLAQILEEEAPQNSALPQE 144
Cdd:smart00431  82 DLERELDEPGQQVSAHVHG 100
KRAB smart00349
krueppel associated box;
168-225 9.70e-20

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 9.70e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819833   168 VTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSLGLTVYRPTVIPILE---EPWM 225
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqgeEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
420-752 1.33e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 420 KPYECHQCGKAFSQRAHLTIHQRIHTGEKPYKCNDCGKD--FSQRAHLTIHQRTHTGEKPYKC--LECSKTFSHSSSLIN 495
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 496 HQRVHT------------GEKPYI------------------CNECGKTFSQSTHL-LQHQKIHTGKKPYKCN------- 537
Cdd:COG5048  112 SSSSNSndnnllsshslpPSSRDPqlpdllsisnlrnnplpgNNSSSVNTPQSNSLhPPLPANSLSKDPSSNLsllissn 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 538 ---------ECWKVFSQSTY--LIRHQRIHSGEKCYKCTECGKAFAHSSTLIQHQTTHTGEKSYICNVCGKAFSQSANLT 606
Cdd:COG5048  192 vstsipsssENSPLSSSYSIpsSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 607 QHHRTHTGE-------KPYKCSVCGKAFSQSVHLTQHQR--IHNGE--KPFKC--NTCGKAYRQGANLTQHQRVHTGEKP 673
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 674 YKCHHCGKAFIYSSSLN-------QHRRTHTGERPYKCTH--CNKDFSQRTCLIQHQRIHTGERPYGCR--ICGKSFTQS 742
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410
                 ....*....|
gi 157819833 743 TNLIQHQRVH 752
Cdd:COG5048  432 YNLIPHKKIH 441
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 328-417 2.68e-04

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 328 FDTQSDSKTllynESKPTFTNVSSGGVVHG-----------KILPGDKPYSCNV--CGKKFR-----KYPSLLAHRNNH- 388
Cdd:COG5189  305 ISTGEMIDV----RKLPCTNSSSNGKLAHGgernidtpsrmLKVKDGKPYKCPVegCNKKYKnqnglKYHMLHGHQNQKl 380

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157819833 389 -------------AKDKSYECEECGKEFKHLSSLIAHqRMHT 417
Cdd:COG5189  381 henpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
46-144 5.45e-48

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 165.17  E-value: 5.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833    46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90
                   ....*....|....*....
gi 157819833   126 DLAQILEEEAPQNSALPQE 144
Cdd:smart00431  82 DLERELDEPGQQVSAHVHG 100
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-133 1.01e-45

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.04  E-value: 1.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833   46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 157819833  126 DLAQILEE 133
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 46-129 3.52e-38

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 136.62  E-value: 3.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833  46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 157819833 126 DLAQ 129
Cdd:cd07936   82 DLLA 85
KRAB smart00349
krueppel associated box;
168-225 9.70e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 9.70e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819833   168 VTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSLGLTVYRPTVIPILE---EPWM 225
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqgeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 167-208 4.73e-16

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: 72.12  E-value: 4.73e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 157819833  167 SVTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSLG 208
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 168-207 9.73e-14

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: 65.65  E-value: 9.73e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157819833 168 VTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSL 207
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
420-752 1.33e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 420 KPYECHQCGKAFSQRAHLTIHQRIHTGEKPYKCNDCGKD--FSQRAHLTIHQRTHTGEKPYKC--LECSKTFSHSSSLIN 495
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 496 HQRVHT------------GEKPYI------------------CNECGKTFSQSTHL-LQHQKIHTGKKPYKCN------- 537
Cdd:COG5048  112 SSSSNSndnnllsshslpPSSRDPqlpdllsisnlrnnplpgNNSSSVNTPQSNSLhPPLPANSLSKDPSSNLsllissn 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 538 ---------ECWKVFSQSTY--LIRHQRIHSGEKCYKCTECGKAFAHSSTLIQHQTTHTGEKSYICNVCGKAFSQSANLT 606
Cdd:COG5048  192 vstsipsssENSPLSSSYSIpsSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 607 QHHRTHTGE-------KPYKCSVCGKAFSQSVHLTQHQR--IHNGE--KPFKC--NTCGKAYRQGANLTQHQRVHTGEKP 673
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 674 YKCHHCGKAFIYSSSLN-------QHRRTHTGERPYKCTH--CNKDFSQRTCLIQHQRIHTGERPYGCR--ICGKSFTQS 742
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410
                 ....*....|
gi 157819833 743 TNLIQHQRVH 752
Cdd:COG5048  432 YNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
604-629 2.92e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.92e-05
                          10        20
                  ....*....|....*....|....*.
gi 157819833  604 NLTQHHRTHTGEKPYKCSVCGKAFSQ 629
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 328-417 2.68e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 328 FDTQSDSKTllynESKPTFTNVSSGGVVHG-----------KILPGDKPYSCNV--CGKKFR-----KYPSLLAHRNNH- 388
Cdd:COG5189  305 ISTGEMIDV----RKLPCTNSSSNGKLAHGgernidtpsrmLKVKDGKPYKCPVegCNKKYKnqnglKYHMLHGHQNQKl 380

