NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|11386193|ref|NP_008922|]
View 

zinc finger protein 197 isoform 1 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 12210971)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-150 5.45e-63

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 208.70  E-value: 5.45e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193      38 WETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALV 117
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 11386193     118 EELQKDLDGPAIQVPVLVKDQDTLQKVVSAPGT 150
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 216-256 4.29e-18

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: 78.28  E-value: 4.29e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11386193    216 LVMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSL 256
Cdd:pfam01352    1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
424-853 2.03e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  424 KPYKCNECGKAFSQSAYLLNHQRIHTGEKPYKC--KECGKGFYRHSGLIIHLRRHSGERPYKCNecGKVFSQNAYLIDHQ 501
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  502 RLHKGEEPYKCNKCQK-----AFILKKSLILHQRIHSGEKPYK-CDECGKTFAQTTYLI-DHQRLHSAENPYKCkecgkv 574
Cdd:COG5048  110 LSSSSSNSNDNNLLSShslppSSRDPQLPDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpPLPANSLSKDPSSN------ 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  575 firsKSLLLHQRVHTEKKTFGCKKCGKIFSSKSNFIDHKRMHSREKPYKCTECGKAFTQSaylFDHQRLHNGEKPYECNE 654
Cdd:COG5048  184 ----LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS---LLSQSPSSLSSSDSSSS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  655 CGKVFILKKSLILHQRFHtgenlyeckdcgkvfGSNRNLIDHERLhngEKPYECRECGKTFIMSKSFMVHQ--KLHTQE- 731
Cdd:COG5048  257 ASESPRSSLPTASSQSSS---------------PNESDSSSEKGF---SLPIKSKQCNISFSRSSPLTRHLrsVNHSGEs 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  732 -KAYKC--EDCGKAFSYNSSLLVHRRIHTGEKPFECSECGRAFSSNRNLIE-------HKRIHSGEKPYECDECGKC--- 798
Cdd:COG5048  319 lKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSNSCIrnf 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386193  799 ---FILKKSLIGHqrIHTREKSYKCNDCGKVFSYRSNLIAHQRIHTGEKPYACSECGK 853
Cdd:COG5048  399 krdSNLSLHIITH--LSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
760-1026 2.75e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  760 KPFECSECGRAFSSNRNLIEHKRIHSGEKPYEC--DECGKCFILKKSLIGHQRIHTREKSYKCND-CGKVFSYRSNLIAH 836
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  837 QRIHTGEKPYACSECGKGFTYNRNLIEHQRIHSgekTYECHVCRKVLTSSRNLMVHQRIHtgeKPYKCNECGKDFSQNKN 916
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS---NLRNNPLPGNNSSSVNTPQSNSLH---PPLPANSLSKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  917 LVVHQRMHTGEKPYECDKCRKSFTSKRNLVGHQRIHTGEKPYGCNDCSKVFRQRKNLTVHQKIHTDEKPCECDVSEKEFS 996
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270
                 ....*....|....*....|....*....|..
gi 11386193  997 QTSN--LHLQQKIHTIEEFSWLQNTNESKIEI 1026
Cdd:COG5048  266 PTASsqSSSPNESDSSSEKGFSLPIKSKQCNI 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
384-409 5.03e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.03e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    384 HLINHRRIHTGEKPHKCKECGKGFIQ 409
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-150 5.45e-63

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 208.70  E-value: 5.45e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193      38 WETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALV 117
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 11386193     118 EELQKDLDGPAIQVPVLVKDQDTLQKVVSAPGT 150
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 39-126 3.18e-48

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: 165.74  E-value: 3.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193     39 ETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALVE 118
Cdd:pfam02023    2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                   ....*...
gi 11386193    119 ELQKDLDG 126
Cdd:pfam02023   82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 39-121 2.25e-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: 137.78  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   39 ETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALVE 118
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ...
gi 11386193  119 ELQ 121
Cdd:cd07936   82 DLL 84
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 216-256 4.29e-18

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: 78.28  E-value: 4.29e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11386193    216 LVMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSL 256
Cdd:pfam01352    1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 217-256 2.21e-17

