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Database: UniProt
Entry: Q5I0M0
LinkDB: Q5I0M0
Original site: Q5I0M0 
ID   SETMR_RAT               Reviewed;         315 AA.
AC   Q5I0M0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JAN-2019, entry version 82.
DE   RecName: Full=Histone-lysine N-methyltransferase SETMAR {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:Q53H47};
DE   AltName: Full=SET domain and mariner transposase fusion protein homolog;
GN   Name=Setmar {ECO:0000312|RGD:1565882};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' and
CC       'Lys-36' of histone H3, 2 specific tags for epigenetic
CC       transcriptional activation. Specifically mediates dimethylation of
CC       H3 'Lys-36'. {ECO:0000250|UniProtKB:Q53H47}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000250|UniProtKB:Q53H47};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53H47}.
CC       Chromosome {ECO:0000250|UniProtKB:Q53H47}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250|UniProtKB:Q53H47}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BC088181; AAH88181.1; -; mRNA.
DR   RefSeq; NP_001020219.1; NM_001025048.1.
DR   UniGene; Rn.7640; -.
DR   ProteinModelPortal; Q5I0M0; -.
DR   SMR; Q5I0M0; -.
DR   STRING; 10116.ENSRNOP00000008892; -.
DR   PhosphoSitePlus; Q5I0M0; -.
DR   PaxDb; Q5I0M0; -.
DR   PRIDE; Q5I0M0; -.
DR   GeneID; 500281; -.
DR   KEGG; rno:500281; -.
DR   UCSC; RGD:1565882; rat.
DR   CTD; 6419; -.
DR   RGD; 1565882; Setmar.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000020052; -.
DR   HOVERGEN; HBG093940; -.
DR   InParanoid; Q5I0M0; -.
DR   KO; K11433; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q5I0M0; -.
DR   PRO; PR:Q5I0M0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    315       Histone-lysine N-methyltransferase
FT                                SETMAR.
FT                                /FTId=PRO_0000259528.
FT   DOMAIN       74    137       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      140    264       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      284    300       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      150    152       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q53H47}.
FT   REGION      224    225       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        76     76       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        76     76       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        78     78       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        83     83       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        83     83       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        88     88       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        90     90       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       119    119       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       119    119       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       123    123       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       125    125       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       129    129       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       227    227       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       288    288       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       290    290       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       295    295       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   BINDING     193    193       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     221    221       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   315 AA;  35030 MW;  116FA04700614FEC CRC64;
     MSAEAVKKLS FEIAPSEEES EATIEQQDVA CGLENLPVSL WPLGAGPRPK PFQYTPDHVA
     GPGVDMDPTQ ITFPGCACIK TPCVPGTCSC LRHESNYNDN LCLRDVGSEA KYAKPVFECN
     VLCQCGEHCR NRVVQSGLQF LLQVFQTEKK GWGLRTLEYI PKGRFVCEYA GEVLGFSEVQ
     RRIHLQTAHD PNYIIALREH TYNGQVMETF VDPTYIGNIG RFLNHSCEPN LLMIPVRIDS
     MVPKLALFAA KDILPGEELS YDYSGRFLNQ ISSKDKERID CGQPRKPCYC GAQSCATFLP
     YDSSLYGPLE NPGTS
//
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