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157819833 389 -------------AKDKSYECEECGKEFKHLSSLIAHqRMHT 417
Cdd:COG5189  381 henpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 399-444 2.98e-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: 40.23  E-value: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157819833 399 CGKEFKHLSSLIAHQRMHTgekpYECHQCGKAFSQRAHLTIH-QRIH 444
Cdd:cd20908    7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 2.38e-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: 2.38e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  394 YECEECGKEFKHLSSLIAHQRMH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
46-144 5.45e-48

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 165.17  E-value: 5.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833    46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90
                   ....*....|....*....
gi 157819833   126 DLAQILEEEAPQNSALPQE 144
Cdd:smart00431  82 DLERELDEPGQQVSAHVHG 100
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-133 1.01e-45

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.04  E-value: 1.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833   46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 157819833  126 DLAQILEE 133
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 46-129 3.52e-38

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 136.62  E-value: 3.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833  46 ETCRQNFRNFPYPDVAGPRKALSQLRELCLKWLRPEVHSKEQILELLVLEQFLSILPGEVRTWVNSQYPENSEEVVALVE 125
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 157819833 126 DLAQ 129
Cdd:cd07936   82 DLLA 85
KRAB smart00349
krueppel associated box;
168-225 9.70e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 9.70e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819833   168 VTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSLGLTVYRPTVIPILE---EPWM 225
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqgeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 167-208 4.73e-16

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: 72.12  E-value: 4.73e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 157819833  167 SVTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSLG 208
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 168-207 9.73e-14

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: 65.65  E-value: 9.73e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157819833 168 VTFNDVAVDITQEDWELMRPVEKELYKTVTLQNYWNMVSL 207
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
420-752 1.33e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 420 KPYECHQCGKAFSQRAHLTIHQRIHTGEKPYKCNDCGKD--FSQRAHLTIHQRTHTGEKPYKC--LECSKTFSHSSSLIN 495
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 496 HQRVHT------------GEKPYI------------------CNECGKTFSQSTHL-LQHQKIHTGKKPYKCN------- 537
Cdd:COG5048  112 SSSSNSndnnllsshslpPSSRDPqlpdllsisnlrnnplpgNNSSSVNTPQSNSLhPPLPANSLSKDPSSNLsllissn 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 538 ---------ECWKVFSQSTY--LIRHQRIHSGEKCYKCTECGKAFAHSSTLIQHQTTHTGEKSYICNVCGKAFSQSANLT 606
Cdd:COG5048  192 vstsipsssENSPLSSSYSIpsSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 607 QHHRTHTGE-------KPYKCSVCGKAFSQSVHLTQHQR--IHNGE--KPFKC--NTCGKAYRQGANLTQHQRVHTGEKP 673
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 674 YKCHHCGKAFIYSSSLN-------QHRRTHTGERPYKCTH--CNKDFSQRTCLIQHQRIHTGERPYGCR--ICGKSFTQS 742
Cdd:COG5048  352 AKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRH 431

