MET18_DICDI
ID MET18_DICDI Reviewed; 309 AA.
AC Q55DL2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Histidine protein methyltransferase 1 homolog {ECO:0000305};
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:O95568};
DE AltName: Full=Protein METTL18 homolog {ECO:0000250|UniProtKB:O95568};
GN ORFNames=DDB_G0270580;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Protein-L-histidine N-tele-methyltransferase that probably
CC monomethylates RPL3. Through the methylation of RPL3 may regulate the
CC dynamics of pre-rRNA processing, ribosome biogenesis, and translation.
CC {ECO:0000250|UniProtKB:O95568}.
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:0000250|UniProtKB:O95568};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC Evidence={ECO:0000250|UniProtKB:O95568};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95568}. Nucleus {ECO:0000250|UniProtKB:O95568}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:O95568}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72640.1; -; Genomic_DNA.
DR RefSeq; XP_646119.1; XM_641027.1.
DR AlphaFoldDB; Q55DL2; -.
DR SMR; Q55DL2; -.
DR STRING; 44689.DDB0304996; -.
DR PaxDb; Q55DL2; -.
DR EnsemblProtists; EAL72640; EAL72640; DDB_G0270580.
DR GeneID; 8617068; -.
DR KEGG; ddi:DDB_G0270580; -.
DR dictyBase; DDB_G0270580; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_038704_0_0_1; -.
DR InParanoid; Q55DL2; -.
DR OMA; DINRAKY; -.
DR PhylomeDB; Q55DL2; -.
DR PRO; PR:Q55DL2; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042038; P:peptidyl-histidine methylation, to form tele-methylhistidine; IBA:GO_Central.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..309
FT /note="Histidine protein methyltransferase 1 homolog"
FT /id="PRO_0000328433"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 179..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 209..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
SQ SEQUENCE 309 AA; 35229 MW; 51F8502DBBDF5D18 CRC64;
MSFKFNFQVD EDENDNGNNN EQNNEESKLD ISEFDSSSKM DELPSKYIDL RNNLSSLLSN
VETEIVTFSS NNKLKKLVKP FKGNQDNNND NNVNSNDKND NNNNNNNNNK DYEKLLDKTD
LIPGVYEGGF KLWECSIDII NYLFEEKIDL SGKKVLEIGC GHGLPGIYCL LNGSIVTFQD
YNEEVIYNLT QPNVLINGGD INRAKYISGD WKFVDQLLKN EKFDIILTSD TLYNVGSFKK
LYNLISNHLE SNGKCYLASK TYYFGVGGGI RKFEELLKIL NRLSIKTVRD IKDGLSNVRE
VVEITNKIN
