ID   YOP2_SCHPO              Reviewed;         695 AA.
AC   Q9Y7X2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=N-terminal acetyltransferase A complex subunit-like protein C418.02;
DE            Short=NatA complex subunit-like protein C418.02;
GN   ORFNames=SPBC418.02;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Non-catalytic component of the NatA N-terminal
CC       acetyltransferase, which catalyzes acetylation of proteins beginning
CC       with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal
CC       eukaryotic translation and processing, protect against proteolytic
CC       degradation and protein turnover (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC       complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329671; CAB51353.1; -; Genomic_DNA.
DR   PIR; T40451; T40451.
DR   RefSeq; NP_596495.1; NM_001022415.2.
DR   AlphaFoldDB; Q9Y7X2; -.
DR   SMR; Q9Y7X2; -.
DR   BioGRID; 277327; 13.
DR   STRING; 4896.SPBC418.02.1; -.
DR   MaxQB; Q9Y7X2; -.
DR   PaxDb; Q9Y7X2; -.
DR   EnsemblFungi; SPBC418.02.1; SPBC418.02.1:pep; SPBC418.02.
DR   GeneID; 2540808; -.
DR   KEGG; spo:SPBC418.02; -.
DR   PomBase; SPBC418.02; -.
DR   VEuPathDB; FungiDB:SPBC418.02; -.
DR   eggNOG; KOG1156; Eukaryota.
DR   HOGENOM; CLU_006686_1_1_1; -.
DR   InParanoid; Q9Y7X2; -.
DR   OMA; YLAETEC; -.
DR   PhylomeDB; Q9Y7X2; -.
DR   PRO; PR:Q9Y7X2; -.
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:0031415; C:NatA complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR   GO; GO:0051604; P:protein maturation; NAS:PomBase.
DR   InterPro; IPR021183; NatA_aux_su.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF12569; NARP1; 1.
DR   PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; Repeat; TPR repeat; Transferase.
FT   CHAIN           1..695
FT                   /note="N-terminal acetyltransferase A complex subunit-like
FT                   protein C418.02"
FT                   /id="PRO_0000363382"
FT   REPEAT          8..41
FT                   /note="TPR 1"
FT   REPEAT          43..75
FT                   /note="TPR 2"
FT   REPEAT          76..109
FT                   /note="TPR 3"
FT   REPEAT          111..143
FT                   /note="TPR 4"
FT   REPEAT          145..177
FT                   /note="TPR 5"
FT   REPEAT          217..250
FT                   /note="TPR 6"
FT   REPEAT          262..296
FT                   /note="TPR 7"
FT   REPEAT          365..398
FT                   /note="TPR 8"
FT   REPEAT          399..432
FT                   /note="TPR 9"
FT   REPEAT          477..510
FT                   /note="TPR 10"
SQ   SEQUENCE   695 AA;  81069 MW;  8746D163A26DC872 CRC64;
     MSKLSEKEAF LFDRSIDQFE KGQYSKSLKT IQSVLKKKPK HPDSVALLGL NLCKLHDSRS
     ALLKCGYASS IDPKSQFCWH ALAIVYRETK DYNNSLKCYQ NALAISPNNE SLWYDAAYLQ
     AQLGLYQPLF DNWNRLLQLD SSNLEYRLCF TLSAFLSGNY KESLEQIQYL ISSCNLSPLV
     VSRLISFLPR ICEHIENGSQ TVLEILLMNQ NSFLNNFNFE HIKADFAFRQ KNYEESIYLY
     ARLLIKFPNR LDYSEKYLNS LWNFYKSGGL ALDLLLKRTD SLIKTFSEIL QTGISVLIFL
     LSKNLDYDFC LNHLISYSMH HFIPSFISLL KIPLKTNDAF SKKLITMLSN FREGDSAKNI
     PTHKLWCTYC LCLAHYKLGD YEESNYWLNL AIDHTPTYPE LFLAKAKIFL CMGEIEEALC
     SFKRSVELDK SDRALASKYA KYLIRMDRNE EAYIVLSKFS RFRFGGVCNY LAETECVWFL
     VEDGESLLRQ KLYGLALKRF HSIYQIYKKW SFLKFDYFTQ CAEDGEFQEY VELVEWSDNL
     WSSTDYLRAT LGALTIYLLL FESKFNMYGN KAEEISHMSE VEQIAYARED NKKIMKLQKI
     EEDKIKSYIP SESEEPLVID EDYFGHKLLI TDDPLTEAMR FLQPICWHKI KGWGFLKILS
     SKLYKLKGII FCYYALTNNI EGLHQKANSL ETSVL