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Conserved domains on  [gi|530374122|ref|XP_005247271|]
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histone-lysine N-methyltransferase MECOM isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 47-204 2.60e-113

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


:

Pssm-ID: 380991  Cd Length: 158  Bit Score: 350.01  E-value: 2.60e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   47 CSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEI 126
Cdd:cd19214     1 SSPATSSEAFTPKEGSPYKAPIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530374122  127 LDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEDYPHETMAPDIH 204
Cdd:cd19214    81 LDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSEDYSHETMAPDIH 158
zf-H2C2_2 pfam13465
Zinc-finger double domain;
927-951 5.27e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|....*
gi 530374122   927 NLTRHLRTHTGEQPYRCKYCDRSFS 951
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 913-935 2.78e-05

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: 41.90  E-value: 2.78e-05
                           10        20
                   ....*....|....*....|...
gi 530374122   913 YTCRYCGKIFPRSANLTRHLRTH 935
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 super family cl26169
hypothetical protein
 846-965 5.83e-05

hypothetical protein


The actual alignment was detected with superfamily member PHA00733:

Pssm-ID: 177301  Cd Length: 128  Bit Score: 44.10  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  846 EKYLRPSPGFLFHPQMsaienmaEKLESFSALKPEASELLQSVPSMFNFRapPNALPEN------LLRKGKERYTCRYCG 919
Cdd:PHA00733   10 KKYLSNHKGIFIHVTL-------EELKRYHSLTPEQKRLIRAVVKTLIYN--PQLLDESsylyklLTSKAVSPYVCPLCL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530374122  920 KIFPRSANLTRHLRThtGEQPYRCKYCDRSFSISSNLQRHVRNIHN 965
Cdd:PHA00733   81 MPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDHVCKKHN 124
zf-H2C2_2 pfam13465
Zinc-finger double domain;
277-301 1.43e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.43e-04
                           10        20
                   ....*....|....*....|....*
gi 530374122   277 SLEKHMLSHTEEREYKCDQCPKAFN 301
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 377-399 6.72e-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: 38.05  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   377 FICEVCHKSYTQFSNLCRHKRMH 399
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 970-992 9.66e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 9.66e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   970 FKCHLCDRCFGQQTNLDRHLKKH 992
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
DUF4045 super family cl38397
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 712-799 6.11e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


The actual alignment was detected with superfamily member pfam13254:

Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.54  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   712 PDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSR---ASGTK 788
Cdd:pfam13254  277 PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQSPPKDFRANLRSRevpKDKSK 356

                           90
                   ....*....|.
gi 530374122   789 LTEPRKNHVFG 799
Cdd:pfam13254  357 KDEPEFKNVFG 367
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 291-313 7.44e-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: 7.44e-03
                           10        20
                   ....*....|....*....|...
gi 530374122   291 YKCDQCPKAFNWKSNLIRHQMSH 313
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-360 9.67e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 530374122   334 NLQRHIRSqHVGARAHACPECGKTFAT 360
Cdd:pfam13465    1 NLKRHMRT-HTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 47-204 2.60e-113

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380991  Cd Length: 158  Bit Score: 350.01  E-value: 2.60e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   47 CSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEI 126
Cdd:cd19214     1 SSPATSSEAFTPKEGSPYKAPIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530374122  127 LDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEDYPHETMAPDIH 204
Cdd:cd19214    81 LDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSEDYSHETMAPDIH 158
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 80-196 4.84e-18

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 81.23  E-value: 4.84e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122     80 FELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRS----NLKDPSYGWEILDEFY----NVKFCIDASqpDVGSWLKYI 151
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITseeaEERPKAYDTDGAKAFYlfdiDSDLCIDAR--RKGNLARFI 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 530374122    152 RFAgCYDQHNLVACQINDQ--IFYRVVADIAPGEELLLFMKSEDYPH 196
Cdd:smart00317   79 NHS-CEPNCELLFVEVNGDdrIVIFALRDIKPGEELTIDYGSDYANE 124
zf-H2C2_2 pfam13465
Zinc-finger double domain;
927-951 5.27e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|....*
gi 530374122   927 NLTRHLRTHTGEQPYRCKYCDRSFS 951
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
80-214 1.69e-05

