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Database: UniProt
Entry: W5L904_ASTMX
LinkDB: W5L904_ASTMX
Original site: W5L904_ASTMX 
ID   W5L904_ASTMX            Unreviewed;       636 AA.
AC   W5L904;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
DE            EC=2.1.1.85 {ECO:0000256|PROSITE-ProRule:PRU00898};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000016316.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000016316.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00898};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. SETD3 actin-histidine methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00898}.
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DR   AlphaFoldDB; W5L904; -.
DR   STRING; 7994.ENSAMXP00000016316; -.
DR   Ensembl; ENSAMXT00000016316.2; ENSAMXP00000016316.2; ENSAMXG00000015854.2.
DR   eggNOG; KOG1337; Eukaryota.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; CLU_028272_0_0_1; -.
DR   InParanoid; W5L904; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000015854; Expressed in brain and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19176; SET_SETD3; 1.
DR   Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR   Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR025785; SETD3.
DR   InterPro; IPR044428; SETD3_SET.
DR   PANTHER; PTHR13271:SF47; ACTIN-HISTIDINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51565; SAM_MT85_SETD3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00898}; Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00898}.
FT   DOMAIN          120..340
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          19..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  72023 MW;  631A213BEF68D65C CRC64;
     MFMLEKKEIT PSWKRLRNPL SEHSHTMGKK SRVKTQKSGT GATAVVSPKE MMNLISELLQ
     KCSSAAPSAG KEWEEYVQIR ALVEKIRKKQ KGVSVVFEGS REDYFPELMS WAAECGASCD
     GFEISSFADE GYGLKATRDI KAEELFLWIP RKMLMTVESA KNSVLGPLYS QDRILQAMGN
     VTLALHLLCE RANPASPWLP YIKTLPSDYD TPLYFEEEEV HHLLATQAIQ DVLSQYKNTA
     RQYAYFYKVI HTHPNASKLP LKDAFTFDDY RWAVSSVMTR QNQIPTEDGS RVTLALIPLW
     DMCNHTNGLI TTGYNLEDDR CECVALQDYK ENEQIYIFYG TRSNAEFVIH NGFFFEDNAH
     DRVKIKLGVS KSERLYAMKA EVLARAGIPA SSIFALHCSE PPISAQLLAF LRVFCMTEEE
     LKDYLVGDHA INKIFTLGNT EFPVSWENEI KLWTFLETRA TLLLKTYKTT SEEDRSILQK
     PDLSLHSRVA VKLRLAEKEI LERAVSSGRN KRLHFQKQLE EGSPLPLYEE SDIALLENAD
     AKLPIILRKL DEEDEHAAEA EAHNALLESA QTPPPPLPLL LNGQSKEEVN GNLEEEEEED
     GGKRLQATAK GKEEASSQRE EPSSQRTEDA SKDKGE
//
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