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Database: UniProt
Entry: A0A068YCA2_ECHMU
LinkDB: A0A068YCA2_ECHMU
Original site: A0A068YCA2_ECHMU 
ID   A0A068YCA2_ECHMU        Unreviewed;       505 AA.
AC   A0A068YCA2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
DE            EC=2.1.1.85 {ECO:0000256|PROSITE-ProRule:PRU00898};
GN   ORFNames=EmuJ_000849700 {ECO:0000313|EMBL:CDS40894.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS40894.1};
RN   [1] {ECO:0000313|EMBL:CDS40894.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDS40894.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; LN902841; CDS40894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YCA2; -.
DR   STRING; 6211.A0A068YCA2; -.
DR   eggNOG; KOG1337; Eukaryota.
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};
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          108..330
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
SQ   SEQUENCE   505 AA;  57810 MW;  B5ECDEE5505F9A0C CRC64;
     MLLCVFGSEH QSCLILTCQR SFKMEKKTRL HVKDSSSCVA DLCSELLRLC DVRPDVWNKM
     NYFRSLYEIV TKIRDLQKGA SISRLVLSGD RELRLKALQK RYEECLYFPL SICNCGEAGF
     GVRADKSIEK NSPLLHIPLR YALSVPNVSS PLPKFLKEDP LFSGMDNVAL AIALLHELSL
     NEKSRWKEYI SSLPGVYSTV AYFSDAEFSI LDGFPAADAA LKAYRNMCRQ YAYFYRLFER
     VEQKDSLPVY MKPFCFEDYQ WAISTVMSRN NALPIKGDSD GKLLCLIPLW DMINHKQYQV
     TTDYDPVSEH IVFYAMESHR QGDEIFMDYG KRTSTEFLLY NGFVPEFNLF HKVPINLGLS
     KFDKLMQLRT QILKELGLGS EICLAASPQV GTFPPSQLTA FARVFVMNEV ELQVTLDELT
     SLRSGSDVTD RLLSMTLSNG RVDEEAKKFV ESRIKLLIRN YESRLEKSLQ LVPTASPIRE
     QCLRLCRHDI FTLSQCLAAL SEQSR
//
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