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 45.72  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   80 FELRESnmPGAGLGIWTKRKIEVGEKFGPYVGE--------QRSNLKDPS--YGWEILDEFYnvkfcIDASqpDVGSWLK 149
Cdd:COG2940     8 IEVRPS--PIHGRGVFATRDIPKGTLIGEYPGEvitwaeaeRREPHKEPLhtYLFELDDDGV-----IDGA--LGGNPAR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  150 YIrfagcydQH----NLVACQINDQIFYRVVADIAPGEELllfmkSEDYphetmAPDIHEER-QYRCEDC 214
Cdd:COG2940    79 FI-------NHscdpNCEADEEDGRIFIVALRDIAAGEEL-----TYDY-----GLDYDEEEyPCRCPNC 131
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 913-935 2.78e-05

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: 41.90  E-value: 2.78e-05
                           10        20
                   ....*....|....*....|...
gi 530374122   913 YTCRYCGKIFPRSANLTRHLRTH 935
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 91-186 4.52e-05

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 44.05  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122    91 GLGIWTKRKIEVGEKFGPYVG------EQRSNLKDPSYGWEILDEFY--------NVKFCIDASQPDVGSWLKYIRfagc 156
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEvllitkEEADKRELLYYDKLELRLWGpylftldeDSEYCIDARALYYGNWARFIN---- 76

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 530374122   157 ydqHN--------LVACQINDQIFYRVVADIAPGEELL 186
Cdd:pfam00856   77 ---HScdpncevrVVYVNGGPRIVIFALRDIKPGEELT 111
PHA00733 PHA00733
hypothetical protein
 846-965 5.83e-05

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 44.10  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  846 EKYLRPSPGFLFHPQMsaienmaEKLESFSALKPEASELLQSVPSMFNFRapPNALPEN------LLRKGKERYTCRYCG 919
Cdd:PHA00733   10 KKYLSNHKGIFIHVTL-------EELKRYHSLTPEQKRLIRAVVKTLIYN--PQLLDESsylyklLTSKAVSPYVCPLCL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530374122  920 KIFPRSANLTRHLRThtGEQPYRCKYCDRSFSISSNLQRHVRNIHN 965
Cdd:PHA00733   81 MPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDHVCKKHN 124
zf-H2C2_2 pfam13465
Zinc-finger double domain;
277-301 1.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.43e-04
                           10        20
                   ....*....|....*....|....*
gi 530374122   277 SLEKHMLSHTEEREYKCDQCPKAFN 301
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 377-399 6.72e-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: 38.05  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   377 FICEVCHKSYTQFSNLCRHKRMH 399
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 970-992 9.66e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 9.66e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   970 FKCHLCDRCFGQQTNLDRHLKKH 992
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
907-952 1.09e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 42.16  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530374122  907 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 952
Cdd:COG3677    11 IRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 941-964 2.93e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.93e-03
                           10        20
                   ....*....|....*....|....
gi 530374122   941 YRCKYCDRSFSISSNLQRHVRnIH 964
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 943-977 3.41e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 3.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530374122  943 CKYCDRSFSISSNLQrhvrnIHNKEKPFKCHLCDR 977
Cdd:cd20908     4 CYYCDREFDDEKILI-----QHQKAKHFKCHICHK 33
ZnF_C2H2 smart00355
zinc finger;
913-935 4.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.85e-03
                            10        20
                    ....*....|....*....|...
gi 530374122    913 YTCRYCGKIFPRSANLTRHLRTH 935
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 712-799 6.11e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.54  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   712 PDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSR---ASGTK 788
Cdd:pfam13254  277 PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQSPPKDFRANLRSRevpKDKSK 356

                           90
                   ....*....|.
gi 530374122   789 LTEPRKNHVFG 799
Cdd:pfam13254  357 KDEPEFKNVFG 367
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 291-313 7.44e-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: 7.44e-03
                           10        20
                   ....*....|....*....|...
gi 530374122   291 YKCDQCPKAFNWKSNLIRHQMSH 313
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-360 9.67e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 530374122   334 NLQRHIRSqHVGARAHACPECGKTFAT 360
Cdd:pfam13465    1 NLKRHMRT-HTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 47-204 2.60e-113

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380991  Cd Length: 158  Bit Score: 350.01  E-value: 2.60e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   47 CSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEI 126
Cdd:cd19214     1 SSPATSSEAFTPKEGSPYKAPIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530374122  127 LDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEDYPHETMAPDIH 204
Cdd:cd19214    81 LDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSEDYSHETMAPDIH 158
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 67-201 1.91e-86

