NMT_SCHPO
ID NMT_SCHPO Reviewed; 466 AA.
AC O43010;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97;
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT;
DE AltName: Full=Peptide N-myristoyltransferase;
GN Name=nmt1; ORFNames=SPBC2G2.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17891.1; -; Genomic_DNA.
DR PIR; T40150; T40150.
DR RefSeq; NP_596440.1; NM_001022359.2.
DR AlphaFoldDB; O43010; -.
DR SMR; O43010; -.
DR STRING; 4896.SPBC2G2.11.1; -.
DR iPTMnet; O43010; -.
DR MaxQB; O43010; -.
DR PaxDb; O43010; -.
DR PRIDE; O43010; -.
DR EnsemblFungi; SPBC2G2.11.1; SPBC2G2.11.1:pep; SPBC2G2.11.
DR GeneID; 2540407; -.
DR KEGG; spo:SPBC2G2.11; -.
DR PomBase; SPBC2G2.11; -.
DR VEuPathDB; FungiDB:SPBC2G2.11; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; O43010; -.
DR OMA; RDWHVGV; -.
DR PhylomeDB; O43010; -.
DR Reactome; R-SPO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:O43010; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; ISS:PomBase.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; NAS:PomBase.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000903; NMT.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR PANTHER; PTHR11377; PTHR11377; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR PIRSF; PIRSF015892; N-myristl_transf; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..466
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064247"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 51..54
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 185..187
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 193..197
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 466 AA; 53696 MW; 307B42A7EA33BA61 CRC64;
MDNENNKNTK NSQQDSSFSE GGIRELLDRL ALRSLIEKEE AAAPPKTYED FKFWKTQPVP
KFDDECTQEG PIDPNTDINQ VPREPYRLLK EFEWATIDVT NDNELSEVHE LLTENYVEDA
TAMLRFAYIS EFLRWALMPP GYVKEWHVGV RVKSSRKLVA FISAVPLSIR VRDKIIKKCA
EVNFLCIHKK LRSKRLTPLL IKEVTRRCHL ENVWQAVYTA GVLLPSPVSL SRYMHRSLNW
KKLYDIGFAP FPLGSTEKKE TAKYHLPPNT QTPGLRPMEL KDVPAVQSLL SQYMERFELA
HLFSEEEVRH WFLYTDKVSS GPVVWSYVVE NPESKKITDF FSFYSLPSTV IGNPKYKDIQ
AAYLYYYASD SCPKDLSSES QLAFVERCKL IVNDALILAK KFHFDVFNAV TVLDNNLFLK
DLKFGEGDGF LNYYIYNYNC PKIPGGIDAS KSVDYSRPSG MGFVMI
