ID A0A0M0J3I5_9EUKA Unreviewed; 748 AA.
AC A0A0M0J3I5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00039449};
DE EC=2.1.1.244 {ECO:0000256|ARBA:ARBA00039112};
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00043129};
GN ORFNames=Ctob_000018 {ECO:0000313|EMBL:KOO20818.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO20818.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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 -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO20818.1}.
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DR EMBL; JWZX01003409; KOO20818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J3I5; -.
DR OrthoDB; 5471049at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd06234; M14_PaCCP-like; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008576; MeTrfase_NTM1.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR PANTHER; PTHR12753:SF0; ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1; 1.
DR Pfam; PF05891; Methyltransf_PK; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KOO20818.1};
KW Hydrolase {ECO:0000313|EMBL:KOO20818.1};
KW Protease {ECO:0000313|EMBL:KOO20818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..98
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 115..261
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
SQ SEQUENCE 748 AA; 80920 MW; 709C971AD5361536 CRC64;
MYDPRTELEG CNHMQWFAFR STVLHPYAAA DAWSTTYEIV NAGLCSYMKG WDGLEVCVSH
DLQTWRRVPS TRYDAPSGTL RWSWMHNAAQ PTTFFAYFEP YPYDRQLALV MRCASATAPG
LEVSSLGQSL GGREIDVITV GTGPLHAWII HRQHPGEPQA AFFAEGLLAR LLGLERQGSI
DGLTAQMLEA FTWHVVPSMN PDGGSAGHLR TNLAGANLNR EWAPTGSYEA PSLERSPEVY
HVLRAMQRTG VDFFCDVHGD EGLPFCFCAG NEGTPNWGPR LRALHGAFVG AYARANPDMQ
ARFGYEPDSP GGANPAVGGN QVGMRFDCLA VTLEMPFKDN AANAAARRSG KAFDGHRCAM
LGASLVDALA HVHTALRGVP VPRFELPDDA YVRPTEDVNE IRAFLDAQAR AARGAARDGQ
GEGAGGGAQG NETTILWSNN DMKGTLWTSA EQREQWYDRS KAYWEWDGLH GKGKTNDGVM
SGIGPLHDAD IADSLAFITG GLQPIWPAPF FFPDARALDV GAGIGRVAGA LLLDLCGEVD
LVDGSASHLH EARAALGEPL GEPLAPGTSE PIGGRRETIG RGRVGRYLCS DLQDFVPLAS
HPYDLIWIQW TTMYLTDADL TRLLRDCREA LAPGGVIVLK DNVIDELKGP KGLVDGRYVV
DELDASVSRT RSHLLDLVNE AGLAIVASAT ANLKSEELDG LLKNNGWSEM HPVAMLALRS
AEGPQVARSE DGIDNGDGGG SVFGWVFR
//