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus protein and similar proteins; PRDM16 (also termed PR domain-containing protein 16, transcription factor MEL1, or MDS1/EVI1-like gene 1) functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells. It is closely related to paralog of PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) which is a nuclear transcription factor essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). PRDM3 and PRDM16 are both directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380977  Cd Length: 135  Bit Score: 276.17  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   67 PIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGS 146
Cdd:cd19200     1 PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEFGKVKFWIDASEPGTGN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530374122  147 WLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEDYPHETMAP 201
Cdd:cd19200    81 WMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETMPP 135
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 57-201 5.87e-77

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, also termed PR domain-containing protein 16, or transcription factor MEL1, or MDS1/EVI1-like gene 1, functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells and is closely related to paralog of PRDM3, both of which are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380990  Cd Length: 162  Bit Score: 250.95  E-value: 5.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   57 TPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEIL--------- 127
Cdd:cd19213     1 TPKEGSPYEAPVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQIlndvevssq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  128 --------DEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEDYPHETM 199
Cdd:cd19213    81 egcitkivDDLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKDGVYPLGTM 160


                  ..
gi 530374122  200 AP 201
Cdd:cd19213   161 PP 162
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 73-193 2.46e-35

PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 (also termed GATA-3-binding protein G3B, lysine N-methyltransferase 8, MTB-or MTE-binding protein, PR domain-containing protein 2, retinoblastoma protein-interacting zinc finger protein, or zinc finger protein RIZ) is S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. It may function as a DNA-binding transcription factor.


Pssm-ID: 380965  Cd Length: 123  Bit Score: 130.64  E-value: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   73 DIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQ--RSNLKDPSYGWEILdeFYNVK-FCIDASQPDVGSWLK 149
Cdd:cd19188     1 LMGLPEELELKPSAVDKTRIGVWAKKSIPKGRKFGPFVGEKkkRSQVKNNVYMWEIY--GPKRGwMCVDASDPTKGNWLR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530374122  150 YIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSED 193
Cdd:cd19188    79 YVNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGED 122
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 76-186 9.33e-32

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 120.80  E-value: 9.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGE--QRSNLKDPSYGWEIlDEFYNVKFCIDASQPDVGSWLKYIRF 153
Cdd:cd19193     4 LPPGLSIKRSSIPGAGLGVWAEAPIPKGMVFGPYEGEivEDEEAADSGYSWQI-YKGGKLSHYIDAKDESKSNWMRYVNC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530374122  154 AGCYDQHNLVACQINDQIFYRVVADIAPGEELL 186
Cdd:cd19193    83 ARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELL 115
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 76-188 1.73e-23

PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family of proteins is defined based on the conserved N-terminal PR domain, which is closely related to the Su(var)3-9, enhancer of zeste, and trithorax (SET) domains of histone methyltransferases, and is specifically called PR-SET domain. The family consists of 17 members in primates. PRDMs play diverse roles in cell-cycle regulation, differentiation, and meiotic recombination. The family also contains zinc finger protein ZFPM1 and ZFPM2. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380932  Cd Length: 83  Bit Score: 95.34  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQrsnlkdpsygweildefynvkfcidasqpdvgSWLKYIRFAG 155
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFARRTIPAGTRFGPLEGVV--------------------------------NWMRFVRPAR 48

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530374122  156 CYDQHNLVACQINDQIFYRVVADIAPGEELLLF 188
Cdd:cd10534    49 NEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVW 81
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 76-186 1.72e-21

PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 (also termed PR domain-containing protein 12) acts as a transcription factor that is involved in the positive regulation of histone H3-K9 dimethylation.


Pssm-ID: 380973 [Multi-domain]  Cd Length: 130  Bit Score: 91.26  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVG-----EQRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGSWLKY 150
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVFSKTWIKEGTEMGPYTGrivspEDVDPCKNNNLMWEVFNEDGTVSHFIDASQENHRSWMTF 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530374122  151 IRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELL 186
Cdd:cd19196    81 VNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELL 116
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 75-188 4.61e-20

PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380978  Cd Length: 122  Bit Score: 87.01  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   75 PIPAEFELRESNMPGAGL-GIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGSWLKYIRF 153
Cdd:cd19201     2 SLPGELELRKPSQDAGRSgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAQGSKGGEGLLLLTEDSGTWLKLVRS 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530374122  154 AGCYDQHNLVACQINDQIFYRVVADIAPGEELLLF 188
Cdd:cd19201    82 ADDEDEANLILYFKGGQIWCEVTKDIPPGEELILV 116
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 76-188 6.06e-20

PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro.


Pssm-ID: 380968  Cd Length: 128  Bit Score: 86.76  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVG------EQRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGSWLK 149
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGvlvspeKQIGAVRNTQHLWEIYDQEGTLQHFIDGGDPSKSSWMR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530374122  150 YIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLF 188
Cdd:cd19191    81 YIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVW 119
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 68-187 2.09e-19

PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 (also termed PR domain-containing protein 5) is a sequence-specific DNA-binding transcription factor that represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.


Pssm-ID: 380967  Cd Length: 127  Bit Score: 85.42  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   68 IYIPDdipipaEFELRESNMPGaGLGIWTKRKIEVGEKFGPYVGEQRSNLK-----DPSYGWEILDEFYNVKFCIDASQP 142
Cdd:cd19190     3 MYVPD------RFSLKSSKVQD-GMGLYTARRVKKGEKFGPFAGEKRMPNEldesmDPRLMWEVRGSKGEVLYILDASNP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530374122  143 DVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLL 187
Cdd:cd19190    76 RHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLI 120
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 80-196 4.84e-18

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 81.23  E-value: 4.84e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122     80 FELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRS----NLKDPSYGWEILDEFY----NVKFCIDASqpDVGSWLKYI 151
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITseeaEERPKAYDTDGAKAFYlfdiDSDLCIDAR--RKGNLARFI 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 530374122    152 RFAgCYDQHNLVACQINDQ--IFYRVVADIAPGEELLLFMKSEDYPH 196
Cdd:smart00317   79 NHS-CEPNCELLFVEVNGDdrIVIFALRDIKPGEELTIDYGSDYANE 124
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 92-186 1.74e-17

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 80.06  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   92 LGIWTKRKIEVGEKFGPYVGEQRSNLKDPS-----YGWEILDEFYNVKFcIDASQPDVGSWLKYIRFAGCYDQHNLVACQ 166
Cdd:cd19187    19 LGVWSSDYIPRGTRFGPLVGEIYTNDPVPKganrkYFWRIYSNGEFYHY-IDGFDPSKSNWMRYVNPAHSLQEQNLVACQ 97

                          90       100
                  ....*....|....*....|
gi 530374122  167 INDQIFYRVVADIAPGEELL 186
Cdd:cd19187    98 IGMNIYFYTVKPIPPNQELL 117
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 76-194 2.47e-15

PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 (also termed PR domain-containing protein 4, or PFM1) may function as a transcription factor involved in cell differentiation.


Pssm-ID: 380966  Cd Length: 133  Bit Score: 74.04  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELRESNMpGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEILDEFYNV------KFCIDASQPDVGSWLK 149
Cdd:cd19189     6 LPRQLYLRQSET-GAEVGVWTKETIPVRTCFGPLIGQQSHSAEVADWTDKAAPHIWKIyhndvlEFCIITTDENECNWMM 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530374122  150 YIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEElLLFMKSEDY 194
Cdd:cd19189    85 FVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQE-LLFYYSRDY 128
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 93-186 2.22e-12

PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance.


Pssm-ID: 380975  Cd Length: 133  Bit Score: 65.50  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   93 GIWTKRKIEVGEKFGPYVGE--QRSNLK---DPSYGWEILDEFYNVKFcIDAsQPDVGSWLKYIRFAGCYDQHNLVACQI 167
Cdd:cd19198    21 GVFCKKTIPKGTRFGPFRGRvvNTSEIKtydDNSFMWEIFEDGKLSHF-IDG-RGSTGNWMSYVNCARYAEEQNLIAIQC 98

                          90
                  ....*....|....*....
gi 530374122  168 NDQIFYRVVADIAPGEELL 186
Cdd:cd19198    99 QGQIFYESCKEILQGQELL 117
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 92-185 9.81e-12

PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 (also termed PR domain-containing protein 10, or tristanin) may be involved in transcriptional regulation.


Pssm-ID: 380971  Cd Length: 128  Bit Score: 63.52  E-value: 9.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   92 LGIWTKRKIEVGEKFGPYVGE--QRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQIND 169
Cdd:cd19194    20 GGVFAKRRIPKRTQFGPLEGPlvKKSELKDNKIHPLELEEDDGEDLYFDLSDENKCNWMMFVRPAQNHLEQNLVAYQYGQ 99

                          90
                  ....*....|....*.
gi 530374122  170 QIFYRVVADIAPGEEL 185
Cdd:cd19194   100 EIYFTTIKNIEPKQEL 115
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 99-194 6.97e-10

PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 (also termed PR domain-containing protein 11) may be involved in transcription regulation.


Pssm-ID: 380972  Cd Length: 127  Bit Score: 57.94  E-value: 6.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   99 KIEVGEKFGPYVGEQRSNLKDPS-YGWEILDEFYNVKFcIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVA 177
Cdd:cd19195    27 VIPKGHIFGPYEGQICTQDKSSGfFSWLIVDKNNRYKS-IDGSDETKANWMRYVVISREEREQNLLAFQHSEQIYFRACR 105

                          90
                  ....*....|....*..
gi 530374122  178 DIAPGEELLLFMkSEDY 194
Cdd:cd19195   106 DIRPGEKLRVWY-SEDY 121
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 76-185 1.02e-09

PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 (also termed PR domain-containing protein 15, or zinc finger protein 298 (ZNF298)) may be involved in transcriptional regulation. It plays an essential role as a chromatin factor that modulates the transcription of upstream regulators of WNT and MAPK-ERK signaling to safeguard naive pluripotency.


Pssm-ID: 380976  Cd Length: 126  Bit Score: 57.42  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   76 IPAEFELResNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEILDEFYNVKFCIDASQPDVGSWLKYIRFAG 155
Cdd:cd19199     7 LPDNLEIR--QLEDGSEGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVVYLDTSNEDDCNWMMFVRPAT 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 530374122  156 CYDQHNLVACQINDQIFYRVVADIAPGEEL 185
Cdd:cd19199    85 DVEHQNLTAYQQGEDIYFTTSRDIQPGAEL 114
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 85-187 1.67e-07

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 51.19  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   85 SNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLK---DPSYGWEILDEFYNVKFC--IDASQpdVGSWLKYIRFAgcyDQ 159
Cdd:cd10522     8 PNLSHNGLGLFAAETIAKGEFVGEYTGEVLDRWEedrDSVYHYDPLYPFDLNGDIlvIDAGK--KGNLTRFINHS---DQ 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 530374122  160 HNLVACQINDQ----IFYRVVADIAPGEELLL 187
Cdd:cd10522    83 PNLELIVRTLKgeqhIGFVAIRDIKPGEELFI 114
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 100-188 2.17e-06

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


Pssm-ID: 380974  Cd Length: 103  Bit Score: 47.51  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  100 IEVGEKFGPY-----VGEQRSNLKDPsyGWEILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQ--INDQIF 172
Cdd:cd19197     1 IPAGLRLGPVpgifkLGKYLSDRKEP--GNKKKVRRVRGDYLVDESGSPATEWIGLVRAARNNQEQNLEAIAdlPGGQIF 78

                          90
                  ....*....|....*.
gi 530374122  173 YRVVADIAPGEELLLF 188
Cdd:cd19197    79 YRALRDIQPGEELTVW 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
927-951 5.27e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|....*
gi 530374122   927 NLTRHLRTHTGEQPYRCKYCDRSFS 951
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 89-187 5.28e-06

PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 (also termed zinc finger protein 408 (ZNF408)) may be involved in transcriptional regulation.


Pssm-ID: 380918  Cd Length: 121  Bit Score: 46.64  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   89 GAGLGIW-TKRKIEVGEKFGPYVGEQRSNLKDPsygwEILDEFYNVKFCIDASQP-DVGSWLKYIRFAGCYDQHNLVACQ 166
Cdd:cd10520    18 EERLGVWcVGDALQKGTFLGPLEEELESHDLTE----GGSPRQEESGQSGDVLACeQSSKWMRFACRARSEEESNVAVVR 93

                          90       100
                  ....*....|....*....|.
gi 530374122  167 INDQIFYRVVADIAPGEELLL 187
Cdd:cd10520    94 LSGRLHLRVCKDIEPGSELLL 114
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
80-214 1.69e-05

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 45.72  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   80 FELRESnmPGAGLGIWTKRKIEVGEKFGPYVGE--------QRSNLKDPS--YGWEILDEFYnvkfcIDASqpDVGSWLK 149
Cdd:COG2940     8 IEVRPS--PIHGRGVFATRDIPKGTLIGEYPGEvitwaeaeRREPHKEPLhtYLFELDDDGV-----IDGA--LGGNPAR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  150 YIrfagcydQH----NLVACQINDQIFYRVVADIAPGEELllfmkSEDYphetmAPDIHEER-QYRCEDC 214
Cdd:COG2940    79 FI-------NHscdpNCEADEEDGRIFIVALRDIAAGEEL-----TYDY-----GLDYDEEEyPCRCPNC 131
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 913-935 2.78e-05

