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Conserved domains on  [gi|568959785|ref|XP_006510534|]
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PR domain zinc finger protein 10 isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 197-328 6.01e-79

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: 253.43  E-value: 6.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  197 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKDRDLHEDLWFELSDET 273
Cdd:cd19194     1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568959785  274 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 328
Cdd:cd19194    74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 399-504 1.09e-35

Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of natively unstructured sequence on tristanin like or PR domain zinc finger protein 10s found in higher eukaryotes. It lies between two C2H2-type zinc-fingers. The function is not known.


:

Pssm-ID: 465211  Cd Length: 130  Bit Score: 131.88  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785   399 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQASIPIPQLPQETP-PSLEQEPETHTLHL 477
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIEAPPEGPPeTQSVTPPETTDLDL 102

                           90       100
                   ....*....|....*....|....*...
gi 568959785   478 QPQQEES-LVPTQTTLTADDMRRAKRIR 504
Cdd:pfam16638  103 QPKEEPAqSSQSESHLTSQDMRRAKRIR 130
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 718-892 3.27e-05

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22540:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 511  Bit Score: 47.61  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  718 SSKTKMVQHIRKKHPEYAQLPNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 794
Cdd:cd22540   226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  795 yqRIQYIPVSQSASGLQQPQHiQLQVVQVAPATSPHQSQQSTVDVGQLHDPQTYTQHAI-------QVQHIQVTEPAPAA 867
Cdd:cd22540   288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIktpsgevQTVLLQEAPAATAT 364

                         170       180
                  ....*....|....*....|....*
gi 568959785  868 PSASQVAGQPLSPSAQQVQQGLSPS 892
Cdd:cd22540   365 PSSSTSTVQQQVTANNGTGTSKPNY 389
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 1.44e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.44e-04
                           10        20
                   ....*....|....*....|...
gi 568959785   518 YQCTECDKAFCRPDKLRLHMLRH 540
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf_PR_Knuckle super family cl39781
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 167-194 2.52e-04

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


The actual alignment was detected with superfamily member pfam18445:

Pssm-ID: 375871  Cd Length: 38  Bit Score: 39.20  E-value: 2.52e-04
                           10        20
                   ....*....|....*....|....*...
gi 568959785   167 LWCEECNNAHSSVCPKHGPLHPIPNRPV 194
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-527 4.96e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.96e-03
                           10        20
                   ....*....|....*....|..
gi 568959785   506 KKHVRSFHSEKIYQCTECDKAF 527
Cdd:pfam13465    3 KRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 351-371 8.74e-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: 34.84  E-value: 8.74e-03
                           10        20
                   ....*....|....*....|.
gi 568959785   351 CYECNRRFISSEQLQQHLNSH 371
Cdd:pfam12171    4 CVLCDKYFKSENALQNHLKSK 24
 
Name Accession Description Interval E-value
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 197-328 6.01e-79

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: 253.43  E-value: 6.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  197 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKDRDLHEDLWFELSDET 273
Cdd:cd19194     1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568959785  274 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 328
Cdd:cd19194    74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 399-504 1.09e-35

Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of natively unstructured sequence on tristanin like or PR domain zinc finger protein 10s found in higher eukaryotes. It lies between two C2H2-type zinc-fingers. The function is not known.


Pssm-ID: 465211  Cd Length: 130  Bit Score: 131.88  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785   399 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQASIPIPQLPQETP-PSLEQEPETHTLHL 477
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIEAPPEGPPeTQSVTPPETTDLDL 102

                           90       100
                   ....*....|....*....|....*...
gi 568959785   478 QPQQEES-LVPTQTTLTADDMRRAKRIR 504
Cdd:pfam16638  103 QPKEEPAqSSQSESHLTSQDMRRAKRIR 130
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 718-892 3.27e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 47.61  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  718 SSKTKMVQHIRKKHPEYAQLPNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 794
Cdd:cd22540   226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  795 yqRIQYIPVSQSASGLQQPQHiQLQVVQVAPATSPHQSQQSTVDVGQLHDPQTYTQHAI-------QVQHIQVTEPAPAA 867
Cdd:cd22540   288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIktpsgevQTVLLQEAPAATAT 364

