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Conserved domains on  [gi|1229184783|ref|XP_022106093|]
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PR domain zinc finger protein 16-like isoform X1 [Acanthaster planci]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 84-218 6.75e-77

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: 249.59  E-value: 6.75e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   84 AVYVPEDVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCAWEIVDADGRVRCWIDASEPGTGN 163
Cdd:cd19200      1 PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEFGKVKFWIDASEPGTGN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229184783  164 WMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLVLKEAAFPDQEGIPI 218
Cdd:cd19200     81 WMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETMPP 135
zf-H2C2_2 pfam13465
Zinc-finger double domain;
920-944 1.52e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.52e-05
                           10        20
                   ....*....|....*....|....*
gi 1229184783  920 NLTRHLRTHTGEQPYSCKYCDRSFS 944
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 906-928 5.82e-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: 41.13  E-value: 5.82e-05
                           10        20
                   ....*....|....*....|...
gi 1229184783  906 YTCKYCGKLFPRSANLTRHLRTH 928
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-358 7.96e-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: 40.75  E-value: 7.96e-05
                           10        20
                   ....*....|....*....|..
gi 1229184783  337 FPCEHCDKTFSDPSNLQRHIRT 358
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 339-384 1.85e-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: 41.39  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1229184783  339 CEHCDKTFSDPSNLQRHIRTQHVgarshACPECGKTFATSSGLKQH 384
Cdd:cd20908      4 CYYCDREFDDEKILIQHQKAKHF-----KCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
301-582 1.82e-03

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  301 SEYRANRDFHCDKCPKSFHWKSNLLRHQNEHSSDHQFPCEH--CDKTFSDPSNLQRHIRTQHVGARSHACPECGKTFATS 378
Cdd:COG5048     26 SLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  379 SGLKQHTHIHSSIKPFICEVCLKS----YTQFSNLcrHKRMHADCRTQLKCNNCSQMFATVTSLNK-HRRFCHGNQLLNN 453
Cdd:COG5048    106 SSSSLSSSSSNSNDNNLLSSHSLPpssrDPQLPDL--LSISNLRNNPLPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  454 QISTTQAASVPSVVRNGSC-PVMTPNPSLIGVGMLGANNPLHPANLAHLwnaNLHLTHQALLQNNLLGYPGSDKTPLPSH 532
Cdd:COG5048    184 LSLLISSNVSTSIPSSSENsPLSSSYSIPSSSSDQNLENSSSSLPLTTN---SQLSPKSLLSQSPSSLSSSDSSSSASES 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229184783  533 PYFMGYSPMPTQSPLLPSNFNKQNHTSRSGSGGTSPNGSINSaDDWLKHY 582
Cdd:COG5048    261 PRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRS-SPLTRHL 309
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 963-985 4.71e-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: 4.71e-03
                           10        20
                   ....*....|....*....|...
gi 1229184783  963 FKCPLCERCFGQQTNLDRHLKKH 985
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 84-218 6.75e-77

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: 249.59  E-value: 6.75e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   84 AVYVPEDVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCAWEIVDADGRVRCWIDASEPGTGN 163
Cdd:cd19200      1 PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEFGKVKFWIDASEPGTGN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229184783  164 WMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLVLKEAAFPDQEGIPI 218
Cdd:cd19200     81 WMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETMPP 135
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 95-204 2.45e-08

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: 53.49  E-value: 2.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783    95 PEFELRESCIqeAGLGVFSLVDIPVGERFGPFAGV--------ERSLVQDMLCAWEIVDADGRVRCWIDASEpgTGNWMK 166
Cdd:smart00317    1 NKLEVFKSPG--KGWGVRATEDIPKGEFIGEYVGEiitseeaeERPKAYDTDGAKAFYLFDIDSDLCIDARR--KGNLAR 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 1229184783   167 YVRSAATfEDQNMVPVQIEN--KVYFKVIRPIGPGKELLV 204
Cdd:smart00317   77 FINHSCE-PNCELLFVEVNGddRIVIFALRDIKPGEELTI 115
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 108-204 8.38e-07

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: 49.06  E-value: 8.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  108 GLGVFSLVDIPVGERFGPFAGV------------ERSLVQDMLCAWE--IVDADGRVRCWIDASEPGTGNWMKYVRSAAt 173
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVllitkeeadkreLLYYDKLELRLWGpyLFTLDEDSEYCIDARALYYGNWARFINHSC- 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1229184783  174 feDQNM----VPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:pfam00856   80 --DPNCevrvVYVNGGPRIVIFALRDIKPGEELTI 112
zf-H2C2_2 pfam13465
Zinc-finger double domain;
920-944 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.52e-05
                           10        20
                   ....*....|....*....|....*
gi 1229184783  920 NLTRHLRTHTGEQPYSCKYCDRSFS 944
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 906-928 5.82e-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: 41.13  E-value: 5.82e-05
                           10        20
                   ....*....|....*....|...
gi 1229184783  906 YTCKYCGKLFPRSANLTRHLRTH 928
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-358 7.96e-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: 40.75  E-value: 7.96e-05
                           10        20
                   ....*....|....*....|..
gi 1229184783  337 FPCEHCDKTFSDPSNLQRHIRT 358
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 339-384 1.85e-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: 41.39  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1229184783  339 CEHCDKTFSDPSNLQRHIRTQHVgarshACPECGKTFATSSGLKQH 384
Cdd:cd20908      4 CYYCDREFDDEKILIQHQKAKHF-----KCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
301-582 1.82e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  301 SEYRANRDFHCDKCPKSFHWKSNLLRHQNEHSSDHQFPCEH--CDKTFSDPSNLQRHIRTQHVGARSHACPECGKTFATS 378
Cdd:COG5048     26 SLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  379 SGLKQHTHIHSSIKPFICEVCLKS----YTQFSNLcrHKRMHADCRTQLKCNNCSQMFATVTSLNK-HRRFCHGNQLLNN 453
Cdd:COG5048    106 SSSSLSSSSSNSNDNNLLSSHSLPpssrDPQLPDL--LSISNLRNNPLPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  454 QISTTQAASVPSVVRNGSC-PVMTPNPSLIGVGMLGANNPLHPANLAHLwnaNLHLTHQALLQNNLLGYPGSDKTPLPSH 532
Cdd:COG5048    184 LSLLISSNVSTSIPSSSENsPLSSSYSIPSSSSDQNLENSSSSLPLTTN---SQLSPKSLLSQSPSSLSSSDSSSSASES 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229184783  533 PYFMGYSPMPTQSPLLPSNFNKQNHTSRSGSGGTSPNGSINSaDDWLKHY 582
Cdd:COG5048    261 PRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRS-SPLTRHL 309
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
887-958 1.85e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229184783  887 STVLYPSSGEKMIMRSKDRYT--CKYCGKLFPRSANLTRHLRTHTGEQPYSCKY--CDRSFSISSNLQRHVRNIHN 958
Cdd:COG5048     13 NSVLSSTPKSTLKSLSNAPRPdsCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
351-377 4.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 4.21e-03
                           10        20
                   ....*....|....*....|....*..
gi 1229184783  351 NLQRHIRTqHVGARSHACPECGKTFAT 377
Cdd:pfam13465    1 NLKRHMRT-HTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 963-985 4.71e-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: 4.71e-03
                           10        20
                   ....*....|....*....|...
gi 1229184783  963 FKCPLCERCFGQQTNLDRHLKKH 985
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 933-985 6.84e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 6.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229184783  933 PYSCKYCDRSFSISSNLQRHVR-NIHNKekpfKCPLCERCF-GQQTNLDRHLKKH 985
Cdd:PHA00733    73 PYVCPLCLMPFSSSVSLKQHIRyTEHSK----VCPVCGKEFrNTDSTLDHVCKKH 123
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
900-945 7.59e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 39.47  E-value: 7.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1229184783  900 MRSKDRYTCKYCGklfprSANLTRHLRTHTGEQPYSCKYCDRSFSI 945
Cdd:COG3677     11 IRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 367-445 9.19e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.01  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  367 ACPECGKTFATSSGLKQHTHIHSSI------KPFICEV--CLKSYTQFSNLCRHKRMHADCRTQLKCNNCSQMFATVTSL 438
Cdd:pfam15909    3 SSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSAlsCTETFPSMQELVAHSKLHYKPNRYFKCENCLLRFRTHRSL 82


                   ....*..
gi 1229184783  439 NKHRRFC 445
Cdd:pfam15909   83 FKHLHVC 89
ZnF_C2H2 smart00355
zinc finger;
906-928 9.21e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 9.21e-03
                            10        20
                    ....*....|....*....|...
gi 1229184783   906 YTCKYCGKLFPRSANLTRHLRTH 928
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 84-218 6.75e-77

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: 249.59  E-value: 6.75e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   84 AVYVPEDVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCAWEIVDADGRVRCWIDASEPGTGN 163
Cdd:cd19200      1 PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEFGKVKFWIDASEPGTGN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229184783  164 WMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLVLKEAAFPDQEGIPI 218
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, ...
 83-212 1.25e-43

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: 156.19  E-value: 1.25e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   83 AAVYVPEDVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCAWE-----------------IVD 145
Cdd:cd19213     10 APVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEqilndvevssqegcitkIVD 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229184783  146 ADGRVRCWIDASEPGTGNWMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV-LKEAAFPD 212
Cdd:cd19213     90 DLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVyVKDGVYPL 157
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 83-216 5.03e-37

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: 136.99  E-value: 5.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   83 AAVYVPEDVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCAWEIVDADGRVRCWIDASEPGTG 162
Cdd:cd19214     20 APIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEVLDEFGNVKFCIDASQPDVG 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229184783  163 NWMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLVLKEAAFPDQEGI 216
Cdd:cd19214    100 SWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSEDYSHETM 153
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 90-204 5.99e-33

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: 124.09  E-value: 5.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   90 DVVLPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAG--VERSLVQDMLCAWEIVDADGRVRCwIDASEPGTGNWMKY 167
Cdd:cd19188      1 LMGLPEELELKPSAVDKTRIGVWAKKSIPKGRKFGPFVGekKKRSQVKNNVYMWEIYGPKRGWMC-VDASDPTKGNWLRY 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1229184783  168 VRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19188     80 VNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLC 116
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 93-204 1.19e-29

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: 114.64  E-value: 1.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAG--VERSLVQDMLCAWEIvDADGRVRCWIDASEPGTGNWMKYVRS 170
Cdd:cd19193      4 LPPGLSIKRSSIPGAGLGVWAEAPIPKGMVFGPYEGeiVEDEEAADSGYSWQI-YKGGKLSHYIDAKDESKSNWMRYVNC 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1229184783  171 AATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19193     83 ARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLV 116
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 93-204 2.95e-26

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: 103.43  E-value: 2.95e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVErslvqdmlcaweivdadgrvrcwidasepgtgNWMKYVRSAA 172
Cdd:cd10534      1 LPAGLELVLSSIPEGGLGVFARRTIPAGTRFGPLEGVV--------------------------------NWMRFVRPAR 48

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1229184783  173 TFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd10534     49 NEEEQNLVAYQHGGQIYFRTTRDIPPGEELLV 80
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 93-204 1.77e-22

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: 94.35  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLC-----AWEIVDADGRVRCWIDASEPGTGNWMKY 167
Cdd:cd19196      1 LPSQVIIAQSSIPGAGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCknnnlMWEVFNEDGTVSHFIDASQENHRSWMTF 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1229184783  168 VRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19196     81 VNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLV 117
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 93-204 1.65e-21

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: 91.38  E-value: 1.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGVERSLVQDMLCA------WEIVDADGRVRCWIDASEPGTGNWMK 166
Cdd:cd19191      1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGVLVSPEKQIGAVrntqhlWEIYDQEGTLQHFIDGGDPSKSSWMR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1229184783  167 YVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19191     81 YIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLV 118
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 93-204 2.06e-21

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: 90.87  E-value: 2.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELREScIQEAGL--GVFSLVDIPVGERFGPFAGVERSLVQDMLCAWEIVDADGRVR-CWIDASEPGtGNWMKYVR 169
Cdd:cd19201      3 LPGELELRKP-SQDAGRsgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAQGSKGGeGLLLLTEDS-GTWLKLVR 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1229184783  170 SAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19201     81 SADDEDEANLILYFKGGQIWCEVTKDIPPGEELIL 115
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 93-204 2.18e-21

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: 91.23  E-value: 2.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVDIPVGERFGPFAGvERSLVQdmlcawEIVDADGRVRCW-----------IDASEPGT 161
Cdd:cd19187      3 LPRNLTLKYSSVGREVLGVWSSDYIPRGTRFGPLVG-EIYTND------PVPKGANRKYFWriysngefyhyIDGFDPSK 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1229184783  162 GNWMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19187     76 SNWMRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLV 118
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 110-218 1.27e-17

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: 80.52  E-value: 1.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  110 GVFSLVDIPVGERFGPFAG--VERSLVQ---DMLCAWEIVdADGRVRCWIDAsEPGTGNWMKYVRSAATFEDQNMVPVQI 184
Cdd:cd19198     21 GVFCKKTIPKGTRFGPFRGrvVNTSEIKtydDNSFMWEIF-EDGKLSHFIDG-RGSTGNWMSYVNCARYAEEQNLIAIQC 98

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1229184783  185 ENKVYFKVIRPIGPGKELLVLKEAAFPDQEGIPI 218
Cdd:cd19198     99 QGQIFYESCKEILQGQELLVWYGDCYLQFMGIPV 132
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 93-204 2.64e-15

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: 73.87  E-value: 2.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEaGLGVFSLVDIPVGERFGPFAGVER---SLVQDMLC--AWEIVDADGRVRCWIDASEPGTGNWMKY 167
Cdd:cd19190      5 VPDRFSLKSSKVQD-GMGLYTARRVKKGEKFGPFAGEKRmpnELDESMDPrlMWEVRGSKGEVLYILDASNPRHSNWLRF 83

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1229184783  168 VRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19190     84 VHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLI 120
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 93-204 6.37e-15

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: 72.45  E-value: 6.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELREscIQEAGLGVFSLVDIPVGERFGPF-AGVERSLVQDMLCAWEIVDADGRVRCwIDASEPGTGNWMKYVRSA 171
Cdd:cd19199      7 LPDNLEIRQ--LEDGSEGVFALVPLVKRTQFGPFeAKRVARLDGFAVFPLKVFEKDGSVVY-LDTSNEDDCNWMMFVRPA 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1229184783  172 ATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19199     84 TDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRV 116
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 93-204 6.94e-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: 72.50  E-value: 6.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQeAGLGVFSLVDIPVGERFGPFAG-------VERSLVQDMLCAWEIVDADGRVRCwIDASEPGTGNWM 165
Cdd:cd19189      6 LPRQLYLRQSETG-AEVGVWTKETIPVRTCFGPLIGqqshsaeVADWTDKAAPHIWKIYHNDVLEFC-IITTDENECNWM 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1229184783  166 KYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19189     84 MFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLF 122
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 109-204 1.05e-14

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: 72.00  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  109 LGVFSLVDIPVGERFGPFAG--VERSLVQDMLCAWEIVDADGRVRCWIDASEPGTGNWMKYVRSAATFEDQNMVPVQIEN 186
Cdd:cd19194     20 GGVFAKRRIPKRTQFGPLEGplVKKSELKDNKIHPLELEEDDGEDLYFDLSDENKCNWMMFVRPAQNHLEQNLVAYQYGQ 99

                           90
                   ....*....|....*...
gi 1229184783  187 KVYFKVIRPIGPGKELLV 204
Cdd:cd19194    100 EIYFTTIKNIEPKQELKV 117
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 93-207 2.15e-13

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: 67.83  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   93 LPPEFELRESCIQEAGLGVFSLVD-IPVGERFGPFAGVErslvqdmlcawEIVDADGRVR-------CWIDASEPGT-GN 163
Cdd:cd10520      5 LPPGLALGPSLAQEERLGVWCVGDaLQKGTFLGPLEEEL-----------ESHDLTEGGSprqeesgQSGDVLACEQsSK 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1229184783  164 WMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLVLKE 207
Cdd:cd10520     74 WMRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWPE 117
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 83-204 1.84e-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: 59.87  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783   83 AAVYVPE--DVVLPPEFELRESCIQEAglgvfslvdIPVGERFGPFAGveRSLVQDM---LCAWEIVDADGRVRCwIDAS 157
Cdd:cd19195      1 AALTAPQgiEVVKDTSGESDVRCVDEV---------IPKGHIFGPYEG--QICTQDKssgFFSWLIVDKNNRYKS-IDGS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1229184783  158 EPGTGNWMKYVRSAATFEDQNMVPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:cd19195     69 DETKANWMRYVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRV 115
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 95-204 2.45e-08

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: 53.49  E-value: 2.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783    95 PEFELRESCIqeAGLGVFSLVDIPVGERFGPFAGV--------ERSLVQDMLCAWEIVDADGRVRCWIDASEpgTGNWMK 166
Cdd:smart00317    1 NKLEVFKSPG--KGWGVRATEDIPKGEFIGEYVGEiitseeaeERPKAYDTDGAKAFYLFDIDSDLCIDARR--KGNLAR 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 1229184783   167 YVRSAATfEDQNMVPVQIEN--KVYFKVIRPIGPGKELLV 204
Cdd:smart00317   77 FINHSCE-PNCELLFVEVNGddRIVIFALRDIKPGEELTI 115
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 110-204 5.36e-08

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: 52.82  E-value: 5.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  110 GVFSLVDIPVGERFGPFAGVERSLVQDMLCA-----WEIVDADGRVRCWIDASEPGTGNWMKYVRSAATFEDQNM-VPVQ 183
Cdd:cd19192     21 SVVTTTDIPAGTIFGPCVLSFTLGYDIADIAlkttdKRVVPYIFRVDTGACNGSSEPSDWLRLVQPARDRHEQNLeAFRK 100

                           90       100
                   ....*....|....*....|.
gi 1229184783  184 IENKVYFKVIRPIGPGKELLV 204
Cdd:cd19192    101 NEGQVYFRTLRRIRKGEELLV 121
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 108-204 8.38e-07

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: 49.06  E-value: 8.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  108 GLGVFSLVDIPVGERFGPFAGV------------ERSLVQDMLCAWE--IVDADGRVRCWIDASEPGTGNWMKYVRSAAt 173
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVllitkeeadkreLLYYDKLELRLWGpyLFTLDEDSEYCIDARALYYGNWARFINHSC- 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1229184783  174 feDQNM----VPVQIENKVYFKVIRPIGPGKELLV 204
Cdd:pfam00856   80 --DPNCevrvVYVNGGPRIVIFALRDIKPGEELTI 112
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 104-204 1.46e-05

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: 45.80  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  104 IQEAGLGVFSLVDIPVGERFGPFAGVERS-LVQDMLCAWEI-------VDADGRVrcwIDASEpgTGNWMKYVRSAATFe 175
Cdd:cd10522     10 LSHNGLGLFAAETIAKGEFVGEYTGEVLDrWEEDRDSVYHYdplypfdLNGDILV---IDAGK--KGNLTRFINHSDQP- 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1229184783  176 dqNMVPVQI----ENKVYFKVIRPIGPGKELLV 204
Cdd:cd10522     84 --NLELIVRtlkgEQHIGFVAIRDIKPGEELFI 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
920-944 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.52e-05
                           10        20
                   ....*....|....*....|....*
gi 1229184783  920 NLTRHLRTHTGEQPYSCKYCDRSFS 944
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 906-928 5.82e-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: 41.13  E-value: 5.82e-05
                           10        20
                   ....*....|....*....|...
gi 1229184783  906 YTCKYCGKLFPRSANLTRHLRTH 928
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 337-358 7.96e-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: 40.75  E-value: 7.96e-05
                           10        20
                   ....*....|....*....|..
gi 1229184783  337 FPCEHCDKTFSDPSNLQRHIRT 358
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRT 22
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 117-204 1.40e-04

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: 42.50  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  117 IPVGERFGPFAGVERSL--VQDMLCAWEIVDAD-GRVRCWIDASEPGTGNWMKYVRSAATFEDQNMVPVQ--IENKVYFK 191
Cdd:cd19197      1 IPAGLRLGPVPGIFKLGkyLSDRKEPGNKKKVRrVRGDYLVDESGSPATEWIGLVRAARNNQEQNLEAIAdlPGGQIFYR 80

                           90
                   ....*....|...
gi 1229184783  192 VIRPIGPGKELLV 204
Cdd:cd19197     81 ALRDIQPGEELTV 93
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 339-384 1.85e-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: 41.39  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1229184783  339 CEHCDKTFSDPSNLQRHIRTQHVgarshACPECGKTFATSSGLKQH 384
Cdd:cd20908      4 CYYCDREFDDEKILIQHQKAKHF-----KCHICHKKLYTAGGLAVH 44
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 337-360 1.43e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 37.24  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|....
gi 1229184783  337 FPCEHCDKTFSDPSNLQRHIRTQH 360
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTHH 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
301-582 1.82e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  301 SEYRANRDFHCDKCPKSFHWKSNLLRHQNEHSSDHQFPCEH--CDKTFSDPSNLQRHIRTQHVGARSHACPECGKTFATS 378
Cdd:COG5048     26 SLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  379 SGLKQHTHIHSSIKPFICEVCLKS----YTQFSNLcrHKRMHADCRTQLKCNNCSQMFATVTSLNK-HRRFCHGNQLLNN 453
Cdd:COG5048    106 SSSSLSSSSSNSNDNNLLSSHSLPpssrDPQLPDL--LSISNLRNNPLPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  454 QISTTQAASVPSVVRNGSC-PVMTPNPSLIGVGMLGANNPLHPANLAHLwnaNLHLTHQALLQNNLLGYPGSDKTPLPSH 532
Cdd:COG5048    184 LSLLISSNVSTSIPSSSENsPLSSSYSIPSSSSDQNLENSSSSLPLTTN---SQLSPKSLLSQSPSSLSSSDSSSSASES 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229184783  533 PYFMGYSPMPTQSPLLPSNFNKQNHTSRSGSGGTSPNGSINSaDDWLKHY 582
Cdd:COG5048    261 PRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRS-SPLTRHL 309
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
887-958 1.85e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229184783  887 STVLYPSSGEKMIMRSKDRYT--CKYCGKLFPRSANLTRHLRTHTGEQPYSCKY--CDRSFSISSNLQRHVRNIHN 958
Cdd:COG5048     13 NSVLSSTPKSTLKSLSNAPRPdsCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 336-360 1.87e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 36.76  E-value: 1.87e-03
                           10        20
                   ....*....|....*....|....*.
gi 1229184783  336 QFPCEHCDKTFSDPSNLQRHIRT-QH 360
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLKSkKH 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
351-377 4.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 4.21e-03
                           10        20
                   ....*....|....*....|....*..
gi 1229184783  351 NLQRHIRTqHVGARSHACPECGKTFAT 377
Cdd:pfam13465    1 NLKRHMRT-HTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 963-985 4.71e-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: 4.71e-03
                           10        20
                   ....*....|....*....|...
gi 1229184783  963 FKCPLCERCFGQQTNLDRHLKKH 985
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 933-985 6.84e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 6.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229184783  933 PYSCKYCDRSFSISSNLQRHVR-NIHNKekpfKCPLCERCF-GQQTNLDRHLKKH 985
Cdd:PHA00733    73 PYVCPLCLMPFSSSVSLKQHIRyTEHSK----VCPVCGKEFrNTDSTLDHVCKKH 123
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
900-945 7.59e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 39.47  E-value: 7.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1229184783  900 MRSKDRYTCKYCGklfprSANLTRHLRTHTGEQPYSCKYCDRSFSI 945
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 ...
 934-954 7.92e-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: 7.92e-03
                           10        20
                   ....*....|....*....|.
gi 1229184783  934 YSCKYCDRSFSISSNLQRHVR 954
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR 21
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 367-445 9.19e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.01  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229184783  367 ACPECGKTFATSSGLKQHTHIHSSI------KPFICEV--CLKSYTQFSNLCRHKRMHADCRTQLKCNNCSQMFATVTSL 438
Cdd:pfam15909    3 SSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSAlsCTETFPSMQELVAHSKLHYKPNRYFKCENCLLRFRTHRSL 82


                   ....*..
gi 1229184783  439 NKHRRFC 445
Cdd:pfam15909   83 FKHLHVC 89
ZnF_C2H2 smart00355
zinc finger;
906-928 9.21e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 9.21e-03
                            10        20
                    ....*....|....*....|...
gi 1229184783   906 YTCKYCGKLFPRSANLTRHLRTH 928
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
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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