ID   NTO1_SCHPO              Reviewed;         767 AA.
AC   O74759;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Mst2 complex subunit nto1;
GN   Name=nto1; ORFNames=SPBC17D11.04c;
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP   AND FUNCTION.
RX   PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA   Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA   Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA   Jia S.;
RT   "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT   damage checkpoint in fission yeast.";
RL   J. Biol. Chem. 287:4386-4393(2012).
CC   -!- FUNCTION: Component of the mst2 complex which is a highly specific H3
CC       lysine 14 (H3K14) acetyltransferase that functions together with gcn5
CC       to regulate global levels of H3K14 acetylation (H3K14ac), critical for
CC       DNA damage checkpoint activation. {ECO:0000269|PubMed:22184112}.
CC   -!- SUBUNIT: Component of the mst2 complex composed of at least eaf6, mst2,
CC       nto1, pdp3, ptf1, ptf2 and tfg3. {ECO:0000269|PubMed:22184112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000305|PubMed:16823372}.
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DR   EMBL; CU329671; CAA21075.1; -; Genomic_DNA.
DR   PIR; T39715; T39715.
DR   RefSeq; NP_596378.1; NM_001022299.2.
DR   AlphaFoldDB; O74759; -.
DR   SMR; O74759; -.
DR   BioGRID; 276615; 68.
DR   STRING; 4896.SPBC17D11.04c.1; -.
DR   MaxQB; O74759; -.
DR   PaxDb; O74759; -.
DR   PRIDE; O74759; -.
DR   EnsemblFungi; SPBC17D11.04c.1; SPBC17D11.04c.1:pep; SPBC17D11.04c.
DR   GeneID; 2540077; -.
DR   KEGG; spo:SPBC17D11.04c; -.
DR   PomBase; SPBC17D11.04c; nto1.
DR   VEuPathDB; FungiDB:SPBC17D11.04c; -.
DR   eggNOG; KOG0955; Eukaryota.
DR   HOGENOM; CLU_363352_0_0_1; -.
DR   InParanoid; O74759; -.
DR   OMA; CMINKNR; -.
DR   PhylomeDB; O74759; -.
DR   PRO; PR:O74759; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0036410; C:Mst2 histone acetyltransferase complex; TAS:PomBase.
DR   GO; GO:0033100; C:NuA3 histone acetyltransferase complex; ISO:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; NAS:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF10513; EPL1; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; DNA damage; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..767
FT                   /note="Mst2 complex subunit nto1"
FT                   /id="PRO_0000303918"
FT   ZN_FING         194..244
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         248..281
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         305..363
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          724..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  88257 MW;  94664AA082E74245 CRC64;
     MQTFRLTSTG RNILRPDELA FQPREEIPYK SFHPDLQIDE PLEILEGDHT QYAGLRDSLV
     TYKSENSYVL KALLNAKIEN VKPVGVQTEN INPQEKKFGY KTAKQLDWSP DEYFKFVAIH
     PYSKTSFPVS YDLDELDTMW LTYYNEFQLS SNSEWENVSK EFLEIVLTII EREWLYLEAW
     MPKIEPVRVE DELDGRCVIC NEAECENSNA IVFCDNCNTS VHQNCYGIPF VPEGQWFCKK
     CLLAPHEVIC CAFCPDRDGA FCTTLDGRWC HTICAIAIPE ISFHDTSRLD LVRNIASIPK
     SRWKLVCCIC KLRWGTCVQC SDKNCYAAYH ITCARRAGFF YKIYSHSASY DSVDMETYCD
     KHTPPDYLNG LMKRLFPLAE LYYKRMATDV PLNFQATKAP DFVPEGPWKS HPLPAFIVDK
     VTKVLLSYNV KRQDLPSIVT DICKFYHMKR RSRKDAPLLK SQLLMDSLEN LPVRASKDRV
     RSLEVAKALQ DQYQSLLTLV ESTAKRQLLK CQLSNLRKKF LNLNYFPAQR LLQDTLVKII
     DLDVDGLFNM PLDNGWIGWV ELKRQVFSYQ IGSISSLEKK LEPIWDVDGV IQCIDDMEQL
     TAMVQFAQKT EGEVKKLFIK AKIYFESLSL DERGNLKVPS LGINGLEYDN WPGLNELEMS
     QLDIPSQGNL KSLHDFIEGL DLNEKIGKFP ISMFQNQVAQ FSTIEIPKMS GRANGMHNFH
     SEDVTGQSNH ALPNSVTKKN GTKQPYTKNS LPFNERITRS KAKKNYS