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Conserved domains on  [gi|41349460|ref|NP_955469|]
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PR domain zinc finger protein 10 isoform 2 [Homo sapiens]

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 ...
 203-334 1.34e-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: 256.12  E-value: 1.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  203 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKERDLHEDLWFELSDET 279
Cdd:cd19194    1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41349460  280 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 334
Cdd:cd19194   74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 405-510 2.91e-39

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: 142.28  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    405 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQTTIPI---PQLPQETQSslEHEPETHTL 481
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIeapPEGPPETQS--VTPPETTDL 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 41349460    482 HLQPQHEESV-VPTQSTLTADDMRRAKRIR 510
Cdd:pfam16638  101 DLQPKEEPAQsSQSESHLTSQDMRRAKRIR 130
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 840-1014 2.95e-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: 48.00  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  840 SSKTKMVQHIRKKHPEFAQLSNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 916
Cdd:cd22540  226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  917 yqRIQYIPVSQSASGLQQPQHiQLQVVQVASATSPHQSQQSTVDVG-QLHDPQP------YPQHAIQVQHIQVSEPTASA 989
Cdd:cd22540  288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQiQNSEPTPtqvyikTPSGEVQTVLLQEAPAATAT 364

                        170       180
                 ....*....|....*....|....*
gi 41349460  990 PSSAQVSGQPLSPSAQQAQQGLSPS 1014
Cdd:cd22540  365 PSSSTSTVQQQVTANNGTGTSKPNY 389
zf_PR_Knuckle super family cl39781
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 173-200 3.09e-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: 3.09e-04
                           10        20
                   ....*....|....*....|....*...
gi 41349460    173 LWCEECNNAHASVCPKHGPLHPIPNRPV 200
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 640-662 4.75e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.75e-04
                           10        20
                   ....*....|....*....|...
gi 41349460    640 YQCTECDKAFCRPDKLRLHMLRH 662
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
555-688 1.26e-03

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  555 PLTCDLCNKGFISSTSLESHMKLHSD----QKTYSC--IFCPESFDRLDLLKDHVAIHINDGYFTCPT--CKKRFPDFIQ 626
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRSVNHsgesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLN 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349460  627 VKKHVRSFHSEKI--YQCTECDKAFC-RPDKLRLHMLRHSDR------KDFLCSTCGKQFKRKDKLREHMQ 688
Cdd:COG5048  369 NEPPQSLQQYKDLknDKKSETLSNSCiRNFKRDSNLSLHIIThlsfrpYNCKNPPCSKSFNRHYNLIPHKK 439
 
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 ...
 203-334 1.34e-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: 256.12  E-value: 1.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  203 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKERDLHEDLWFELSDET 279
Cdd:cd19194    1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41349460  280 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 334
Cdd:cd19194   74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 405-510 2.91e-39

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: 142.28  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    405 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQTTIPI---PQLPQETQSslEHEPETHTL 481
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIeapPEGPPETQS--VTPPETTDL 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 41349460    482 HLQPQHEESV-VPTQSTLTADDMRRAKRIR 510
Cdd:pfam16638  101 DLQPKEEPAQsSQSESHLTSQDMRRAKRIR 130
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 840-1014 2.95e-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: 48.00  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  840 SSKTKMVQHIRKKHPEFAQLSNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 916
Cdd:cd22540  226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  917 yqRIQYIPVSQSASGLQQPQHiQLQVVQVASATSPHQSQQSTVDVG-QLHDPQP------YPQHAIQVQHIQVSEPTASA 989
Cdd:cd22540  288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQiQNSEPTPtqvyikTPSGEVQTVLLQEAPAATAT 364