                        410
                 ....*....|
gi 157819833 743 TNLIQHQRVH 752
Cdd:COG5048  432 YNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
267-602 4.20e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 267 SCDCEDGLERQPAYAFRKIHIDEDDFSLKSELSqedptEECLSKYDLYRDNFEKHTNLIIQFDTQSDSKTLLYNESKPTF 346
Cdd:COG5048  115 SNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLR-----NNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 347 TNVSSGGVVHGKILPGDKPYSCNVCG---KKFRKYPSLLAHRNNHAKDKSYECEecgkefKHLSSLIAHQRMHTGEKPYE 423
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSsdqNLENSSSSLPLTTNSQLSPKSLLSQ------SPSSLSSSDSSSSASESPRS 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 424 CHQcGKAFSQRAHLTIHQRIHTG-EKPYKCNDCGKDFSQRAHLTIHQRT--HTGE--KPYKCLE--CSKTFSHSSSLINH 496
Cdd:COG5048  264 SLP-TASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 497 QRVHTGEKPYIC--NECGKTFSQSTH-----LLQHQKIHTGKKPYKC--NECWKVFSQSTYLIRH--QRIHSGEKCYKCT 565
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNP 422

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 157819833 566 ECGKAFAHSSTLIQHQTTHTGEKSYICNVCGKAFSQS 602
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
448-753 4.24e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 448 KPYKCNDCGKDFSQRAHLTIHQRTHTGEKPYKCL--ECSKTFSHSSSLINHQRVHTGEKPYIC----------------N 509
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 510 ECGKTFSQSTHLLQHQKIHTGKKPYKCNECWKVFSQSTYLIRHQRIHSGEKCYKCT--------ECGKAFAHSSTLIQHQ 581
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpplpansLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 582 TTHTGEKSYICNVCGKAFSQSANLTQHHRTHTgEKPYKCSVCGKAFSQSVHLTQHQRIHNGEKPFKCNTCGKAYRQGANL 661
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 662 TQHQRVHTGE-------KPYKCHHCGKAFIYSSSLNQHRRT--HTGE--RPYKCTH--CNKDFSQRTCLIQHQRIHTGER 728
Cdd:COG5048  271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340
                 ....*....|....*....|....*..
gi 157819833 729 PYGC--RICGKSFTQSTNLIQHQRVHM 753
Cdd:COG5048  351 PAKEklLNSSSKFSPLLNNEPPQSLQQ 377
zf-H2C2_2 pfam13465
Zinc-finger double domain;
604-629 2.92e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.92e-05
                          10        20
                  ....*....|....*....|....*.
gi 157819833  604 NLTQHHRTHTGEKPYKCSVCGKAFSQ 629
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
660-685 4.45e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.45e-05
                          10        20
                  ....*....|....*....|....*.
gi 157819833  660 NLTQHQRVHTGEKPYKCHHCGKAFIY 685
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
389-519 6.87e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 389 AKDKSYECEECGKEFKHLSSLIAHQRM--HTGE--KPYEC--HQCGKAFSQRAHLTIHQRIHTGEKPYKC---------- 452
Cdd:COG5048  285 GFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEkllnssskfs 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 453 ---------------------------NDCGKDFSQRAHLTIHQRTHTGEKP--YKCLECSKTFSHSSSLINHQRVHTGE 503
Cdd:COG5048  365 pllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNH 444

                        170
                 ....*....|....*.
gi 157819833 504 KPYICNECGKTFSQST 519
Cdd:COG5048  445 APLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
436-461 1.71e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.71e-04
                          10        20
                  ....*....|....*....|....*.
gi 157819833  436 HLTIHQRIHTGEKPYKCNDCGKDFSQ 461
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
408-433 2.16e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.16e-04
                          10        20
                  ....*....|....*....|....*.
gi 157819833  408 SLIAHQRMHTGEKPYECHQCGKAFSQ 433
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-489 2.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 157819833  464 HLTIHQRTHTGEKPYKCLECSKTFSH 489
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 328-417 2.68e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 328 FDTQSDSKTllynESKPTFTNVSSGGVVHG-----------KILPGDKPYSCNV--CGKKFR-----KYPSLLAHRNNH- 388
Cdd:COG5189  305 ISTGEMIDV----RKLPCTNSSSNGKLAHGgernidtpsrmLKVKDGKPYKCPVegCNKKYKnqnglKYHMLHGHQNQKl 380