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: 76.43  E-value: 2.21e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 11386193  217 VMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSL 256
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB smart00349
krueppel associated box;
217-257 7.05e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 72.63  E-value: 7.05e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 11386193     217 VMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSLE 257
Cdd:smart00349    1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
424-853 2.03e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  424 KPYKCNECGKAFSQSAYLLNHQRIHTGEKPYKC--KECGKGFYRHSGLIIHLRRHSGERPYKCNecGKVFSQNAYLIDHQ 501
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  502 RLHKGEEPYKCNKCQK-----AFILKKSLILHQRIHSGEKPYK-CDECGKTFAQTTYLI-DHQRLHSAENPYKCkecgkv 574
Cdd:COG5048  110 LSSSSSNSNDNNLLSShslppSSRDPQLPDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpPLPANSLSKDPSSN------ 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  575 firsKSLLLHQRVHTEKKTFGCKKCGKIFSSKSNFIDHKRMHSREKPYKCTECGKAFTQSaylFDHQRLHNGEKPYECNE 654
Cdd:COG5048  184 ----LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS---LLSQSPSSLSSSDSSSS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  655 CGKVFILKKSLILHQRFHtgenlyeckdcgkvfGSNRNLIDHERLhngEKPYECRECGKTFIMSKSFMVHQ--KLHTQE- 731
Cdd:COG5048  257 ASESPRSSLPTASSQSSS---------------PNESDSSSEKGF---SLPIKSKQCNISFSRSSPLTRHLrsVNHSGEs 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  732 -KAYKC--EDCGKAFSYNSSLLVHRRIHTGEKPFECSECGRAFSSNRNLIE-------HKRIHSGEKPYECDECGKC--- 798
Cdd:COG5048  319 lKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSNSCIrnf 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386193  799 ---FILKKSLIGHqrIHTREKSYKCNDCGKVFSYRSNLIAHQRIHTGEKPYACSECGK 853
Cdd:COG5048  399 krdSNLSLHIITH--LSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
760-1026 2.75e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  760 KPFECSECGRAFSSNRNLIEHKRIHSGEKPYEC--DECGKCFILKKSLIGHQRIHTREKSYKCND-CGKVFSYRSNLIAH 836
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  837 QRIHTGEKPYACSECGKGFTYNRNLIEHQRIHSgekTYECHVCRKVLTSSRNLMVHQRIHtgeKPYKCNECGKDFSQNKN 916
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS---NLRNNPLPGNNSSSVNTPQSNSLH---PPLPANSLSKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  917 LVVHQRMHTGEKPYECDKCRKSFTSKRNLVGHQRIHTGEKPYGCNDCSKVFRQRKNLTVHQKIHTDEKPCECDVSEKEFS 996
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270
                 ....*....|....*....|....*....|..
gi 11386193  997 QTSN--LHLQQKIHTIEEFSWLQNTNESKIEI 1026
Cdd:COG5048  266 PTASsqSSSPNESDSSSEKGFSLPIKSKQCNI 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
888-913 3.19e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.19e-05
                           10        20
                   ....*....|....*....|....*.
gi 11386193    888 NLMVHQRIHTGEKPYKCNECGKDFSQ 913
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-437 2.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.74e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    412 SLLMHLRNHSGEKPYKCNECGKAFSQ 437
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
384-409 5.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.03e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    384 HLINHRRIHTGEKPHKCKECGKGFIQ 409
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 568-725 9.75e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 42.94  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   568 CKECgKVFIRSKSLLLHQrVHTEKKTFGCKK--CGkIFSSKSNFIDHkrMHsrekpykCTECGKAFtQSAYLFDHQRLHN 645
Cdd:PLN03086  410 CRNC-KHYIPSRSIALHE-AYCSRHNVVCPHdgCG-IVLRVEEAKNH--VH-------CEKCGQAF-QQGEMEKHMKVFH 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   646 geKPYECnECGkVFILKKSLILHQRFHTGENLYECKDCGKVF--GSN--------RNLIDHERLhNGEKPYECRECGKTf 715
Cdd:PLN03086  477 --EPLQC-PCG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVqaGGSamdvrdrlRGMSEHESI-CGSRTAPCDSCGRS- 550

                         170
                  ....*....|
gi 11386193   716 IMSKSFMVHQ 725
Cdd:PLN03086  551 VMLKEMDIHQ 560
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 844-896 1.23e-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: 38.69  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 11386193  844 KPYaCSECGKGFTYNRNLIEHQRihsgEKTYECHVCRKVLTSSRNLMVH-QRIH 896
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 536-591 1.37e-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: 38.69  E-value: 1.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386193  536 KPYkCDECGKTFAQTTYLIDHQRLHSaenpYKCKECGKVFIRSKSLLLH-QRVHTEK 591
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-150 5.45e-63

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 208.70  E-value: 5.45e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193      38 WETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALV 117
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100       110
                    ....*....|....*....|....*....|...
gi 11386193     118 EELQKDLDGPAIQVPVLVKDQDTLQKVVSAPGT 150
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 39-126 3.18e-48

