ID   PPK9_SCHPO              Reviewed;         532 AA.
AC   O13945;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Protein kinase domain-containing protein ppk9;
GN   Name=ppk9; ORFNames=SPAC23H4.02;
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   IDENTIFICATION.
RX   PubMed=15821139; DOI=10.1128/ec.4.4.799-813.2005;
RA   Bimbo A., Jia Y., Poh S.L., Karuturi R.K.M., den Elzen N., Peng X.,
RA   Zheng L., O'Connell M., Liu E.T., Balasubramanian M.K., Liu J.;
RT   "Systematic deletion analysis of fission yeast protein kinases.";
RL   Eukaryot. Cell 4:799-813(2005).
RN   [3]
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
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DR   EMBL; CU329670; CAB11657.1; -; Genomic_DNA.
DR   PIR; T38326; T38326.
DR   RefSeq; NP_593404.1; NM_001018836.2.
DR   AlphaFoldDB; O13945; -.
DR   SMR; O13945; -.
DR   BioGRID; 278267; 30.
DR   STRING; 4896.SPAC23H4.02.1; -.
DR   iPTMnet; O13945; -.
DR   MaxQB; O13945; -.
DR   PaxDb; O13945; -.
DR   PRIDE; O13945; -.
DR   EnsemblFungi; SPAC23H4.02.1; SPAC23H4.02.1:pep; SPAC23H4.02.
DR   GeneID; 2541773; -.
DR   KEGG; spo:SPAC23H4.02; -.
DR   PomBase; SPAC23H4.02; ppk9.
DR   VEuPathDB; FungiDB:SPAC23H4.02; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_3_1; -.
DR   InParanoid; O13945; -.
DR   OMA; IQGRYYD; -.
DR   PhylomeDB; O13945; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SPO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-SPO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   PRO; PR:O13945; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:PomBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..532
FT                   /note="Protein kinase domain-containing protein ppk9"
FT                   /id="PRO_0000256816"
FT   DOMAIN          23..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          316..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         29..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   532 AA;  59910 MW;  43C53A20847C233C CRC64;
     MQTPSSASAE SEKDSGNTYV GPWLLGRTLG QGNLAKVKLG KHFQTNEKVA LKMVYNDELE
     DKDTWKRLQR EVTILRQLHH PNIITLYQVF RVPKYTVLAL EYMDTDLHSM VVKHNRLDEC
     TTRKIFRQIV HAIDYCHLHR VAHRDLKLEN ILLNKDLVVK LTDFGLSNFM LDGSFLSTSC
     GTPHYAAPEV IQGRYYDGCD VDVWGCGILL YLMLVGEFPF EDVTISNVLS RVCKGIYTIP
     SFVSSSASDL IRQMLMVLPT SRIKVAEIMQ HPWFIADLPT HSRLPSRTSS FSSKHRSVTF
     SPPDLAILFD PSITSPSSSV GQIPQPTDHS ALSPSKPMSI SGTESPNPDP ASLCYSSYED
     LYSATSWHSD MAESSGFLDP TDIPPIPSNV ETLRSSLPQR HASFMNKVYN HPLSRPPAPN
     RLRSLRWHYG IQTAKNPIEV LRKLCEALLE LGARFRPCDE ESFLKENKYK VFSCITCHNS
     PVYLVIELFS IGPSASVIDI RFSSSDDSIK YTSSYSPMPF LEVVKQLILK IA