                        170       180
                 ....*....|....*....|....*
gi 41349460  990 PSSAQVSGQPLSPSAQQAQQGLSPS 1014
Cdd:cd22540  365 PSSSTSTVQQQVTANNGTGTSKPNY 389
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 220-325 2.33e-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: 41.74  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    220 GVFSKRRIPKRTQFGP-VEGPLVRGSELKDCYIHLKVSLDKGDRKE--RDLHEDLWFELSDETLC--NWMMFVrpaqNH- 293
Cdd:pfam00856    3 GLFATEDIPKGEFIGEyVEVLLITKEEADKRELLYYDKLELRLWGPylFTLDEDSEYCIDARALYygNWARFI----NHs 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 41349460    294 ----LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWY 325
Cdd:pfam00856   79 cdpnCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 173-200 3.09e-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: 3.09e-04
                           10        20
                   ....*....|....*....|....*...
gi 41349460    173 LWCEECNNAHASVCPKHGPLHPIPNRPV 200
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 640-662 4.75e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.75e-04
                           10        20
                   ....*....|....*....|...
gi 41349460    640 YQCTECDKAFCRPDKLRLHMLRH 662
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
555-688 1.26e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  555 PLTCDLCNKGFISSTSLESHMKLHSD----QKTYSC--IFCPESFDRLDLLKDHVAIHINDGYFTCPT--CKKRFPDFIQ 626
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRSVNHsgesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLN 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349460  627 VKKHVRSFHSEKI--YQCTECDKAFC-RPDKLRLHMLRHSDR------KDFLCSTCGKQFKRKDKLREHMQ 688
Cdd:COG5048  369 NEPPQSLQQYKDLknDKKSETLSNSCiRNFKRDSNLSLHIIThlsfrpYNCKNPPCSKSFNRHYNLIPHKK 439
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 913-1016 4.56e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.17  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    913 PQGDYQRIQYIPVSQSASGLQQPQHIQLQVVQvasatsPHQSQQstvdvgqlhdPQPYPQHAIQVQHIQVSEPTASAPSS 992
Cdd:pfam09770  215 APAPAQPPAAPPAQQAQQQQQFPPQIQQQQQP------QQQPQQ----------PQQHPGQGHPVTILQRPQSPQPDPAQ 278

                           90       100
                   ....*....|....*....|....
gi 41349460    993 AQVSGQPLSPSAQQAQQGLSPSHI 1016
Cdd:pfam09770  279 PSIQPQAQQFHQQPPPVPVQPTQI 302
 
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 ...
 203-334 1.34e-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: 256.12  E-value: 1.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  203 RARASLPLVLYIDRF---LGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHlkvsldkGDRKERDLHEDLWFELSDET 279
Cdd:cd19194    1 RARASLPLILQIFRFgetLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIH-------PLELEEDDGEDLYFDLSDEN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41349460  280 LCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVN 334
Cdd:cd19194   74 KCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
Tristanin_u2 pfam16638
Unstructured region on methyltransferase between zinc-fingers; Tristanin_u2 is a region of ...
 405-510 2.91e-39

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: 142.28  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    405 PGRPPKFIRLEITSENGEKSddgTQDLLHFPTKEQFDEAEPATLNGLDQPEQTTIPI---PQLPQETQSslEHEPETHTL 481
Cdd:pfam16638   26 PGRPPKFIRLEPPNENGDKC---TQEMLHFSEKGPFEERGEAALNGLDQVEQTPEPIeapPEGPPETQS--VTPPETTDL 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 41349460    482 HLQPQHEESV-VPTQSTLTADDMRRAKRIR 510
Cdd:pfam16638  101 DLQPKEEPAQsSQSESHLTSQDMRRAKRIR 130
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 203-330 1.10e-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: 125.99  E-value: 1.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  203 RARASLPLVLYIDRFLG---GVFSKRRIPKRTQFGPVEGPLVRgselkdcyihlkvSLDKGDRK-----ERDLHEdLWFE 274
Cdd:cd19199    2 RARSSLPDNLEIRQLEDgseGVFALVPLVKRTQFGPFEAKRVA-------------RLDGFAVFplkvfEKDGSV-VYLD 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349460  275 LSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYA 330
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 ...
 220-325 1.99e-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: 1.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLvrgselkdcyihlkvsldkgdrkerdlhedlwfelsdetlcNWMMFVRPAQNHLEQNLV 299
Cdd:cd10534   18 GVFARRTIPAGTRFGPLEGVV-----------------------------------------NWMRFVRPARNEEEQNLV 56

