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Conserved domains on  [gi|1130226247|ref|XP_019758974|]
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transcription factor hamlet isoform X1 [Dendroctonus ponderosae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 107-212 1.32e-22

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. 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 has 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 N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19201:

Pssm-ID: 394802  Cd Length: 122  Bit Score: 93.95  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKED--------RVYARSNISKGTRYGPFQGKWASIPEHPRFAWEIVA--GTEVRGWLDGSLNHQNWIKLIRSD 176
Cdd:cd19201     3 LPGELELRKPsqdagrsgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAqgSKGGEGLLLLTEDSGTWLKLVRSA 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1130226247 177 SNKNAANMKYFLVSGEVWYETIVDIAAGDEICLGPK 212
Cdd:cd19201    83 DDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLR 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-775 1.57e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*
gi 1130226247 751 NLTRHLRTHTGEQPYKCRYCERSFS 775
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 2.01e-05

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.01e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 737 YACKYCGKVFPRSANLTRHLRTH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 2.44e-05

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 330 FHCENCPKVFTDPSNLQRHIRTH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-370 3.10e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.10e-04
                          10        20
                  ....*....|....*....|....*..
gi 1130226247 344 NLQRHIRTHHvGARSHACPECGKTFNS 370
Cdd:pfam13465   1 NLKRHMRTHT-GEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 387-409 3.77e-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: 3.77e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 387 FQCEVCFKAYTQFSNLCRHKRMH 409
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 535-666 3.79e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247  535 PPRVPIIAEKVSPPTAEEADLTPSPARPTTFSMPREKLHSTSED--------ETVKDTASRPSSATSEEgdqPLDLSGWN 606
Cdd:PHA03247  2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTAPPPPPGPPPP---SLPLGGSV 2856

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1130226247  607 AT------RAPEKEP--KKEHKVEKVESRLATPPPPVKAEKIEIVELEEQKKSSPITPPMAYPRPTYP 666
Cdd:PHA03247  2857 APggdvrrRPPSRSPaaKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 794-816 4.91e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 4.91e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 794 FKCPLCERCFGQQTNLDRHLKKH 816
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 107-212 1.32e-22

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: 93.95  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKED--------RVYARSNISKGTRYGPFQGKWASIPEHPRFAWEIVA--GTEVRGWLDGSLNHQNWIKLIRSD 176
Cdd:cd19201     3 LPGELELRKPsqdagrsgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAqgSKGGEGLLLLTEDSGTWLKLVRSA 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1130226247 177 SNKNAANMKYFLVSGEVWYETIVDIAAGDEICLGPK 212
Cdd:cd19201    83 DDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLR 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-775 1.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*
gi 1130226247 751 NLTRHLRTHTGEQPYKCRYCERSFS 775
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 2.01e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.01e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 737 YACKYCGKVFPRSANLTRHLRTH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 2.44e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 330 FHCENCPKVFTDPSNLQRHIRTH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-370 3.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.10e-04
                          10        20
                  ....*....|....*....|....*..
gi 1130226247 344 NLQRHIRTHHvGARSHACPECGKTFNS 370
Cdd:pfam13465   1 NLKRHMRTHT-GEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
726-789 9.94e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 9.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1130226247 726 HQQNSGKIKDRYACKYCGKVFPRSANLTRHLRTHTGEQPYKCRYCER--SFSISSNLQRHVRNIHN 789
Cdd:COG5048    23 TLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHN 88
ZnF_C2H2 smart00355
zinc finger;
330-352 2.68e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|...
gi 1130226247  330 FHCENCPKVFTDPSNLQRHIRTH 352
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 387-409 3.77e-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: 3.77e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 387 FQCEVCFKAYTQFSNLCRHKRMH 409
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 535-666 3.79e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247  535 PPRVPIIAEKVSPPTAEEADLTPSPARPTTFSMPREKLHSTSED--------ETVKDTASRPSSATSEEgdqPLDLSGWN 606
Cdd:PHA03247  2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTAPPPPPGPPPP---SLPLGGSV 2856