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: 165.74  E-value: 3.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193     39 ETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALVE 118
Cdd:pfam02023    2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                   ....*...
gi 11386193    119 ELQKDLDG 126
Cdd:pfam02023   82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 39-121 2.25e-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: 137.78  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   39 ETSHLHFRQLRYHETSGPQEALSRLRELCRRWLRPEARTKAQILELLVLEQFLSILPGEIRTWVQLHHPGSGEEAVALVE 118
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ...
gi 11386193  119 ELQ 121
Cdd:cd07936   82 DLL 84
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 216-256 4.29e-18

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: 78.28  E-value: 4.29e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11386193    216 LVMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSL 256
Cdd:pfam01352    1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 217-256 2.21e-17

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: 76.43  E-value: 2.21e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 11386193  217 VMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSL 256
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB smart00349
krueppel associated box;
217-257 7.05e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 72.63  E-value: 7.05e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 11386193     217 VMFEEVSVCFTSEEWACLGPIQRALYWDVMLENYGNVTSLE 257
Cdd:smart00349    1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
424-853 2.03e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.04  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  424 KPYKCNECGKAFSQSAYLLNHQRIHTGEKPYKC--KECGKGFYRHSGLIIHLRRHSGERPYKCNecGKVFSQNAYLIDHQ 501
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  502 RLHKGEEPYKCNKCQK-----AFILKKSLILHQRIHSGEKPYK-CDECGKTFAQTTYLI-DHQRLHSAENPYKCkecgkv 574
Cdd:COG5048  110 LSSSSSNSNDNNLLSShslppSSRDPQLPDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpPLPANSLSKDPSSN------ 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  575 firsKSLLLHQRVHTEKKTFGCKKCGKIFSSKSNFIDHKRMHSREKPYKCTECGKAFTQSaylFDHQRLHNGEKPYECNE 654
Cdd:COG5048  184 ----LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS---LLSQSPSSLSSSDSSSS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  655 CGKVFILKKSLILHQRFHtgenlyeckdcgkvfGSNRNLIDHERLhngEKPYECRECGKTFIMSKSFMVHQ--KLHTQE- 731
Cdd:COG5048  257 ASESPRSSLPTASSQSSS---------------PNESDSSSEKGF---SLPIKSKQCNISFSRSSPLTRHLrsVNHSGEs 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  732 -KAYKC--EDCGKAFSYNSSLLVHRRIHTGEKPFECSECGRAFSSNRNLIE-------HKRIHSGEKPYECDECGKC--- 798
Cdd:COG5048  319 lKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSNSCIrnf 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386193  799 ---FILKKSLIGHqrIHTREKSYKCNDCGKVFSYRSNLIAHQRIHTGEKPYACSECGK 853
Cdd:COG5048  399 krdSNLSLHIITH--LSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
370-774 6.42e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.50  E-value: 6.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  370 YKCDMCCKHFNKISHLINHRRIHTGEKPHKC--KECGKGFIQRSSLLMHLRNHSGEKPYKCN-ECGKAFSQSAYLLNHQR 446
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  447 IHTGEKPYKCKECGKGFYRHSGLIIHLRRHS---GERPYKCNECGKVFSQNAYLI-DHQRLHKGEEPYKCNkcqkafilk 522
Cdd:COG5048  114 SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQSNSLHpPLPANSLSKDPSSNL--------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  523 kSLILHQRIHSGEKPYKCDECGKTFAQTTYLIDHQRLHSAENPYKCKECGkvFIRSKSLLLHQRVHTEKKTFG--CKKCG 600
Cdd:COG5048  185 -SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSSDSSssASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  601 KIFSSKSNFID--HKRMHSRE-----KPYKCTECGKAFTQSAYLFDHQR--LHNGE--KPYECNE--CGKVFILKKSLIL 667
Cdd:COG5048  262 RSSLPTASSQSssPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  668 HQRFHTGENLYECKDC-------GKVFGSNRNLIDHERLHNGEKPYEC--RECGKTFIMSKSFMVHQKLHT--QEKAYKC 736
Cdd:COG5048  342 HILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKN 421