                         90       100
                 ....*....|....*....|....*.
gi 41349460  300 AYQYGHHVYYTTIKNVEPKQELKVWY 325
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 ...
 203-333 2.23e-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: 2.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  203 RARASLPLVLYIDR-FLG---GVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvSLDKGDRK-----ERDLHEDLwF 273
Cdd:cd19189    1 RARLSLPRQLYLRQsETGaevGVWTKETIPVRTCFGPLIGQQSHSAEVAD-------WTDKAAPHiwkiyHNDVLEFC-I 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  274 ELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFV 333
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 ...
 220-331 6.88e-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: 95.09  E-value: 6.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvsldKGDRKE-----RDLHEDLWFELSDETLCNWMMFVRPAQNHL 294
Cdd:cd19187   20 GVWSSDYIPRGTRFGPLVGEIYTNDPVPK----------GANRKYfwriySNGEFYHYIDGFDPSKSNWMRYVNPAHSLQ 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41349460  295 EQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 331
Cdd:cd19187   90 EQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFAR 126
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 220-331 6.02e-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: 6.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELKDC-YIHLkvsLDKGDRKerdlheDLWFELSDETLCNWMMFVRPAQNHLEQNL 298
Cdd:cd19193   21 GVWAEAPIPKGMVFGPYEGEIVEDEEAADSgYSWQ---IYKGGKL------SHYIDAKDESKSNWMRYVNCARNEEEQNL 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41349460  299 VAYQYGHHVYYTTIKNVEPKQELKVWYAASYAE 331
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 ...
 220-332 7.29e-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: 83.95  E-value: 7.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSEL---KDCYIHLKVSLDKGDRKErdlhedlWFELSDETLCNWMMFVRPAQNHLEQ 296
Cdd:cd19196   18 GVFSKTWIKEGTEMGPYTGRIVSPEDVdpcKNNNLMWEVFNEDGTVSH-------FIDASQENHRSWMTFVNCARNEQEQ 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 41349460  297 NLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 332
Cdd:cd19196   91 NLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTF 126
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 220-332 7.17e-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: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELKDcyihlkvsldkgdrkerdlHED---LWFELSDETLC----------NWMMF 286
Cdd:cd19198   21 GVFCKKTIPKGTRFGPFRGRVVNTSEIKT-------------------YDDnsfMWEIFEDGKLShfidgrgstgNWMSY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 41349460  287 VRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 332
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 ...
 220-325 8.33e-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: 8.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKVsldKGDRKErdlhedlWF--ELSDETLCNWMMFVRPAQNHLEQN 297
Cdd:cd19188   21 GVWAKKSIPKGRKFGPFVGEKKKRSQVKNNVYMWEI---YGPKRG-------WMcvDASDPTKGNWLRYVNWARSGEEQN 90

                         90       100
                 ....*....|....*....|....*...
gi 41349460  298 LVAYQYGHHVYYTTIKNVEPKQELKVWY 325
Cdd:cd19188   91 LFPLQINRAIYYKTLKPIAPGEELLCWY 118
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 219-325 3.14e-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: 70.45  E-value: 3.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  219 GGVFSKRRIPKRTQFGPVEGPLVRgselkdcyIHLKVSLDKGDRKERDLHEDLWFELSDETlCNWMMFVRPAQNHLEQNL 298
Cdd:cd19201   20 GGVWAKQPLPEGTRFGPYPGKLVK--------EPLDPSYEWKVEAQGSKGGEGLLLLTEDS-GTWLKLVRSADDEDEANL 90

                         90       100
                 ....*....|....*....|....*..
gi 41349460  299 VAYQYGHHVYYTTIKNVEPKQELKVWY 325
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 ...
 227-330 1.34e-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: 67.92  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  227 IPKRTQFGPVEGplvrgselkdcyiHLKVSLDKGDRKERDLHEDLWF-------ELSDETLCNWMMFVRPAQNHLEQNLV 299
Cdd:cd19197    1 IPAGLRLGPVPG-------------IFKLGKYLSDRKEPGNKKKVRRvrgdylvDESGSPATEWIGLVRAARNNQEQNLE 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41349460  300 AYQ--YGHHVYYTTIKNVEPKQELKVWYAASYA 330
Cdd:cd19197   68 AIAdlPGGQIFYRALRDIQPGEELTVWYSNSLA 100
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 220-332 1.39e-12

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: 65.96  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKVSLDKGDRKERDLHedlWFELSDETLCNWMMFVRPAQNHLEQNLV 299
Cdd:cd19191   18 GICAAQRIPQGTWIGPFEGVLVSPEKQIGAVRNTQHLWEIYDQEGTLQH---FIDGGDPSKSSWMRYIRCARHCGEQNLT 94

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41349460  300 AYQYGHHVYYTTIKNVEPKQELKVWYAASYAEF 332
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 ...
 220-331 1.74e-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: 65.85  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGplVRGSELKDCYIHLKVSLDKGdrkerdlHEDLWFELSDETLCNWMMFVRPAQNHLEQNLV 299
Cdd:cd19200   27 GVWTKVRIEVGEKFGPFVG--VQRSSVKDPTYAWEIVDEFG-------KVKFWIDASEPGTGNWMKYIRSAPSCEQQNLM 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41349460  300 AYQYGHHVYYTTIKNVEPKQELKVWY-AASYAE 331
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 ...
 227-329 8.68e-12