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157819833 389 -------------AKDKSYECEECGKEFKHLSSLIAHqRMHT 417
Cdd:COG5189  381 henpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 399-444 2.98e-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: 40.23  E-value: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157819833 399 CGKEFKHLSSLIAHQRMHTgekpYECHQCGKAFSQRAHLTIH-QRIH 444
Cdd:cd20908    7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
688-713 3.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|....*.
gi 157819833  688 SLNQHRRTHTGERPYKCTHCNKDFSQ 713
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 450-472 6.21e-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: 37.66  E-value: 6.21e-04
                          10        20
                  ....*....|....*....|...
gi 157819833  450 YKCNDCGKDFSQRAHLTIHQRTH 472
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 674-696 6.71e-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: 6.71e-04
                          10        20
                  ....*....|....*....|...
gi 157819833  674 YKCHHCGKAFIYSSSLNQHRRTH 696
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 448-500 6.79e-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: 39.08  E-value: 6.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157819833 448 KPYkCNDCGKDFSQRAHLTIHQRTHTgekpYKCLECSKTFSHSSSLINH-QRVH 500
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 670-752 8.11e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 670 GEKPYKCH--HCGKAFIYSSSLNQHRrthtgerpyKCTHCNKDFSQRTCLIQHQRIHTGERPYGCRICGKSFtQSTNLIQ 747
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415


                 ....*
gi 157819833 748 HQRVH 752
Cdd:COG5189  416 YHRKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
548-573 1.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 157819833  548 YLIRHQRIHSGEKCYKCTECGKAFAH 573
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 422-444 1.17e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  422 YECHQCGKAFSQRAHLTIHQRIH 444
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
632-657 1.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.34e-03
                          10        20
                  ....*....|....*....|....*.
gi 157819833  632 HLTQHQRIHNGEKPFKCNTCGKAYRQ 657
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 618-640 1.35e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.35e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  618 YKCSVCGKAFSQSVHLTQHQRIH 640
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 700-752 1.39e-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: 38.31  E-value: 1.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157819833 700 RPYkCTHCNKDFSQRTCLIQHQRIHTgerpYGCRICGKSFTQSTNLIQH-QRVH 752
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 590-612 2.18e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.18e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  590 YICNVCGKAFSQSANLTQHHRTH 612
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 2.38e-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: 2.38e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  394 YECEECGKEFKHLSSLIAHQRMH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
531-709 2.60e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 531 KKPYKCNECWKVFSQSTYLIRHQRIHSGEKCYKCT--ECGKAFAHSSTLIQHQTTHTGEKSYICNVCGKAFSQSANLTQH 608
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819833 609 HRTHTGEkPYKCSVCGKAFSQSVHLTQH----QRIHNGEKPFKCNTCGKAYRQGANLTQHQRVHTgekpykcHHCGKAFI 684
Cdd:COG5048  111 SSSSSNS-NDNNLLSSHSLPPSSRDPQLpdllSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-------SLSKDPSS 182

                        170       180
                 ....*....|....*....|....*
gi 157819833 685 YSSSLNQHRRTHTGERPYKCTHCNK 709
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS 207
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 534-556 2.90e-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: 2.90e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  534 YKCNECWKVFSQSTYLIRHQRIH 556
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 506-528 3.59e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.59e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  506 YICNECGKTFSQSTHLLQHQKIH 528
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
520-545 4.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|....*.
gi 157819833  520 HLLQHQKIHTGKKPYKCNECWKVFSQ 545
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 478-500 4.29e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 4.29e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  478 YKCLECSKTFSHSSSLINHQRVH 500
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 616-668 4.46e-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: 4.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157819833 616 KPYkCSVCGKAFSQSVHLTQHQRihngEKPFKCNTCGKAYRQGANLTQH-QRVH 668
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
717-741 5.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.09e-03
                          10        20
                  ....*....|....*....|....*
gi 157819833  717 LIQHQRIHTGERPYGCRICGKSFTQ 741
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 562-584 5.81e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.81e-03
                          10        20
                  ....*....|....*....|...
gi 157819833  562 YKCTECGKAFAHSSTLIQHQTTH 584
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
492-517 8.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.09e-03
                          10        20
                  ....*....|....*....|....*.
gi 157819833  492 SLINHQRVHTGEKPYICNECGKTFSQ 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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