                         170       180
                  ....*....|....*....|....*
gi 568959785  868 PSASQVAGQPLSPSAQQVQQGLSPS 892
Cdd:cd22540   365 PSSSTSTVQQQVTANNGTGTSKPNY 389
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 1.44e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.44e-04
                           10        20
                   ....*....|....*....|...
gi 568959785   518 YQCTECDKAFCRPDKLRLHMLRH 540
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 167-194 2.52e-04

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


Pssm-ID: 375871  Cd Length: 38  Bit Score: 39.20  E-value: 2.52e-04
                           10        20
                   ....*....|....*....|....*...
gi 568959785   167 LWCEECNNAHSSVCPKHGPLHPIPNRPV 194
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 214-319 3.19e-04

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: 41.35  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785   214 GVFSKRRIPKRTQFGP-VEGPLVRGSELKDCYIHLKVSLDKGDRKD--RDLHEDLWFELSDETLC--NWMMFVrpaqNH- 287
Cdd:pfam00856    3 GLFATEDIPKGEFIGEyVEVLLITKEEADKRELLYYDKLELRLWGPylFTLDEDSEYCIDARALYygNWARFI----NHs 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568959785   288 ----LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWY 319
Cdd:pfam00856   79 cdpnCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-527 4.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.96e-03
                           10        20
                   ....*....|....*....|..
gi 568959785   506 KKHVRSFHSEKIYQCTECDKAF 527
Cdd:pfam13465    3 KRHMRTHTGEKPYKCPECGKSF 24
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
214-325 6.72e-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: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSElkdcyihlkvsLDKGDRKDRDLHEDLwFELSDET-----LC-NWMMFVrpaqNH 287
Cdd:COG2940    19 GVFATRDIPKGTLIGEYPGEVITWAE-----------AERREPHKEPLHTYL-FELDDDGvidgaLGgNPARFI----NH 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568959785  288 -LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 325
Cdd:COG2940    83 sCDPNCEADEEDGRIFIVALRDIAAGEELTYDYGLDYDE 121
ZnF_C2H2 smart00355
zinc finger;
518-540 7.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 7.54e-03
                            10        20
                    ....*....|....*....|...
gi 568959785    518 YQCTECDKAFCRPDKLRLHMLRH 540
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 351-371 8.74e-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: 34.84  E-value: 8.74e-03
                           10        20
                   ....*....|....*....|.
gi 568959785   351 CYECNRRFISSEQLQQHLNSH 371
Cdd:pfam12171    4 CVLCDKYFKSENALQNHLKSK 24
 
Name Accession Description Interval E-value
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 197-328 6.01e-79

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: 253.43  E-value: 6.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  197 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKDRDLHEDLWFELSDET 273
Cdd:cd19194     1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568959785  274 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 328
Cdd:cd19194    74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 399-504 1.09e-35

Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of natively unstructured sequence on tristanin like or PR domain zinc finger protein 10s found in higher eukaryotes. It lies between two C2H2-type zinc-fingers. The function is not known.


Pssm-ID: 465211  Cd Length: 130  Bit Score: 131.88  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785   399 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQASIPIPQLPQETP-PSLEQEPETHTLHL 477
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIEAPPEGPPeTQSVTPPETTDLDL 102

                           90       100
                   ....*....|....*....|....*...
gi 568959785   478 QPQQEES-LVPTQTTLTADDMRRAKRIR 504
Cdd:pfam16638  103 QPKEEPAqSSQSESHLTSQDMRRAKRIR 130
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 197-324 7.87e-33

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: 123.29  E-value: 7.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  197 RARASLPLVLYIDRFLG---GVFSKRRIPKRTQFGPVEGPLVRgselkdcyihlkvSLDKGDRK-----DRDLHEdLWFE 268
Cdd:cd19199     2 RARSSLPDNLEIRQLEDgseGVFALVPLVKRTQFGPFEAKRVA-------------RLDGFAVFplkvfEKDGSV-VYLD 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568959785  269 LSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYA 324
Cdd:cd19199    68 TSNEDDCNWMMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYA 123
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 214-319 1.77e-27

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: 106.51  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLvrgselkdcyihlkvsldkgdrkdrdlhedlwfelsdetlcNWMMFVRPAQNHLEQNLV 293
Cdd:cd10534    18 GVFARRTIPAGTRFGPLEGVV-----------------------------------------NWMRFVRPARNEEEQNLV 56

                          90       100
                  ....*....|....*....|....*.
gi 568959785  294 AYQYGHHVYYTTIKNVEPKQELKVWY 319
Cdd:cd10534    57 AYQHGGQIYFRTTRDIPPGEELLVWY 82
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 197-327 2.51e-26

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: 105.24  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  197 RARASLPLVLYIDR-FLG---GVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvSLDKGDRK-----DRDLHEDLwF 267
Cdd:cd19189     1 RARLSLPRQLYLRQsETGaevGVWTKETIPVRTCFGPLIGQQSHSAEVAD-------WTDKAAPHiwkiyHNDVLEFC-I 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  268 ELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFV 327
Cdd:cd19189    73 ITTDENECNWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQL 132
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 214-325 4.77e-23

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: 95.47  E-value: 4.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPL------VRGSELKDCY-IHlkvsldkgdrKDRDLHedLWFELSDETLCNWMMFVRPAQN 286
Cdd:cd19187    20 GVWSSDYIPRGTRFGPLVGEIytndpvPKGANRKYFWrIY----------SNGEFY--HYIDGFDPSKSNWMRYVNPAHS 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568959785  287 HLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 325
Cdd:cd19187    88 LQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFAR 126
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 214-325 5.32e-22

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: 92.68  E-value: 5.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELKDC-YIHLkvsLDKGDRKDrdlhedLWFELSDETLCNWMMFVRPAQNHLEQNL 292
Cdd:cd19193    21 GVWAEAPIPKGMVFGPYEGEIVEDEEAADSgYSWQ---IYKGGKLS------HYIDAKDESKSNWMRYVNCARNEEEQNL 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568959785  293 VAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 325
Cdd:cd19193    92 VAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAK 124
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 214-326 3.93e-19

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: 84.33  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELkdcyihlkvsldkgdrkDRDLHEDLWFEL-------------SDETLCNWMMF 280
Cdd:cd19196    18 GVFSKTWIKEGTEMGPYTGRIVSPEDV-----------------DPCKNNNLMWEVfnedgtvshfidaSQENHRSWMTF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568959785  281 VRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 326
Cdd:cd19196    81 VNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTF 126
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 214-326 6.34e-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: 78.21  E-value: 6.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvsldkgdrkdrdlHED---LWFELSDETLC----------NWMMF 280
Cdd:cd19198    21 GVFCKKTIPKGTRFGPFRGRVVNTSEIKT-------------------YDDnsfMWEIFEDGKLShfidgrgstgNWMSY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568959785  281 VRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 326
Cdd:cd19198    82 VNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQF 127
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 214-319 7.66e-16

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: 74.79  E-value: 7.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKVSLDKGDrkdrdlhedlWF--ELSDETLCNWMMFVRPAQNHLEQN 291
Cdd:cd19188    21 GVWAKKSIPKGRKFGPFVGEKKKRSQVKNNVYMWEIYGPKRG----------WMcvDASDPTKGNWLRYVNWARSGEEQN 90

                          90       100
                  ....*....|....*....|....*...
gi 568959785  292 LVAYQYGHHVYYTTIKNVEPKQELKVWY 319
Cdd:cd19188    91 LFPLQINRAIYYKTLKPIAPGEELLCWY 118
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 213-319 1.18e-14

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: 71.22  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  213 GGVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvslDKGDRKDRDLHEDLWFELSDETLCNWMMFVRPAQNHLEQNL 292
Cdd:cd19201    20 GGVWAKQPLPEGTRFGPYPGKLVKEPLDPS---------YEWKVEAQGSKGGEGLLLLTEDSGTWLKLVRSADDEDEANL 90

                          90       100
                  ....*....|....*....|....*..
gi 568959785  293 VAYQYGHHVYYTTIKNVEPKQELKVWY 319
Cdd:cd19201    91 ILYFKGGQIWCEVTKDIPPGEELILVL 117
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 221-324 2.00e-13

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: 67.15  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  221 IPKRTQFGPVEGPLVRG---SELKDCYIHLKVSLDKGDRKDrdlhedlwfELSDETLCNWMMFVRPAQNHLEQNLVAYQ- 296
Cdd:cd19197     1 IPAGLRLGPVPGIFKLGkylSDRKEPGNKKKVRRVRGDYLV---------DESGSPATEWIGLVRAARNNQEQNLEAIAd 71

                          90       100
                  ....*....|....*....|....*....
gi 568959785  297 -YGHHVYYTTIKNVEPKQELKVWYAASYA 324
Cdd:cd19197    72 lPGGQIFYRALRDIQPGEELTVWYSNSLA 100
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 214-326 8.75e-13

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: 66.35  E-value: 8.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKVSLDKGDRKDRDLHedlWFELSDETLCNWMMFVRPAQNHLEQNLV 293
Cdd:cd19191    18 GICAAQRIPQGTWIGPFEGVLVSPEKQIGAVRNTQHLWEIYDQEGTLQH---FIDGGDPSKSSWMRYIRCARHCGEQNLT 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568959785  294 AYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 326
Cdd:cd19191    95 VVQYRGCIFYRACRDIPRGTELLVWYDDSYTSF 127
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 214-325 2.49e-12

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: 65.08  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGplVRGSELKDCYIHLKVSLDKGdrkdrdlHEDLWFELSDETLCNWMMFVRPAQNHLEQNLV 293
Cdd:cd19200    27 GVWTKVRIEVGEKFGPFVG--VQRSSVKDPTYAWEIVDEFG-------KVKFWIDASEPGTGNWMKYIRSAPSCEQQNLM 97

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568959785  294 AYQYGHHVYYTTIKNVEPKQELKVWY-AASYAE 325
Cdd:cd19200    98 ACQIDEQIYYKVVRDIQPGEELLLYMkAAVYPH 130
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 221-323 1.26e-11

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: 62.95  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  221 IPKRTQFGPVEGPLVRGSELKDCYIHLKVslDKGDRKDRdlhedlwFELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHH 300
Cdd:cd19195    28 IPKGHIFGPYEGQICTQDKSSGFFSWLIV--DKNNRYKS-------IDGSDETKANWMRYVVISREEREQNLLAFQHSEQ 98

                          90       100
                  ....*....|....*....|...
gi 568959785  301 VYYTTIKNVEPKQELKVWYAASY 323
Cdd:cd19195    99 IYFRACRDIRPGEKLRVWYSEDY 121
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 214-318 8.83e-09

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: 55.65  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGplVRGSELKDCYIHLKVSL-DKGDRKDRDLHEDLWFELSDETLC---------NWMMFVRP 283
Cdd:cd19213    37 GVWAKRKIEAGERFGPYTG--VQRSTLKDTNFGWEQILnDVEVSSQEGCITKIVDDLGNEKFCvdagqagagSWLKYIRV 114

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568959785  284 AQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVW 318
Cdd:cd19213   115 ACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVY 149
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 195-325 2.54e-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: 53.59  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  195 LTRARASLPLvlyiDRFLGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKV--------SLDKGDRKDrdlhedlw 266
Cdd:cd19192     6 LWRGGSKSVL----TDIFTSVVTTTDIPAGTIFGPCVLSFTLGYDIADIALKTTDkrvvpyifRVDTGACNG-------- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  267 felSDETLcNWMMFVRPAQNHLEQNLVAYQYGH-HVYYTTIKNVEPKQELKVWYAASYAE 325
Cdd:cd19192    74 ---SSEPS-DWLRLVQPARDRHEQNLEAFRKNEgQVYFRTLRRIRKGEELLVWYSDELAE 129
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 214-322 3.35e-07

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: 50.37  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSELK---DCYIHLKVSLDKGdrkdrdlhEDLW-FELSDETLCNWMMFVRPAQNHLE 289
Cdd:cd19190    21 GLYTARRVKKGEKFGPFAGEKRMPNELDesmDPRLMWEVRGSKG--------EVLYiLDASNPRHSNWLRFVHEAPSQEQ 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568959785  290 QNLVAYQYGHHVYYTTIKNVEPKQELKVWYAAS 322
Cdd:cd19190    93 KNLAAIQEGENIFYLAVDDIETDTELLIGYLDS 125
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 214-315 1.05e-05

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: 46.86  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPlvRGSELKDCYIHLKVSLDKGDRKdrdlhedLWFELSDETLCNWMMFVRPAQNHLEQNLV 293
Cdd:cd19214    47 GIWTKRKIEVGEKFGPYVGE--QRSNLKDPSYGWEVLDEFGNVK-------FCIDASQPDVGSWLKYIRFAGCYDQHNLV 117

                          90       100
                  ....*....|....*....|..
gi 568959785  294 AYQYGHHVYYTTIKNVEPKQEL 315
Cdd:cd19214   118 ACQINDQIFYRAVADIDPGEEL 139
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 718-892 3.27e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 47.61  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  718 SSKTKMVQHIRKKHPEYAQLPNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 794
Cdd:cd22540   226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  795 yqRIQYIPVSQSASGLQQPQHiQLQVVQVAPATSPHQSQQSTVDVGQLHDPQTYTQHAI-------QVQHIQVTEPAPAA 867
Cdd:cd22540   288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIktpsgevQTVLLQEAPAATAT 364

                         170       180
                  ....*....|....*....|....*
gi 568959785  868 PSASQVAGQPLSPSAQQVQQGLSPS 892
Cdd:cd22540   365 PSSSTSTVQQQVTANNGTGTSKPNY 389
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 1.44e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.44e-04
                           10        20
                   ....*....|....*....|...
gi 568959785   518 YQCTECDKAFCRPDKLRLHMLRH 540
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 219-318 2.37e-04

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: 42.02  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  219 RRIPKRTQFGPVEGPLVRGSElkdcyihlkvsldKGDRKDRDLHEDLW-FELSDETLCNWMMFVRPAQNHLEQNLVAYQY 297
Cdd:cd10520    28 DALQKGTFLGPLEEELESHDL-------------TEGGSPRQEESGQSgDVLACEQSSKWMRFACRARSEEESNVAVVRL 94

                          90       100
                  ....*....|....*....|.
gi 568959785  298 GHHVYYTTIKNVEPKQELKVW 318
Cdd:cd10520    95 SGRLHLRVCKDIEPGSELLLW 115
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 167-194 2.52e-04

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


Pssm-ID: 375871  Cd Length: 38  Bit Score: 39.20  E-value: 2.52e-04
                           10        20
                   ....*....|....*....|....*...
gi 568959785   167 LWCEECNNAHSSVCPKHGPLHPIPNRPV 194
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 214-319 3.19e-04

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: 41.35  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785   214 GVFSKRRIPKRTQFGP-VEGPLVRGSELKDCYIHLKVSLDKGDRKD--RDLHEDLWFELSDETLC--NWMMFVrpaqNH- 287
Cdd:pfam00856    3 GLFATEDIPKGEFIGEyVEVLLITKEEADKRELLYYDKLELRLWGPylFTLDEDSEYCIDARALYygNWARFI----NHs 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568959785   288 ----LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWY 319
Cdd:pfam00856   79 cdpnCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-527 4.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.96e-03
                           10        20
                   ....*....|....*....|..
gi 568959785   506 KKHVRSFHSEKIYQCTECDKAF 527
Cdd:pfam13465    3 KRHMRTHTGEKPYKCPECGKSF 24
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
214-325 6.72e-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: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959785  214 GVFSKRRIPKRTQFGPVEGPLVRGSElkdcyihlkvsLDKGDRKDRDLHEDLwFELSDET-----LC-NWMMFVrpaqNH 287
Cdd:COG2940    19 GVFATRDIPKGTLIGEYPGEVITWAE-----------AERREPHKEPLHTYL-FELDDDGvidgaLGgNPARFI----NH 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568959785  288 -LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 325
Cdd:COG2940    83 sCDPNCEADEEDGRIFIVALRDIAAGEELTYDYGLDYDE 121
ZnF_C2H2 smart00355
zinc finger;
518-540 7.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 7.54e-03
                            10        20
                    ....*....|....*....|...
gi 568959785    518 YQCTECDKAFCRPDKLRLHMLRH 540
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 351-371 8.74e-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: 34.84  E-value: 8.74e-03
                           10        20
                   ....*....|....*....|.
gi 568959785   351 CYECNRRFISSEQLQQHLNSH 371
Cdd:pfam12171    4 CVLCDKYFKSENALQNHLKSK 24
 
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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