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: 63.34  E-value: 8.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  227 IPKRTQFGPVEGPLVRGSELKDCYIHLKVslDKGDRKERdlhedlwFELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHH 306
Cdd:cd19195   28 IPKGHIFGPYEGQICTQDKSSGFFSWLIV--DKNNRYKS-------IDGSDETKANWMRYVVISREEREQNLLAFQHSEQ 98

                         90       100
                 ....*....|....*....|...
gi 41349460  307 VYYTTIKNVEPKQELKVWYAASY 329
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, ...
 220-324 3.78e-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: 56.81  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGplVRGSELKDCYIHLKVSL-DKGDRKERDLHEDLWFELSDETLC---------NWMMFVRP 289
Cdd:cd19213   37 GVWAKRKIEAGERFGPYTG--VQRSTLKDTNFGWEQILnDVEVSSQEGCITKIVDDLGNEKFCvdagqagagSWLKYIRV 114

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41349460  290 AQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVW 324
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 ...
 201-331 6.68e-09

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: 55.51  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  201 LTRARASLPLvlyiDRFLGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKV--------SLDKGDRKErdlhedlw 272
Cdd:cd19192    6 LWRGGSKSVL----TDIFTSVVTTTDIPAGTIFGPCVLSFTLGYDIADIALKTTDkrvvpyifRVDTGACNG-------- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  273 felSDETLcNWMMFVRPAQNHLEQNLVAYQYGH-HVYYTTIKNVEPKQELKVWYAASYAE 331
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 ...
 220-328 3.78e-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: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPLVRGSELK---DCYIHLKVSLDKGdrkerdlhEDLW-FELSDETLCNWMMFVRPAQNHLE 295
Cdd:cd19190   21 GLYTARRVKKGEKFGPFAGEKRMPNELDesmDPRLMWEVRGSKG--------EVLYiLDASNPRHSNWLRFVHEAPSQEQ 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41349460  296 QNLVAYQYGHHVYYTTIKNVEPKQELKVWYAAS 328
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 ...
 220-321 8.49e-06

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: 47.24  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  220 GVFSKRRIPKRTQFGPVEGPlvRGSELKDCYIHLKVSLDKGDRKerdlhedLWFELSDETLCNWMMFVRPAQNHLEQNLV 299
Cdd:cd19214   47 GIWTKRKIEVGEKFGPYVGE--QRSNLKDPSYGWEVLDEFGNVK-------FCIDASQPDVGSWLKYIRFAGCYDQHNLV 117

                         90       100
                 ....*....|....*....|..
gi 41349460  300 AYQYGHHVYYTTIKNVEPKQEL 321
Cdd:cd19214  118 ACQINDQIFYRAVADIDPGEEL 139
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 840-1014 2.95e-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: 48.00  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  840 SSKTKMVQHIRKKHPEFAQLSNTIHTPLTTAVIsatpavlttdsatgETvvTTDLLTQAMTELS---QTLTTDYRTPQgd 916
Cdd:cd22540  226 AAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLI--------------ET--TADNIIQAGNNLLivqSPGTGQPAVLQ-- 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  917 yqRIQYIPVSQSASGLQQPQHiQLQVVQVASATSPHQSQQSTVDVG-QLHDPQP------YPQHAIQVQHIQVSEPTASA 989
Cdd:cd22540  288 --QVQVLQPKQEQQVVQIPQQ-ALRVVQAASATLPTVPQKPLQNIQiQNSEPTPtqvyikTPSGEVQTVLLQEAPAATAT 364

                        170       180
                 ....*....|....*....|....*
gi 41349460  990 PSSAQVSGQPLSPSAQQAQQGLSPS 1014
Cdd:cd22540  365 PSSSTSTVQQQVTANNGTGTSKPNY 389
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 865-1116 3.03e-05

N-terminal domain of transcription factor Specificity Protein (SP) 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. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 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 SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 47.99  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  865 TPLTTAVISAT---PAVLTTDSATGETVVTTDLLTQAMTELSQTLTTDYRTPQG--DYQRIQYIPVSQSASGLQ------ 933
Cdd:cd22536  279 TPITTASVSTMpesPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASSERTeeEPQTSAAESEAQSSSQLQsnglqn 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  934 -QPQHIQLQVVQVASATSP--HQSQQSTVDVGQLHDPQPYPQHAIQ-VQHIQ------VSEPTASAPSSAQVSGQPLSPS 1003
Cdd:cd22536  359 vQDQSNSLQQVQIVGQPILqqIQIQQPQQQIIQAIQPQSFQLQSGQtIQTIQqqplqnVQLQAVQSPTQVLIRAPTLTPS 438