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 11386193  737 EDCGKAFSYNSSLLVHRRIHTGEKPFECSECGRAFSSN 774
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
536-939 1.32e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  536 KPYKCDECGKTFAQTTYLIDHQRLHSAENPYKC--KECGKVFIRSKSLLLHQRVHTEKKTFGCKKCGKIFSSKSNF--ID 611
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSssLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  612 HKRMHSReKPYKCTECGKAFTQSAYL--FDHQRLHNGEKPYE-CNECGKVFI--LKKSLILHQRFHTGENLyeckdcgkv 686
Cdd:COG5048  112 SSSSNSN-DNNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPgNNSSSVNTPqsNSLHPPLPANSLSKDPS--------- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  687 fgSNRNLIDHERLHNGEKPYECRECGKTFIMSKSFMVHQKLHTQEKAYKCEDCGKAFSYNSSLLVHRRIHTGEKPFECSE 766
Cdd:COG5048  182 --SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  767 CGRAFSSNRNLIEHKRIHSGE-------KPYECDECGKCFILKKSLIGHQR--IHTRE--KSYKC--NDCGKVFSYRSNL 833
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  834 IAHQRIHTGEKPYACSECGKGFTYNRNLIE-------HQRIHSGEKTYEC--HVCRKVLTSSRNLMVHQRIHTGEKP--Y 902
Cdd:COG5048  340 KRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynC 419

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 11386193  903 KCNECGKDFSQNKNLVVHQRMHTGEKPYECDKCRKSF 939
Cdd:COG5048  420 KNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
620-981 2.31e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  620 KPYKCTECGKAFTQSAYLFDHQRLHNGEKPYECNECGKVFILKKSLILHQRF---HTGENLYECKDCGKVFGSNRNLIDH 696
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLrthHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  697 ERLHNGEKPYECRECGKTFIMSKSFMVHQKLHTQEKAYKCEDCGKAF----------------------SYNSSLLVHRR 754
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvntpqsnslhpplpanslskdpSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  755 IHTGEKPFECSECGRAFSSNRNLIEHKRIHSGEKPYECDECGkcFILKKSLIGHQRIHTREKSYKCNDC-------GKVF 827
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSSDSSSSASesprsslPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  828 SYRSNLIAH-QRIHTG-EKPYACSECGKGFTYNRNLIEHQR--IHSGE--KTYECHV--CRKVLTSSRNLMVHQRIHTGE 899
Cdd:COG5048  270 SQSSSPNESdSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  900 KPYKC--NECGKDFSQNKNLVVHQRMH-----TGEKPYECD--KCRKSFTSKRNLVGHQRIHTGEKPYGCND--CSKVFR 968
Cdd:COG5048  350 SPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFN 429

                        410
                 ....*....|...
gi 11386193  969 QRKNLTVHQKIHT 981
Cdd:COG5048  430 RHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
760-1026 2.75e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  760 KPFECSECGRAFSSNRNLIEHKRIHSGEKPYEC--DECGKCFILKKSLIGHQRIHTREKSYKCND-CGKVFSYRSNLIAH 836
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  837 QRIHTGEKPYACSECGKGFTYNRNLIEHQRIHSgekTYECHVCRKVLTSSRNLMVHQRIHtgeKPYKCNECGKDFSQNKN 916
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS---NLRNNPLPGNNSSSVNTPQSNSLH---PPLPANSLSKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  917 LVVHQRMHTGEKPYECDKCRKSFTSKRNLVGHQRIHTGEKPYGCNDCSKVFRQRKNLTVHQKIHTDEKPCECDVSEKEFS 996
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270
                 ....*....|....*....|....*....|..
gi 11386193  997 QTSN--LHLQQKIHTIEEFSWLQNTNESKIEI 1026
Cdd:COG5048  266 PTASsqSSSPNESDSSSEKGFSLPIKSKQCNI 297
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
405-607 4.07e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  405 KGFIQRSSLLMHLRNHSG-EKPYKCNECGKAFSQSAYLLNHQR--IHTGE--KPYKCKE--CGKGFYRHSGLIIHLRRHS 477
Cdd:COG5048  268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193  478 GERPYKC--NECGKVFSQNAylidhqrlhkgeepykcNKCQKAFILKKSLILHQRIHSGEKPYKCDECGKTFAQTTYLID 555
Cdd:COG5048  348 SISPAKEklLNSSSKFSPLL-----------------NNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIIT 410

