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Conserved domains on  [gi|294610662|ref|NP_001170976|]
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zinc finger protein with KRAB and SCAN domains 7 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein; zinc finger and BTB domain-containing protein( domain architecture ID 12210801)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation| zinc finger and BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
46-156 1.10e-57

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 190.98  E-value: 1.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662    46 EIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 294610662   126 DFQRHLSESGE-VSPPVQEQDVHLKKMGALSA 156
Cdd:smart00431  82 DLERELDEPGQqVSAHVHGQEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
333-702 1.56e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 333 MPSSPVEHQGEAKRQKSYQCDECGKVFSQSSRFLGHQRIHVGERPFECNK--CGKTFQQISQLVVHLRIHTQEKPYECC- 409
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 410 --------------------------ESGKTYCHSSHLIQH-------QRLRNGDKPYKGNECVRASIQSSQllvhkrtH 456
Cdd:COG5048   97 slplsnskasssslsssssnsndnnlLSSHSLPPSSRDPQLpdllsisNLRNNPLPGNNSSSVNTPQSNSLH-------P 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 457 TGEKPDESGEAFIWNKSLIQHQVLHISKKLYECNECGKaFYTNRNLIDHQRIHTGEKPYECIEC---------------- 520
Cdd:COG5048  170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNsqlspksllsqspssl 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 521 GKSFSRSKCLTRHQSLHTGEKT-------------------YKCSECGKAFLQNSQLIDHKR--VHTGE--KPFECSE-- 575
Cdd:COG5048  249 SSSDSSSSASESPRSSLPTASSqssspnesdsssekgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 576 CGKKFSLGKCLIRHQRLHTGEKPYKC--SECGKSFNQNSH-----LIIHQRIHTGEKPYGC--NECGKVFSYSSSLMVHQ 646
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294610662 647 RTHTGEKP--YKCKDCMKAFGDSSQLIVHQRVHTGEKPYECAECGKAFSQRSTFNHHQ 702
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
46-156 1.10e-57

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 190.98  E-value: 1.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662    46 EIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 294610662   126 DFQRHLSESGE-VSPPVQEQDVHLKKMGALSA 156
Cdd:smart00431  82 DLERELDEPGQqVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-133 6.92e-50

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: 168.82  E-value: 6.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662   46 EIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMVE 125
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 294610662  126 DFQRHLSE 133
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-129 2.84e-39

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: 139.32  E-value: 2.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662  45 CEIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMV 124
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 294610662 125 EDFQR 129
Cdd:cd07936   81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
333-702 1.56e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 333 MPSSPVEHQGEAKRQKSYQCDECGKVFSQSSRFLGHQRIHVGERPFECNK--CGKTFQQISQLVVHLRIHTQEKPYECC- 409
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 410 --------------------------ESGKTYCHSSHLIQH-------QRLRNGDKPYKGNECVRASIQSSQllvhkrtH 456
Cdd:COG5048   97 slplsnskasssslsssssnsndnnlLSSHSLPPSSRDPQLpdllsisNLRNNPLPGNNSSSVNTPQSNSLH-------P 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 457 TGEKPDESGEAFIWNKSLIQHQVLHISKKLYECNECGKaFYTNRNLIDHQRIHTGEKPYECIEC---------------- 520
Cdd:COG5048  170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNsqlspksllsqspssl 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 521 GKSFSRSKCLTRHQSLHTGEKT-------------------YKCSECGKAFLQNSQLIDHKR--VHTGE--KPFECSE-- 575
Cdd:COG5048  249 SSSDSSSSASESPRSSLPTASSqssspnesdsssekgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 576 CGKKFSLGKCLIRHQRLHTGEKPYKC--SECGKSFNQNSH-----LIIHQRIHTGEKPYGC--NECGKVFSYSSSLMVHQ 646
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294610662 647 RTHTGEKP--YKCKDCMKAFGDSSQLIVHQRVHTGEKPYECAECGKAFSQRSTFNHHQ 702
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-526 1.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 294610662  501 NLIDHQRIHTGEKPYECIECGKSFSR 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 597-645 3.51e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 3.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 294610662 597 KPYkCSECGKSFNQNSHLIIHQRIHTgekpYGCNECGKVFSYSSSLMVH 645
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
46-156 1.10e-57

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 190.98  E-value: 1.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662    46 EIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 294610662   126 DFQRHLSESGE-VSPPVQEQDVHLKKMGALSA 156
Cdd:smart00431  82 DLERELDEPGQqVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-133 6.92e-50

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: 168.82  E-value: 6.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662   46 EIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMVE 125
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 294610662  126 DFQRHLSE 133
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-129 2.84e-39