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460 1004 AQQAQQGLSPSHIQGSSstqgqalqqqqqqqqNSSVQHTYLPsawnsfrgysseiQMMTLPPgqfvITDSGVATPVTTGQ 1083
Cdd:cd22536  439 GQISWQTVQVQNIQSLS---------------NLQVQNAGLP-------------QQLTLTP----VSSSAGGTTIAQIA 486

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 41349460 1084 VKAVTSGHYVLSESQ-SELEEKQT----SALSGGVQVE 1116
Cdd:cd22536  487 PVAVAGTPITLNAAQlASVPNLQTvnvaNLGAAGVQVQ 524
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 225-324 9.07e-05

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: 43.18  E-value: 9.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  225 RRIPKRTQFGPVEGPLVRGSElkdcyihlkvsldKGDRKERDLHEDLW-FELSDETLCNWMMFVRPAQNHLEQNLVAYQY 303
Cdd:cd10520   28 DALQKGTFLGPLEEELESHDL-------------TEGGSPRQEESGQSgDVLACEQSSKWMRFACRARSEEESNVAVVRL 94

                         90       100
                 ....*....|....*....|.
gi 41349460  304 GHHVYYTTIKNVEPKQELKVW 324
Cdd:cd10520   95 SGRLHLRVCKDIEPGSELLLW 115
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 220-325 2.33e-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: 41.74  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    220 GVFSKRRIPKRTQFGP-VEGPLVRGSELKDCYIHLKVSLDKGDRKE--RDLHEDLWFELSDETLC--NWMMFVrpaqNH- 293
Cdd:pfam00856    3 GLFATEDIPKGEFIGEyVEVLLITKEEADKRELLYYDKLELRLWGPylFTLDEDSEYCIDARALYygNWARFI----NHs 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 41349460    294 ----LEQNLVAYQYGHHVYYTTIKNVEPKQELKVWY 325
Cdd:pfam00856   79 cdpnCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 173-200 3.09e-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: 3.09e-04
                           10        20
                   ....*....|....*....|....*...
gi 41349460    173 LWCEECNNAHASVCPKHGPLHPIPNRPV 200
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDTPI 38
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 640-662 4.75e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 4.75e-04
                           10        20
                   ....*....|....*....|...
gi 41349460    640 YQCTECDKAFCRPDKLRLHMLRH 662
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
555-688 1.26e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  555 PLTCDLCNKGFISSTSLESHMKLHSD----QKTYSC--IFCPESFDRLDLLKDHVAIHINDGYFTCPT--CKKRFPDFIQ 626
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRSVNHsgesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLN 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349460  627 VKKHVRSFHSEKI--YQCTECDKAFC-RPDKLRLHMLRHSDR------KDFLCSTCGKQFKRKDKLREHMQ 688
Cdd:COG5048  369 NEPPQSLQQYKDLknDKKSETLSNSCiRNFKRDSNLSLHIIThlsfrpYNCKNPPCSKSFNRHYNLIPHKK 439
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 912-1070 3.83e-03

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; 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 the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 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. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 41.16  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  912 TPQGDYQRIQY-IPVSQSASGLQQPQHIQLQVV---QVASATSPHQSQQSTVDVGQLHDPQPYPQHAIQVQHIQvsePTa 987
Cdd:cd22553  168 NGQTVYQTIQVpIQAIQSGNAGGGNQALQAQVIpqlAQAAQLQPQQLAQVSSQGYIQQIPANASQQQPQMVQQG---PN- 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460  988 sapSSAQVSGQPLSPSAQQAQQGLSPSHIQ----GSSSTQGQALQQQQQQQQNSSVQHTYLPSAWNSFRGYSSEIQMMTL 1063
Cdd:cd22553  244 ---QSGQIIGQVASASSIQAAAIPLTVYTGalagQNGSNQQQVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQGNPL 320


                 ....*..
gi 41349460 1064 PPGQFVI 1070
Cdd:cd22553  321 PPGTQII 327
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 913-1016 4.56e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.17  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349460    913 PQGDYQRIQYIPVSQSASGLQQPQHIQLQVVQvasatsPHQSQQstvdvgqlhdPQPYPQHAIQVQHIQVSEPTASAPSS 992
Cdd:pfam09770  215 APAPAQPPAAPPAQQAQQQQQFPPQIQQQQQP------QQQPQQ----------PQQHPGQGHPVTILQRPQSPQPDPAQ 278

                           90       100
                   ....*....|....*....|....
gi 41349460    993 AQVSGQPLSPSAQQAQQGLSPSHI 1016
Cdd:pfam09770  279 PSIQPQAQQFHQQPPPVPVQPTQI 302
 
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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