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 11386193  556 HQRLHSAEnpYKCKECGKVFIRSKSLLLHQRVHTEKKTFGCKKCGKIFSSKS 607
Cdd:COG5048  411 HLSFRPYN--CKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
888-913 3.19e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.19e-05
                           10        20
                   ....*....|....*....|....*.
gi 11386193    888 NLMVHQRIHTGEKPYKCNECGKDFSQ 913
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
916-941 1.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.68e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    916 NLVVHQRMHTGEKPYECDKCRKSFTS 941
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-437 2.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.74e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    412 SLLMHLRNHSGEKPYKCNECGKAFSQ 437
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
776-799 3.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.93e-04
                           10        20
                   ....*....|....*....|....
gi 11386193    776 NLIEHKRIHSGEKPYECDECGKCF 799
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 818-840 4.20e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.20e-04
                           10        20
                   ....*....|....*....|...
gi 11386193    818 YKCNDCGKVFSYRSNLIAHQRIH 840
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
524-549 4.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 4.51e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    524 SLILHQRIHSGEKPYKCDECGKTFAQ 549
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
440-465 4.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.74e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    440 YLLNHQRIHTGEKPYKCKECGKGFYR 465
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
384-409 5.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.03e-04
                           10        20
                   ....*....|....*....|....*.
gi 11386193    384 HLINHRRIHTGEKPHKCKECGKGFIQ 409
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 568-725 9.75e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 42.94  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   568 CKECgKVFIRSKSLLLHQrVHTEKKTFGCKK--CGkIFSSKSNFIDHkrMHsrekpykCTECGKAFtQSAYLFDHQRLHN 645
Cdd:PLN03086  410 CRNC-KHYIPSRSIALHE-AYCSRHNVVCPHdgCG-IVLRVEEAKNH--VH-------CEKCGQAF-QQGEMEKHMKVFH 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386193   646 geKPYECnECGkVFILKKSLILHQRFHTGENLYECKDCGKVF--GSN--------RNLIDHERLhNGEKPYECRECGKTf 715
Cdd:PLN03086  477 --EPLQC-PCG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVqaGGSamdvrdrlRGMSEHESI-CGSRTAPCDSCGRS- 550

                         170
                  ....*....|
gi 11386193   716 IMSKSFMVHQ 725
Cdd:PLN03086  551 VMLKEMDIHQ 560
zf-H2C2_2 pfam13465
Zinc-finger double domain;
832-857 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 1.07e-03
                           10        20
                   ....*....|....*....|....*.
gi 11386193    832 NLIAHQRIHTGEKPYACSECGKGFTY 857
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 844-896 1.23e-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: 38.69  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 11386193  844 KPYaCSECGKGFTYNRNLIEHQRihsgEKTYECHVCRKVLTSSRNLMVH-QRIH 896
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 536-591 1.37e-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: 38.69  E-value: 1.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386193  536 KPYkCDECGKTFAQTTYLIDHQRLHSaenpYKCKECGKVFIRSKSLLLH-QRVHTEK 591
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
748-773 1.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.42e-03
                           10        20
                   ....*....|....*....|....*.
gi 11386193    748 SLLVHRRIHTGEKPFECSECGRAFSS 773
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
608-633 1.78e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.78e-03
                           10        20
                   ....*....|....*....|....*.
gi 11386193    608 NFIDHKRMHSREKPYKCTECGKAFTQ 633
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 424-473 2.03e-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: 37.92  E-value: 2.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 11386193  424 KPYkCNECGKAFSQSAYLLNHQRIHTgekpYKCKECGKGFYRHSGLIIHL 473
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45
zf-H2C2_2 pfam13465
Zinc-finger double domain;
472-493 3.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.18e-03
                           10        20
                   ....*....|....*....|..
gi 11386193    472 HLRRHSGERPYKCNECGKVFSQ 493
Cdd:pfam13465    5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 902-924 4.25e-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: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 11386193    902 YKCNECGKDFSQNKNLVVHQRMH 924
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 426-448 4.97e-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: 4.97e-03
                           10        20
                   ....*....|....*....|...
gi 11386193    426 YKCNECGKAFSQSAYLLNHQRIH 448
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 900-952 5.10e-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: 5.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 11386193  900 KPYkCNECGKDFSQNKNLVVHQRMHTgekpYECDKCRKSFTSKRNLVGH-QRIH 952
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 ...
 566-588 5.33e-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: 5.33e-03
                           10        20
                   ....*....|....*....|...
gi 11386193    566 YKCKECGKVFIRSKSLLLHQRVH 588
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 734-756 5.49e-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: 5.49e-03
                           10        20
                   ....*....|....*....|...
gi 11386193    734 YKCEDCGKAFSYNSSLLVHRRIH 756
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 482-504 6.55e-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: 6.55e-03
                           10        20
                   ....*....|....*....|...
gi 11386193    482 YKCNECGKVFSQNAYLIDHQRLH 504
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
692-715 6.99e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 6.99e-03
                           10        20
                   ....*....|....*....|....
gi 11386193    692 NLIDHERLHNGEKPYECRECGKTF 715
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH