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Conserved domains on  [gi|568931886|ref|XP_006539235|]
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histone-lysine N-methyltransferase PRDM16 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 61-222 7.33e-107

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: 333.38  E-value: 7.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   61 TPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDTEVSSQ 140
Cdd:cd19213     1 TPKEGSPYEAPVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQILNDVEVSSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  141 ESCIKKISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVM 220
Cdd:cd19213    81 EGCITKIVDDLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKDGVYPLGTM 160


                  ..
gi 568931886  221 AP 222
Cdd:cd19213   161 PP 162
zf-H2C2_2 pfam13465
Zinc-finger double domain;
966-990 2.83e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.83e-06
                           10        20
                   ....*....|....*....|....*
gi 568931886   966 NLTRHLRTHTGEQPYRCKYCDRSFS 990
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 952-974 1.57e-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: 42.67  E-value: 1.57e-05
                           10        20
                   ....*....|....*....|...
gi 568931886   952 YTCRYCGKIFPRSANLTRHLRTH 974
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-320 8.57e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 8.57e-05
                           10        20
                   ....*....|....*....|....*
gi 568931886   296 SLEQHMIVHTEEREYKCDQCPKAFN 320
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 982-1016 2.59e-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.


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 41.00  E-value: 2.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568931886  982 CKYCDRSFSISSNLQrhvrnIHNKEKPFKCHLCNR 1016
Cdd:cd20908     4 CYYCDREFDDEKILI-----QHQKAKHFKCHICHK 33
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 395-417 4.18e-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: 4.18e-04
                           10        20
                   ....*....|....*....|...
gi 568931886   395 FICEVCHKSYTQFSNLCRHKRMH 417
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1009-1031 8.73e-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: 8.73e-04
                           10        20
                   ....*....|....*....|...
gi 568931886  1009 FKCHLCNRCFGQQTNLDRHLKKH 1031
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 367-389 1.22e-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: 37.28  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   367 HACPDCGKTFATSSGLKQHKHIH 389
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 1.65e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   282 HECKDCERMFPNKYSLEQHMIVH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-359 1.84e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|..
gi 568931886   338 FECENCVKVFTDPSNLQRHIRS 359
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 310-332 4.72e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 4.72e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   310 YKCDQCPKAFNWKSNLIRHQMSH 332
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 61-222 7.33e-107

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: 333.38  E-value: 7.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   61 TPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDTEVSSQ 140
Cdd:cd19213     1 TPKEGSPYEAPVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQILNDVEVSSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  141 ESCIKKISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVM 220
Cdd:cd19213    81 EGCITKIVDDLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKDGVYPLGTM 160


                  ..
gi 568931886  221 AP 222
Cdd:cd19213   161 PP 162
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 84-209 1.90e-10

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: 59.66  E-value: 1.90e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886     84 FELRESSIPGAGLGIWAKRKMEIGERFGPYV--VTPRAALKEADfgwEQMLTDTEVSSQESCIKkisedlgsEKFCVDAn 161
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVgeIITSEEAEERP---KAYDTDGAKAFYLFDID--------SDLCIDA- 68

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568931886    162 qAGSGSWLKYIRVACSCDDQNLAMCQINE-QIYYKVIKDIEPGEELLVH 209
Cdd:smart00317   69 -RRKGNLARFINHSCEPNCELLFVEVNGDdRIVIFALRDIKPGEELTID 116
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 95-209 3.39e-08

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: 52.91  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886    95 GLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDTEVSSQESCIKKISEDlgsEKFCVDANQAGSGSWLKYIRV 174
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLWGPYLFTLDED---SEYCIDARALYYGNWARFINH 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568931886   175 ACscdDQNLAM----CQINEQIYYKVIKDIEPGEELLVH 209
Cdd:pfam00856   78 SC---DPNCEVrvvyVNGGPRIVIFALRDIKPGEELTID 113
zf-H2C2_2 pfam13465
Zinc-finger double domain;
966-990 2.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.83e-06
                           10        20
                   ....*....|....*....|....*
gi 568931886   966 NLTRHLRTHTGEQPYRCKYCDRSFS 990
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 952-974 1.57e-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: 42.67  E-value: 1.57e-05
                           10        20
                   ....*....|....*....|...
gi 568931886   952 YTCRYCGKIFPRSANLTRHLRTH 974
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-320 8.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 8.57e-05
                           10        20
                   ....*....|....*....|....*
gi 568931886   296 SLEQHMIVHTEEREYKCDQCPKAFN 320
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 982-1016 2.59e-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: 41.00  E-value: 2.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568931886  982 CKYCDRSFSISSNLQrhvrnIHNKEKPFKCHLCNR 1016
Cdd:cd20908     4 CYYCDREFDDEKILI-----QHQKAKHFKCHICHK 33
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 395-417 4.18e-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: 4.18e-04
                           10        20
                   ....*....|....*....|...
gi 568931886   395 FICEVCHKSYTQFSNLCRHKRMH 417
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
932-1004 6.12e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 6.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931886  932 NFRSPPPTLSDPILRKGKERYT-CRYCGKIFPRSANLTRHLRTHTGEQPYRCKY--CDRSFSISSNLQRHVRNIHN 1004
Cdd:COG5048    13 NSVLSSTPKSTLKSLSNAPRPDsCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1009-1031 8.73e-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: 8.73e-04
                           10        20
                   ....*....|....*....|...
gi 568931886  1009 FKCHLCNRCFGQQTNLDRHLKKH 1031
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
946-991 1.13e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 42.16  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568931886  946 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 991
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 ...
 367-389 1.22e-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: 37.28  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   367 HACPDCGKTFATSSGLKQHKHIH 389
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 1.65e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   282 HECKDCERMFPNKYSLEQHMIVH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 980-1003 1.75e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.75e-03
                           10        20
                   ....*....|....*....|....
gi 568931886   980 YRCKYCDRSFSISSNLQRHVRnIH 1003
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-359 1.84e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|..
gi 568931886   338 FECENCVKVFTDPSNLQRHIRS 359
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
ZnF_C2H2 smart00355
zinc finger;
952-974 2.90e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.90e-03
                            10        20
                    ....*....|....*....|...
gi 568931886    952 YTCRYCGKIFPRSANLTRHLRTH 974
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 310-332 4.72e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 4.72e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   310 YKCDQCPKAFNWKSNLIRHQMSH 332
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 61-222 7.33e-107

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: 333.38  E-value: 7.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   61 TPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDTEVSSQ 140
Cdd:cd19213     1 TPKEGSPYEAPVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQILNDVEVSSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  141 ESCIKKISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVM 220
Cdd:cd19213    81 EGCITKIVDDLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKDGVYPLGTM 160


                  ..
gi 568931886  221 AP 222
Cdd:cd19213   161 PP 162
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 71-222 4.60e-72

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: 236.11  E-value: 4.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   71 PVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDtevssqescikkised 150
Cdd:cd19200     1 PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEF---------------- 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931886  151 lGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAP 222
Cdd:cd19200    65 -GKVKFWIDASEPGTGNWMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETMPP 135
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 52-224 2.65e-65

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: 217.88  E-value: 2.65e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   52 SPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEqm 131
Cdd:cd19214     2 SPATSSEAFTPKEGSPYKAPIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  132 ltdtevssqescikkISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVK 211
Cdd:cd19214    80 ---------------VLDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMK 144

                         170
                  ....*....|...
gi 568931886  212 EGAYSLGVMAPSL 224
Cdd:cd19214   145 SEDYSHETMAPDI 157
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 80-208 1.07e-27

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: 109.25  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYV--VTPRAALKEADFGWEqmltdtevssqescikkISEDLGSeKFC 157
Cdd:cd19193     4 LPPGLSIKRSSIPGAGLGVWAEAPIPKGMVFGPYEgeIVEDEEAADSGYSWQ-----------------IYKGGKL-SHY 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568931886  158 VDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19193    66 IDAKDESKSNWMRYVNCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLV 116
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 77-208 3.93e-25

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: 101.75  E-value: 3.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   77 DIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYV--VTPRAALKEADFGWEqmltdtevssqescikKISEDLGSe 154
Cdd:cd19188     1 LMGLPEELELKPSAVDKTRIGVWAKKSIPKGRKFGPFVgeKKKRSQVKNNVYMWE----------------IYGPKRGW- 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568931886  155 kFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19188    64 -MCVDASDPTKGNWLRYVNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLC 116
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 80-209 2.95e-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: 94.57  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVvtpraalkeadfgweqmltdtevssqescikkisedlgsekfcvd 159
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFARRTIPAGTRFGPLE--------------------------------------------- 35

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568931886  160 anqaGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVH 209
Cdd:cd10534    36 ----GVVNWMRFVRPARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVW 81
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 80-208 1.40e-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: 91.65  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGAGLGIWAKRKMEIGERFGPY---VVTPR--AALKEADFGWEQMLTDTEVSsqescikkisedlgse 154
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVFSKTWIKEGTEMGPYtgrIVSPEdvDPCKNNNLMWEVFNEDGTVS---------------- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568931886  155 kFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19196    65 -HFIDASQENHRSWMTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLV 117
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 79-212 5.67e-18

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: 81.24  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   79 PIPPDFELRESSIPGAGL-GIWAKRKMEIGERFGPYvvtpraalkeadfgwEQMLTDTEVSSQESCIKKISEDLGSEKFC 157
Cdd:cd19201     2 SLPGELELRKPSQDAGRSgGVWAKQPLPEGTRFGPY---------------PGKLVKEPLDPSYEWKVEAQGSKGGEGLL 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568931886  158 VDANqaGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKE 212
Cdd:cd19201    67 LLTE--DSGTWLKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLRE 119
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 80-208 3.63e-16

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: 76.36  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGAGLGIWAKRKMEIGERFGPY--VVTPR----AALKEADFGWEqmltdtevssqescikkISEDLGS 153
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFegVLVSPekqiGAVRNTQHLWE-----------------IYDQEGT 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568931886  154 EKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19191    64 LQHFIDGGDPSKSSWMRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLV 118
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 80-208 3.80e-12

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: 64.62  E-value: 3.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGaGLGIWAKRKMEIGERFGPYVvtpraalkeadfGWEQMLTDTEVSSQESCIKKISEDLGSEKFCVD 159
Cdd:cd19190     5 VPDRFSLKSSKVQD-GMGLYTARRVKKGEKFGPFA------------GEKRMPNELDESMDPRLMWEVRGSKGEVLYILD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568931886  160 ANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19190    72 ASNPRHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLI 120
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 80-208 2.80e-11

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: 62.05  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELREssIPGAGLGIWAKRKMEIGERFGPYVVTPRAAL-KEADFGWEQMLTDTEVSsqesCIKKISEDLgsekfCv 158
Cdd:cd19199     7 LPDNLEIRQ--LEDGSEGVFALVPLVKRTQFGPFEAKRVARLdGFAVFPLKVFEKDGSVV----YLDTSNEDD-----C- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568931886  159 danqagsgSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19199    75 --------NWMMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRV 116
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 81-208 4.14e-11

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: 61.57  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   81 PPDFELRESSIPGAGLGIWAKRKMEIGERFGPYV-------VTPRAAlkEADFGWeqmltdtevssqescikKISEDlGS 153
Cdd:cd19187     4 PRNLTLKYSSVGREVLGVWSSDYIPRGTRFGPLVgeiytndPVPKGA--NRKYFW-----------------RIYSN-GE 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568931886  154 EKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19187    64 FYHYIDGFDPSKSNWMRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLV 118
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 84-209 1.90e-10

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: 59.66  E-value: 1.90e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886     84 FELRESSIPGAGLGIWAKRKMEIGERFGPYV--VTPRAALKEADfgwEQMLTDTEVSSQESCIKkisedlgsEKFCVDAn 161
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVgeIITSEEAEERP---KAYDTDGAKAFYLFDID--------SDLCIDA- 68

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568931886    162 qAGSGSWLKYIRVACSCDDQNLAMCQINE-QIYYKVIKDIEPGEELLVH 209
Cdd:smart00317   69 -RRKGNLARFINHSCEPNCELLFVEVNGDdRIVIFALRDIKPGEELTID 116
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 80-208 7.11e-10

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: 58.24  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELReSSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADfgWeqmlTDTEVSSqescIKKISEDlGSEKFCVD 159
Cdd:cd19189     6 LPRQLYLR-QSETGAEVGVWTKETIPVRTCFGPLIGQQSHSAEVAD--W----TDKAAPH----IWKIYHN-DVLEFCII 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568931886  160 ANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19189    74 TTDENECNWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLF 122
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 73-208 8.52e-10

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: 58.18  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   73 YIPEDIPIppdFELRESSIPGAGlgIWAKRKMEIGERFGPY---VVTPrAALKEAD---FGWEqmltdtevssqescikk 146
Cdd:cd19198     2 DLPEGLRV---LQTSFGGTPHYG--VFCKKTIPKGTRFGPFrgrVVNT-SEIKTYDdnsFMWE----------------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931886  147 ISEDlGSEKFCVDAnQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19198    59 IFED-GKLSHFIDG-RGSTGNWMSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLV 118
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 96-208 1.45e-08

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: 54.28  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   96 LGIWAKRKMEIGERFGPYVvtprAALkeadfgweqmltdteVSSQESCIKKISEDL----GSEKFCVDANQAGSGSWLKY 171
Cdd:cd19194    20 GGVFAKRRIPKRTQFGPLE----GPL---------------VKKSELKDNKIHPLEleedDGEDLYFDLSDENKCNWMMF 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568931886  172 IRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19194    81 VRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKV 117
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 80-208 2.83e-08

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: 53.19  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   80 IPPDFELRESSIPGAGLGIW-AKRKMEIGERFGPYvvtpraalkeadfgwEQMLTDTEVSSQESCIKKISEDLGSEKFCV 158
Cdd:cd10520     5 LPPGLALGPSLAQEERLGVWcVGDALQKGTFLGPL---------------EEELESHDLTEGGSPRQEESGQSGDVLACE 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568931886  159 DanqagSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd10520    70 Q-----SSKWMRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLL 114
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 95-209 3.39e-08

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: 52.91  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886    95 GLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEQMLTDTEVSSQESCIKKISEDlgsEKFCVDANQAGSGSWLKYIRV 174
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLWGPYLFTLDED---SEYCIDARALYYGNWARFINH 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568931886   175 ACscdDQNLAM----CQINEQIYYKVIKDIEPGEELLVH 209
Cdd:pfam00856   78 SC---DPNCEVrvvyVNGGPRIVIFALRDIKPGEELTID 113
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 137-208 2.41e-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: 2.41e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931886  137 VSSQESCIKKISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQ--INEQIYYKVIKDIEPGEELLV 208
Cdd:cd19197    20 LSDRKEPGNKKKVRRVRGDYLVDESGSPATEWIGLVRAARNNQEQNLEAIAdlPGGQIFYRALRDIQPGEELTV 93
zf-H2C2_2 pfam13465
Zinc-finger double domain;
966-990 2.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.83e-06
                           10        20
                   ....*....|....*....|....*
gi 568931886   966 NLTRHLRTHTGEQPYRCKYCDRSFS 990
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 952-974 1.57e-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: 42.67  E-value: 1.57e-05
                           10        20
                   ....*....|....*....|...
gi 568931886   952 YTCRYCGKIFPRSANLTRHLRTH 974
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 158-208 5.73e-05

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: 44.08  E-value: 5.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568931886  158 VDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19195    65 IDGSDETKANWMRYVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRV 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-320 8.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 8.57e-05
                           10        20
                   ....*....|....*....|....*
gi 568931886   296 SLEQHMIVHTEEREYKCDQCPKAFN 320
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 982-1016 2.59e-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: 41.00  E-value: 2.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568931886  982 CKYCDRSFSISSNLQrhvrnIHNKEKPFKCHLCNR 1016
Cdd:cd20908     4 CYYCDREFDDEKILI-----QHQKAKHFKCHICHK 33
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 395-417 4.18e-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: 4.18e-04
                           10        20
                   ....*....|....*....|...
gi 568931886   395 FICEVCHKSYTQFSNLCRHKRMH 417
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
932-1004 6.12e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 6.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931886  932 NFRSPPPTLSDPILRKGKERYT-CRYCGKIFPRSANLTRHLRTHTGEQPYRCKY--CDRSFSISSNLQRHVRNIHN 1004
Cdd:COG5048    13 NSVLSSTPKSTLKSLSNAPRPDsCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1009-1031 8.73e-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: 8.73e-04
                           10        20
                   ....*....|....*....|...
gi 568931886  1009 FKCHLCNRCFGQQTNLDRHLKKH 1031
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
946-991 1.13e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 42.16  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568931886  946 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 991
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 ...
 367-389 1.22e-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: 37.28  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   367 HACPDCGKTFATSSGLKQHKHIH 389
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 89-209 1.41e-03

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: 40.02  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886   89 SSIPGA---GLGIWAKRKMEIGERFGPYVVTPRAALKEadfgwEQMLTDTEVSSQEScikkiseDLGSEKFCVDANQAGS 165
Cdd:cd10522     5 SMIPNLshnGLGLFAAETIAKGEFVGEYTGEVLDRWEE-----DRDSVYHYDPLYPF-------DLNGDILVIDAGKKGN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568931886  166 gsWLKYIRvacSCDDQNLAMCQI----NEQIYYKVIKDIEPGEELLVH 209
Cdd:cd10522    73 --LTRFIN---HSDQPNLELIVRtlkgEQHIGFVAIRDIKPGEELFIS 115
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 1.65e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   282 HECKDCERMFPNKYSLEQHMIVH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 980-1003 1.75e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.75e-03
                           10        20
                   ....*....|....*....|....
gi 568931886   980 YRCKYCDRSFSISSNLQRHVRnIH 1003
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-359 1.84e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|..
gi 568931886   338 FECENCVKVFTDPSNLQRHIRS 359
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
276-416 2.84e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  276 GSDGQAHEC--KDCERMFPNKYSLEQHMIVHTEEREYKC--DQCPKAFNWKSNLIRHQMSHDS-----GKRFECE--NCV 344
Cdd:COG5048   316 GESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYkdlknDKKSETLsnSCI 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931886  345 KVFTDPSNLQRHiRSQHVGARAHAC--PDCGKTFATSSGLKQHKHIHSTVKPFICEvCHKSYTQFSNLCRHKRM 416
Cdd:COG5048   396 RNFKRDSNLSLH-IITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCS-ILKSFRRDLDLSNHGKD 467
ZnF_C2H2 smart00355
zinc finger;
952-974 2.90e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.90e-03
                            10        20
                    ....*....|....*....|...
gi 568931886    952 YTCRYCGKIFPRSANLTRHLRTH 974
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-417 3.41e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  336 KRFECENCVKVFTDPSNLQRHIRSQHV---GARAHACP--DCGKTFATSSGLKQHKHIHSTVKPFIC--EVCHKSYTQFS 408
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSVNHsgeSLKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367


                  ....*....
gi 568931886  409 NLCRHKRMH 417
Cdd:COG5048   368 NNEPPQSLQ 376
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 159-208 3.99e-03

PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 (also termed PR domain-containing protein 8) may function as histone methyltransferase, preferentially acting on 'Lys-9' of histone H3.


Pssm-ID: 380969  Cd Length: 131  Bit Score: 38.95  E-value: 3.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568931886  159 DANQAGSGS-WLKYIRVACSCDDQNL-AMCQINEQIYYKVIKDIEPGEELLV 208
Cdd:cd19192    70 ACNGSSEPSdWLRLVQPARDRHEQNLeAFRKNEGQVYFRTLRRIRKGEELLV 121
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 321-414 4.61e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931886  321 WKSNLIRHQMSHDSGKrfECENCVKVFTDPSNLQRHIRSQH-----VGARAHACP--DCGKTFATSSGLKQHK-HIHSTV 392
Cdd:COG5189   301 IRGGISTGEMIDVRKL--PCTNSSSNGKLAHGGERNIDTPSrmlkvKDGKPYKCPveGCNKKYKNQNGLKYHMlHGHQNQ 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568931886  393 ------------------KPFICEVCHKSYTQFSNLCRHK 414
Cdd:COG5189   379 klhenpspekmnifsakdKPYRCEVCDKRYKNLNGLKYHR 418
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 310-332 4.72e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 4.72e-03
                           10        20
                   ....*....|....*....|...
gi 568931886   310 YKCDQCPKAFNWKSNLIRHQMSH 332
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 954-1007 7.75e-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: 36.77  E-value: 7.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568931886  954 CRYCGKIFPRSANLTRHLRTHTgeqpYRCKYCDRSFSISSNLQRHVRNIHnKEK 1007
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVH-KET 52
 
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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