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1130226247  607 AT------RAPEKEP--KKEHKVEKVESRLATPPPPVKAEKIEIVELEEQKKSSPITPPMAYPRPTYP 666
Cdd:PHA03247  2857 APggdvrrRPPSRSPaaKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
ZnF_C2H2 smart00355
zinc finger;
737-759 4.25e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 1130226247  737 YACKYCGKVFPRSANLTRHLRTH 759
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 794-816 4.91e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 4.91e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 794 FKCPLCERCFGQQTNLDRHLKKH 816
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 107-212 1.32e-22

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: 93.95  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKED--------RVYARSNISKGTRYGPFQGKWASIPEHPRFAWEIVA--GTEVRGWLDGSLNHQNWIKLIRSD 176
Cdd:cd19201     3 LPGELELRKPsqdagrsgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAqgSKGGEGLLLLTEDSGTWLKLVRSA 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1130226247 177 SNKNAANMKYFLVSGEVWYETIVDIAAGDEICLGPK 212
Cdd:cd19201    83 DDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLR 118
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 106-213 1.77e-16

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: 77.02  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 106 ALPSELELKEDR-------VYARSNISKGTRYGPFQGKWASIPEHPRFAWEIV-AGTEVRGWLDGSL-NHQNWIKLIRSD 176
Cdd:cd19200     9 PIPPDFELRESAavgaglgVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVdEFGKVKFWIDASEpGTGNWMKYIRSA 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1130226247 177 SNKNAANMKYFLVSGEVWYETIVDIAAGDEICLGPKA 213
Cdd:cd19200    89 PSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKA 125
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 107-207 1.59e-10

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: 57.98  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKED-------RVYARSNISKGTRYGPFQGKWasipehprfaweivagtevrgwldgslnhqNWIKLIRSDSNK 179
Cdd:cd10534     1 LPAGLELVLSsipegglGVFARRTIPAGTRFGPLEGVV------------------------------NWMRFVRPARNE 50

                          90       100
                  ....*....|....*....|....*...
gi 1130226247 180 NAANMKYFLVSGEVWYETIVDIAAGDEI 207
Cdd:cd10534    51 EEQNLVAYQHGGQIYFRTTRDIPPGEEL 78
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 107-209 6.75e-10

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: 58.80  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDR-------VYARSNISKGTRYGPFQGKWASIPEHPRFAWEIV-AGTEVRGWLDGSL-NHQNWIKLIRSDS 177
Cdd:cd19214    30 IPSEFELRESNipgtglgIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEVLdEFGNVKFCIDASQpDVGSWLKYIRFAG 109

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1130226247 178 NKNAANMKYFLVSGEVWYETIVDIAAGDEICL 209
Cdd:cd19214   110 CYDQHNLVACQINDQIFYRAVADIDPGEELLL 141
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 118-207 4.97e-09

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: 55.48  E-value: 4.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 118 VYARSNISKGTRYGPFQGKWASIPE-----HPRFAWEIVAGTEVRGWLDGSLNHQNWIKLIRSDSNKNAANMKYFLVSGE 192
Cdd:cd19198    22 VFCKKTIPKGTRFGPFRGRVVNTSEiktydDNSFMWEIFEDGKLSHFIDGRGSTGNWMSYVNCARYAEEQNLIAIQCQGQ 101

                          90
                  ....*....|....*
gi 1130226247 193 VWYETIVDIAAGDEI 207
Cdd:cd19198   102 IFYESCKEILQGQEL 116
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 107-207 2.14e-08

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: 53.21  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELK----EDR---VYARSNISKGTRYGPFQGKWASIPEH--PRFAWEIVAGTevRGWL--DGS-LNHQNWIKLIR 174
Cdd:cd19188     4 LPEELELKpsavDKTrigVWAKKSIPKGRKFGPFVGEKKKRSQVknNVYMWEIYGPK--RGWMcvDASdPTKGNWLRYVN 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1130226247 175 SDSNKNAANMKYFLVSGEVWYETIVDIAAGDEI 207
Cdd:cd19188    82 WARSGEEQNLFPLQINRAIYYKTLKPIAPGEEL 114
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 107-219 6.07e-08

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: 52.96  E-value: 6.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDR-------VYARSNISKGTRYGPFQGKWASIPEHPRFAWEIVAGTEVRGWLDGSLNHQ------------ 167
Cdd:cd19213    20 IPSDFELRESSipgaglgVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQILNDVEVSSQEGCITKIvddlgnekfcvd 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1130226247 168 -------NWIKLIRSDSNKNAANMKYFLVSGEVWYETIVDIAAGDEIclgpkaLLNLKD 219
Cdd:cd19213   100 agqagagSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEEL------LVYVKD 152
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 107-207 2.05e-07

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: 50.82  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDR-------VYARSNISKGTRYGPFQGKWAS-----IPEHPRFAWEIVAGT-EVRGWLDGS-LNHQNWIKL 172
Cdd:cd19196     1 LPSQVIIAQSSipgaglgVFSKTWIKEGTEMGPYTGRIVSpedvdPCKNNNLMWEVFNEDgTVSHFIDASqENHRSWMTF 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1130226247 173 IRSDSNKNAANMKYFLVSGEVWYETIVDIAAGDEI 207
Cdd:cd19196    81 VNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQEL 115
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 107-207 1.21e-06

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: 48.38  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDR-------VYARSNISKGTRYGPFQGKWAS--IPEHPRFAWEIVAGTEVRGWLDGSL-NHQNWIKLIRSD 176
Cdd:cd19193     4 LPPGLSIKRSSipgaglgVWAEAPIPKGMVFGPYEGEIVEdeEAADSGYSWQIYKGGKLSHYIDAKDeSKSNWMRYVNCA 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1130226247 177 SNKNAANMKYFLVSGEVWYETIVDIAAGDEI 207
Cdd:cd19193    84 RNEEEQNLVAFQYRGKIYYRTCKDIAPGTEL 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-775 1.57e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*
gi 1130226247 751 NLTRHLRTHTGEQPYKCRYCERSFS 775
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 2.01e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.01e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 737 YACKYCGKVFPRSANLTRHLRTH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 2.44e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.90  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|...
gi 1130226247 330 FHCENCPKVFTDPSNLQRHIRTH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 107-210 2.69e-05

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: 44.59  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDRV------YARSNISKGTRYGPFQGKwASIPEH------PRFAWEIVAGT-EVRGWLDGS-LNHQNWIKL 172
Cdd:cd19190     5 VPDRFSLKSSKVqdgmglYTARRVKKGEKFGPFAGE-KRMPNEldesmdPRLMWEVRGSKgEVLYILDASnPRHSNWLRF 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1130226247 173 IRSDSNKNAANMKYFLVSGEVWYETIVDIAAGDEICLG 210
Cdd:cd19190    84 VHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLIG 121
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 107-206 3.30e-05

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: 44.24  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 107 LPSELELKEDR-------VYARSNISKGTRYGPFQGKWASIPEHPRFA-----WEIVAGTEVRGWLDGS-LNHQNWIKLI 173
Cdd:cd19187     3 LPRNLTLKYSSvgrevlgVWSSDYIPRGTRFGPLVGEIYTNDPVPKGAnrkyfWRIYSNGEFYHYIDGFdPSKSNWMRYV 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1130226247 174 RSDSNKNAANMKYFLVSGEVWYETIVDIAAGDE 206
Cdd:cd19187    83 NPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQE 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-370 3.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.10e-04
                          10        20
                  ....*....|....*....|....*..
gi 1130226247 344 NLQRHIRTHHvGARSHACPECGKTFNS 370
Cdd:pfam13465   1 NLKRHMRTHT-GEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
726-789 9.94e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 9.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1130226247 726 HQQNSGKIKDRYACKYCGKVFPRSANLTRHLRTHTGEQPYKCRYCER--SFSISSNLQRHVRNIHN 789
Cdd:COG5048    23 TLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHN 88
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 330-353 1.44e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 36.85  E-value: 1.44e-03
                          10        20
                  ....*....|....*....|....
gi 1130226247 330 FHCENCPKVFTDPSNLQRHIRTHH 353
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
ZnF_C2H2 smart00355
zinc finger;
330-352 2.68e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|...
gi 1130226247  330 FHCENCPKVFTDPSNLQRHIRTH 352
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 387-409 3.77e-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: 3.77e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 387 FQCEVCFKAYTQFSNLCRHKRMH 409
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 535-666 3.79e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247  535 PPRVPIIAEKVSPPTAEEADLTPSPARPTTFSMPREKLHSTSED--------ETVKDTASRPSSATSEEgdqPLDLSGWN 606
Cdd:PHA03247  2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTAPPPPPGPPPP---SLPLGGSV 2856

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1130226247  607 AT------RAPEKEP--KKEHKVEKVESRLATPPPPVKAEKIEIVELEEQKKSSPITPPMAYPRPTYP 666
Cdd:PHA03247  2857 APggdvrrRPPSRSPaaKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
ZnF_C2H2 smart00355
zinc finger;
737-759 4.25e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 1130226247  737 YACKYCGKVFPRSANLTRHLRTH 759
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
118-208 4.86e-03

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 38.02  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 118 VYARSNISKGTRYGPFQGK------WASIPEHP----RFAWEIVAGTEVRGWLDGS----LNHqnwiklirSDsnknAAN 183
Cdd:COG2940    20 VFATRDIPKGTLIGEYPGEvitwaeAERREPHKeplhTYLFELDDDGVIDGALGGNparfINH--------SC----DPN 87

                          90       100
                  ....*....|....*....|....*
gi 1130226247 184 MKYFLVSGEVWYETIVDIAAGDEIC 208
Cdd:COG2940    88 CEADEEDGRIFIVALRDIAAGEELT 112
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 794-816 4.91e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 4.91e-03
                          10        20
                  ....*....|....*....|...
gi 1130226247 794 FKCPLCERCFGQQTNLDRHLKKH 816
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 118-207 5.01e-03

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: 38.10  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 118 VYARSNISKGTRYGPFQGKWASIPEHPRFAWEIVAGTEVRG---WLDGS-LNHQNWIKLIRSDSNKNAANMKYFLVSGEV 193
Cdd:cd19194    22 VFAKRRIPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGedlYFDLSdENKCNWMMFVRPAQNHLEQNLVAYQYGQEI 101

                          90
                  ....*....|....
gi 1130226247 194 WYETIVDIAAGDEI 207
Cdd:cd19194   102 YFTTIKNIEPKQEL 115
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 739-797 5.26e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 5.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1130226247 739 CKYCGKVFPRSANLTRHLRTHTgeqpYKCRYCERSFSISSNLQRHVRNIHnKEKPFKCP 797
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVH-KETLTKVP 57
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 522-671 8.83e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 39.91  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130226247 522 PDKREQYIKERFTPPRVPIIA-EKVSPPTaeeadlTPSPArPTTFSMPREKLHS--TSEDETVKDTASRPSSATSEEGDQ 598
Cdd:PLN03209  423 PEVEPAQVEAKKTRPLSPYARyEDLKPPT------SPSPT-APTGVSPSVSSTSsvPAVPDTAPATAATDAAAPPPANMR 495

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1130226247 599 PLDLSGWNATRAPEKEPKKEHKVEKVESRLATPPPPVKAEKIEIVELEEQKKSSPitppmaYPRP--TYPMVLDM 671
Cdd:PLN03209  496 PLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQP------KPRPlsPYTMYEDL 564
 
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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