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Conserved domains on  [gi|2462605036|ref|XP_054209775|]
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putative histone-lysine N-methyltransferase PRDM6 isoform X2 [Homo sapiens]

Protein Classification

SET domain-containing protein( domain architecture ID 1562517)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain-containing protein may function as a protein-lysine N-methyltransferase, catalyzing the S-adenosyl-L-methionine (SAM)-dependent methylation at specific lysine residues of target proteins such as histones

CATH:  2.170.270.10
EC:  2.1.1.-
Gene Ontology:  GO:0005515|GO:0008168|GO:1904047

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
247-303 3.76e-31

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19191:

Pssm-ID: 394802  Cd Length: 128  Bit Score: 113.34  E-value: 3.76e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605036 247 LPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKvQAGAVRNTQHLWE 303
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGVLVSPEK-QIGAVRNTQHLWE 56
 
Name Accession Description Interval E-value
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
247-303 3.76e-31

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: 113.34  E-value: 3.76e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605036 247 LPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKvQAGAVRNTQHLWE 303
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGVLVSPEK-QIGAVRNTQHLWE 56
 
Name Accession Description Interval E-value
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
247-303 3.76e-31

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: 113.34  E-value: 3.76e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605036 247 LPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKvQAGAVRNTQHLWE 303
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGVLVSPEK-QIGAVRNTQHLWE 56
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
247-284 6.90e-08

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: 49.12  E-value: 6.90e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462605036 247 LPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVL 284
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFARRTIPAGTRFGPLEGVV 38
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
247-303 5.80e-06

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: 45.04  E-value: 5.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605036 247 LPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKVQAgAVRNTQhLWE 303
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDP-CKNNNL-MWE 55
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
240-284 1.60e-03

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: 37.71  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462605036 240 LPEWLRDLPRevclctSTVPGLAYGICAAQRIQQGTWIGPFQGVL 284
Cdd:cd19201     3 LPGELELRKP------SQDAGRSGGVWAKQPLPEGTRFGPYPGKL 41
 
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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