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Database: UniProt
Entry: A0A3B1K7Y5_ASTMX
LinkDB: A0A3B1K7Y5_ASTMX
Original site: A0A3B1K7Y5_ASTMX 
ID   A0A3B1K7Y5_ASTMX        Unreviewed;       610 AA.
AC   A0A3B1K7Y5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:ENSAMXP00000050195.1, 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:ENSAMXP00000050195.1}
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   Ensembl; ENSAMXT00000052960.1; ENSAMXP00000029242.1; ENSAMXG00000015854.2.
DR   Ensembl; ENSAMXT00000056513.1; ENSAMXP00000050195.1; ENSAMXG00000015854.2.
DR   GeneTree; ENSGT00940000153577; -.
DR   OrthoDB; 51002at2759; -.
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          94..314
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          541..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  68844 MW;  AAA99038D4D8988A CRC64;
     MGKKSRVKTQ KSGTGATAVV SPKEMMNLIS ELLQKCSSAA PSAGKEWEEY VQIRALVEKI
     RKKQKGVSVV FEGSREDYFP ELMSWAAECG ASCDGFEISS FADEGYGLKA TRDIKAEELF
     LWIPRKMLMT VESAKNSVLG PLYSQDRILQ AMGNVTLALH LLCERANPAS PWLPYIKTLP
     SDYDTPLYFE EEEVHHLLAT QAIQDVLSQY KNTARQYAYF YKVIHTHPNA SKLPLKDAFT
     FDDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDYKENEQIY IFYGTRSNAE FVIHNGFFFE DNAHDRVKIK LGVSKSERLY AMKAEVLARA
     GIPASSIFAL HCSEPPISAQ LLAFLRVFCM TEEELKDYLV GDHAINKIFT LGNTEFPVSW
     ENEIKLWTFL ETRATLLLKT YKTTSEEDRS ILQKPDLSLH SRVAVKLRLA EKEILERAVS
     SGRNKRLHFQ KQLEEGSPLP LYEESDIALL ENADAKLPII LRKLDEEDEH AAEAEAHNAL
     LESAQTPPPP LPLLLNGQSK EEVNGNLEEE EEEDGGKRLQ ATAKGKEEAS SQREEPSSQR
     TEDASKDKGE
//
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