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: 139.32  E-value: 2.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662  45 CEIFRLHFRQLCYHEMSGPQQALSRLRELCHWWLMPEVHTKEQILELLVLEQFLSILPRELQTWVQLHHPETGEEAVAMV 124
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 294610662 125 EDFQR 129
Cdd:cd07936   81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
333-702 1.56e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 333 MPSSPVEHQGEAKRQKSYQCDECGKVFSQSSRFLGHQRIHVGERPFECNK--CGKTFQQISQLVVHLRIHTQEKPYECC- 409
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 410 --------------------------ESGKTYCHSSHLIQH-------QRLRNGDKPYKGNECVRASIQSSQllvhkrtH 456
Cdd:COG5048   97 slplsnskasssslsssssnsndnnlLSSHSLPPSSRDPQLpdllsisNLRNNPLPGNNSSSVNTPQSNSLH-------P 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 457 TGEKPDESGEAFIWNKSLIQHQVLHISKKLYECNECGKaFYTNRNLIDHQRIHTGEKPYECIEC---------------- 520
Cdd:COG5048  170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNsqlspksllsqspssl 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 521 GKSFSRSKCLTRHQSLHTGEKT-------------------YKCSECGKAFLQNSQLIDHKR--VHTGE--KPFECSE-- 575
Cdd:COG5048  249 SSSDSSSSASESPRSSLPTASSqssspnesdsssekgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 576 CGKKFSLGKCLIRHQRLHTGEKPYKC--SECGKSFNQNSH-----LIIHQRIHTGEKPYGC--NECGKVFSYSSSLMVHQ 646
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294610662 647 RTHTGEKP--YKCKDCMKAFGDSSQLIVHQRVHTGEKPYECAECGKAFSQRSTFNHHQ 702
Cdd:COG5048  409 ITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
525-610 1.22e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 525 SRSKCLTRHQSLHTGEKTYKCSECGKAFLQNSQLIDHKRVHTGEKPFECS--ECGKKFSLGKCLIRHQRLHTGEKPYKCS 602
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS 95


                 ....*...
gi 294610662 603 ECGKSFNQ 610
Cdd:COG5048   96 KSLPLSNS 103
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-526 1.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 294610662  501 NLIDHQRIHTGEKPYECIECGKSFSR 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
304-535 2.00e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 304 LESDFLEKEDKNSTEDRNEECKDVGVHPEMPSSPVEHQGEAKRQKSYQCDECGKVFSQSSRFLGHQR--IHVGE--RPFE 379
Cdd:COG5048  244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFS 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 380 C--NKCGKTFQQISQLVVHLRIHTQEKPYECCES--------GKTYCHSSHLIQHQRLRNGDKPYK-GNECVRASIQSSQ 448
Cdd:COG5048  324 CpySLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfspLLNNEPPQSLQQYKDLKNDKKSETlSNSCIRNFKRDSN 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 449 LLVHKRTHTGEKPDEsgeafiwnksliqhqvlhiskklYECNECGKAFYTNRNLIDHQRIHTGEKPYECIECGKSFSRSK 528
Cdd:COG5048  404 LSLHIITHLSFRPYN-----------------------CKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460


                 ....*..
gi 294610662 529 CLTRHQS 535
Cdd:COG5048  461 LSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
586-610 2.62e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.62e-05
                          10        20
                  ....*....|....*....|....*
gi 294610662  586 LIRHQRLHTGEKPYKCSECGKSFNQ 610
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-664 1.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.27e-04
                          10        20
                  ....*....|....*....|....
gi 294610662  641 SLMVHQRTHTGEKPYKCKDCMKAF 664
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 599-621 1.88e-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: 38.82  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|...
gi 294610662  599 YKCSECGKSFNQNSHLIIHQRIH 621
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
312-585 2.08e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 312 EDKNSTEDRNEECKDvGVHPEMPSSPVEHQGEAKRQKSYQCDECGKVFSQSSRFLGHQRIHVGERPFECNKCGKTFQQIS 391
Cdd:COG5048  190 SNVSTSIPSSSENSP-LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 392 QLVVHlrihtqekpyecceSGKTYCHSSHliqhqrlRNGDKPYKGNECVRASIQSSQLLVHKRT--HTGE--KPDE---- 463
Cdd:COG5048  269 SSQSS--------------SPNESDSSSE-------KGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFScpys 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610662 464 -SGEAFIWNKSLIQHQVLHISKKLYEC--NECGKAFYTNRN-----LIDHQRIHTGEKPYECI--ECGKSFSRSKCLTRH 533
Cdd:COG5048  328 lCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLH 407

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 294610662 534 QSLHTGEKTY--KCSECGKAFLQNSQLIDHKRVHTGEKPFECSECGKKFSLGKC 585
Cdd:COG5048  408 IITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
670-694 3.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....*
gi 294610662  670 LIVHQRVHTGEKPYECAECGKAFSQ 694
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 597-645 3.51e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 3.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 294610662 597 KPYkCSECGKSFNQNSHLIIHQRIHTgekpYGCNECGKVFSYSSSLMVH 645
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
558-581 4.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.97e-04
                          10        20
                  ....*....|....*....|....
gi 294610662  558 LIDHKRVHTGEKPFECSECGKKFS 581
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 569-621 1.75e-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: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 294610662 569 KPFeCSECGKKFSLGKCLIRHQRLHTgekpYKCSECGKSFNQNSHLIIH-QRIH 621
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 ...
 487-509 2.31e-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: 2.31e-03
                          10        20
                  ....*....|....*....|...
gi 294610662  487 YECNECGKAFYTNRNLIDHQRIH 509
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 683-705 2.58e-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: 2.58e-03
                          10        20
                  ....*....|....*....|...
gi 294610662  683 YECAECGKAFSQRSTFNHHQRIH 705
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 629-649 3.42e-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: 3.42e-03
                          10        20
                  ....*....|....*....|.
gi 294610662  629 CNECGKVFSYSSSLMVHQRTH 649
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
530-554 4.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.27e-03
                          10        20
                  ....*....|....*....|....*
gi 294610662  530 LTRHQSLHTGEKTYKCSECGKAFLQ 554
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
613-638 5.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 294610662  613 HLIIHQRIHTGEKPYGCNECGKVFSY 638
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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