MET18_BOVIN
ID MET18_BOVIN Reviewed; 373 AA.
AC Q2KIJ2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Histidine protein methyltransferase 1 homolog {ECO:0000305};
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:O95568};
DE AltName: Full=Methyltransferase-like protein 18;
GN Name=METTL18;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-L-histidine N-tele-methyltransferase that
CC specifically monomethylates RPL3. Through the methylation of RPL3
CC regulates the dynamics of pre-rRNA processing, ribosome biogenesis, and
CC translation. {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 -!- SUBUNIT: Interacts with GRWD1 and members of the heat shock protein 90
CC and 70 families; these proteins may possibly be methylation substrates
CC for the enzyme. {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 -!- PTM: Monomethylated at His-154 through automethylation. Automethylation
CC at His-154 positively regulates the methyltransferase activity toward
CC RPL3. Probably methylated on other residues.
CC {ECO:0000250|UniProtKB:O95568}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000305}.
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DR EMBL; BC112618; AAI12619.1; -; mRNA.
DR RefSeq; NP_001073825.1; NM_001080356.2.
DR RefSeq; XP_005216978.1; XM_005216921.1.
DR RefSeq; XP_005216979.1; XM_005216922.3.
DR AlphaFoldDB; Q2KIJ2; -.
DR SMR; Q2KIJ2; -.
DR STRING; 9913.ENSBTAP00000028878; -.
DR PaxDb; Q2KIJ2; -.
DR PRIDE; Q2KIJ2; -.
DR GeneID; 783955; -.
DR KEGG; bta:783955; -.
DR CTD; 92342; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_038704_0_1_1; -.
DR InParanoid; Q2KIJ2; -.
DR OrthoDB; 803097at2759; -.
DR TreeFam; TF320884; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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 GO; GO:0090069; P:regulation of ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:2000232; P:regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; 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 2: Evidence at transcript level;
KW Cytoplasm; Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..373
FT /note="Histidine protein methyltransferase 1 homolog"
FT /id="PRO_0000247198"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 247..253
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT COMPBIAS 33..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 216..218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 269..271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 154
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
SQ SEQUENCE 373 AA; 42101 MW; E44319A234B0D235 CRC64;
MTFQFNFTIE DHLEDELTSL GDGALALHSS KESLVSERQK GTHRDKKCST EQSDLLQDHL
WEHKSERNEA PSQDPDSSFG AANSSSNLEP HEEKPCLKVA KEHAVPKDLK KVLENKVTET
LPGLQHVNIS IMKTTLLKEN FPGENIISKS FSSHSDLISG VYEGGLKIWE CTFDLLAYLT
KAKVKFAGKK VLDLGCGSGL LGIMALKGGA KEIHFQDYNS VVIDEVTLPN VVANSTLEDE
ENDVNEPDVK RLRRSTVAQE LCKCRFFSGE WSEFCKLVLS SEKLFEKYDL ILTSETIYNP
DYYVPLHQTF LRLLDKNGQV LLASKVHYFG VGGGTHLFQK FVEERNVFET RTLEIIDEGL
KRCLIEMTFK YPT