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: 41.90  E-value: 2.78e-05
                           10        20
                   ....*....|....*....|...
gi 530374122   913 YTCRYCGKIFPRSANLTRHLRTH 935
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 91-186 4.52e-05

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 44.05  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122    91 GLGIWTKRKIEVGEKFGPYVG------EQRSNLKDPSYGWEILDEFY--------NVKFCIDASQPDVGSWLKYIRfagc 156
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEvllitkEEADKRELLYYDKLELRLWGpylftldeDSEYCIDARALYYGNWARFIN---- 76

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 530374122   157 ydqHN--------LVACQINDQIFYRVVADIAPGEELL 186
Cdd:pfam00856   77 ---HScdpncevrVVYVNGGPRIVIFALRDIKPGEELT 111
PHA00733 PHA00733
hypothetical protein
 846-965 5.83e-05

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 44.10  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122  846 EKYLRPSPGFLFHPQMsaienmaEKLESFSALKPEASELLQSVPSMFNFRapPNALPEN------LLRKGKERYTCRYCG 919
Cdd:PHA00733   10 KKYLSNHKGIFIHVTL-------EELKRYHSLTPEQKRLIRAVVKTLIYN--PQLLDESsylyklLTSKAVSPYVCPLCL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530374122  920 KIFPRSANLTRHLRThtGEQPYRCKYCDRSFSISSNLQRHVRNIHN 965
Cdd:PHA00733   81 MPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDHVCKKHN 124
zf-H2C2_2 pfam13465
Zinc-finger double domain;
277-301 1.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.43e-04
                           10        20
                   ....*....|....*....|....*
gi 530374122   277 SLEKHMLSHTEEREYKCDQCPKAFN 301
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 377-399 6.72e-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: 38.05  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   377 FICEVCHKSYTQFSNLCRHKRMH 399
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 970-992 9.66e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 9.66e-04
                           10        20
                   ....*....|....*....|...
gi 530374122   970 FKCHLCDRCFGQQTNLDRHLKKH 992
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
907-952 1.09e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 42.16  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530374122  907 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 952
Cdd:COG3677    11 IRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 941-964 2.93e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.93e-03
                           10        20
                   ....*....|....*....|....
gi 530374122   941 YRCKYCDRSFSISSNLQRHVRnIH 964
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 943-977 3.41e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 3.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530374122  943 CKYCDRSFSISSNLQrhvrnIHNKEKPFKCHLCDR 977
Cdd:cd20908     4 CYYCDREFDDEKILI-----QHQKAKHFKCHICHK 33
ZnF_C2H2 smart00355
zinc finger;
913-935 4.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.85e-03
                            10        20
                    ....*....|....*....|...
gi 530374122    913 YTCRYCGKIFPRSANLTRHLRTH 935
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 712-799 6.11e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.54  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374122   712 PDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSR---ASGTK 788
Cdd:pfam13254  277 PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQSPPKDFRANLRSRevpKDKSK 356

                           90
                   ....*....|.
gi 530374122   789 LTEPRKNHVFG 799
Cdd:pfam13254  357 KDEPEFKNVFG 367
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 291-313 7.44e-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: 7.44e-03
                           10        20
                   ....*....|....*....|...
gi 530374122   291 YKCDQCPKAFNWKSNLIRHQMSH 313
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 915-968 8.40e-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: 36.38  E-value: 8.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530374122  915 CRYCGKIFPRSANLTRHLRTHTgeqpYRCKYCDRSFSISSNLQRHVRNIHnKEK 968
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVH-KET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-360 9.67e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 530374122   334 NLQRHIRSqHVGARAHACPECGKTFAT 360
Cdd:pfam13465    1 NLKRHMRT-HTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 344-396 9.94e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 9.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530374122  344 VGARAHACP--ECGKTFATSSGLKQHK-HIHSSV------------------KPFICEVCHKSYTQFSNLCRHK 396
Cdd:COG5189   345 KDGKPYKCPveGCNKKYKNQNGLKYHMlHGHQNQklhenpspekmnifsakdKPYRCEVCDKRYKNLNGLKYHR 418
 
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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