ID A0A091DNQ3_FUKDA Unreviewed; 425 AA.
AC A0A091DNQ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1 {ECO:0000256|ARBA:ARBA00040761};
DE EC=2.1.1.244 {ECO:0000256|ARBA:ARBA00039112};
DE AltName: Full=Alpha N-terminal protein methyltransferase 1A {ECO:0000256|ARBA:ARBA00041207};
DE AltName: Full=Methyltransferase-like protein 11A {ECO:0000256|ARBA:ARBA00042768};
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A {ECO:0000256|ARBA:ARBA00041385};
GN ORFNames=H920_06671 {ECO:0000313|EMBL:KFO31920.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31920.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO31920.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO31920.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-
CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00035913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-
CC lysyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54736,
CC Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059,
CC ChEBI:CHEBI:138318; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00036157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-
CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00036171};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000256|ARBA:ARBA00009059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN122233; KFO31920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DNQ3; -.
DR STRING; 885580.ENSFDAP00000016325; -.
DR eggNOG; KOG3178; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; IPR008576; MeTrfase_NTM1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR PANTHER; PTHR12753:SF1; N-TERMINAL XAA-PRO-LYS N-METHYLTRANSFERASE 1; 1.
DR Pfam; PF05891; Methyltransf_PK; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:KFO31920.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO31920.1}.
FT REGION 24..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46329 MW; D393694A41DC8E0D CRC64;
MAKPLLAVGS TGLEDLPLLA QGPSHAWPVA ESSTNPGPHG DPRTQGWEEG HRVDGDGQGL
LRQLRVTVRK LCDRQSLSFP SPRASAVPRP HCWGAGQEQD PGCRAPTRDV PGQTAQGRGH
WEDPQGCGTP GVLRGGRVQQ EEEEEEEEED AGERGKQQAS PPLLGHEACS AAGAGRCLIS
PGLDSLGSAP ALPGGAGLRR GSMTSEVIED EQQFYSKAES YWKQIPPTVD GMLGGYGHIS
SIDLSSSRKF LQRFLREGPN KPGTSCALDC GAGIGRITKR LLLPLFEVVD MVDVTEDFLA
KAKTYLGEEG RRVRNYFCCG LQDFSPEPGS YDVIWIQWVI GHLTDQHLAE FLQRCKRGLR
PNGLIIIKDN MAQEGVILDD VDSSVCRDLQ VVRRIVRSAG LSLLAEERQE NLPDEIYHVY
SLALR
//
