ID A0A2U3Y9I4_LEPWE Unreviewed; 370 AA.
AC A0A2U3Y9I4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|ARBA:ARBA00012533};
DE EC=2.1.1.85 {ECO:0000256|ARBA:ARBA00012533};
GN Name=METTL18 {ECO:0000313|RefSeq:XP_006740384.1,
GN ECO:0000313|RefSeq:XP_030891470.1, ECO:0000313|RefSeq:XP_030891471.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006740384.1};
RN [1] {ECO:0000313|RefSeq:XP_006740384.1, ECO:0000313|RefSeq:XP_030891470.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006740384.1,
RC ECO:0000313|RefSeq:XP_030891470.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000256|ARBA:ARBA00038126}.
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DR RefSeq; XP_006740384.1; XM_006740321.2.
DR RefSeq; XP_030891470.1; XM_031035610.1.
DR RefSeq; XP_030891471.1; XM_031035611.1.
DR STRING; 9713.A0A2U3Y9I4; -.
DR GeneID; 102730574; -.
DR KEGG; lww:102730574; -.
DR CTD; 92342; -.
DR OrthoDB; 276605at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR PANTHER; PTHR14614:SF39; HISTIDINE PROTEIN METHYLTRANSFERASE 1 HOMOLOG; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR Pfam; PF06325; PrmA; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|RefSeq:XP_006740384.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|RefSeq:XP_006740384.1}.
FT REGION 15..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41526 MW; 13AA35465F6F910D CRC64;
MTFQFNFTIE NHLENESTPL GDGALALDSS KGPSVSESKK GKHRDRKCST EQFDWPQDHL
SEHKPVGNAA ASQDTDRSLS AANSSNNLEP HEKHPCMSVA KEHPMPKDLK KVLENKVVET
LSGPQHVNVS IVKTILFKEN FPGENIVSQS ISSHSDLITG VYEGGLKIWE CTFDLLAYFT
KANVKFAGKK VLDLGCGSGL LGIVAFKGGA KEIHFQDYNS MVIDEVTLPN VVANSTLEGE
GNDVNEPDVK RCRKSKITQE LCKCRFFSGE WSEFCKLVLS SEKFFEKYDL ILTSETIYNP
DYYDTLHQTF LRLLDKNGRV LLASKAHYFG VGGGIHLFQK FVEERNVFET RTLEIIDEGL
KRFLIEMAFK
//
