ID   PPK29_SCHPO             Reviewed;         872 AA.
AC   Q9USS2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Serine/threonine-protein kinase ppk29;
DE            EC=2.7.11.1;
GN   Name=ppk29; ORFNames=SPBC557.04;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-596 AND SER-657, AND
RP   IDENTIFICATION BY 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CU329671; CAB60671.1; -; Genomic_DNA.
DR   PIR; T50369; T50369.
DR   RefSeq; NP_596027.1; NM_001021936.2.
DR   AlphaFoldDB; Q9USS2; -.
DR   SMR; Q9USS2; -.
DR   BioGRID; 277595; 27.
DR   STRING; 4896.SPBC557.04.1; -.
DR   iPTMnet; Q9USS2; -.
DR   SwissPalm; Q9USS2; -.
DR   MaxQB; Q9USS2; -.
DR   PaxDb; Q9USS2; -.
DR   PRIDE; Q9USS2; -.
DR   EnsemblFungi; SPBC557.04.1; SPBC557.04.1:pep; SPBC557.04.
DR   PomBase; SPBC557.04; ppk29.
DR   VEuPathDB; FungiDB:SPBC557.04; -.
DR   eggNOG; KOG1989; Eukaryota.
DR   HOGENOM; CLU_016628_0_0_1; -.
DR   InParanoid; Q9USS2; -.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q9USS2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030479; C:actin cortical patch; ISO:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:PomBase.
DR   GO; GO:0023052; P:signaling; IC:PomBase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..872
FT                   /note="Serine/threonine-protein kinase ppk29"
FT                   /id="PRO_0000256826"
FT   DOMAIN          25..310
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          339..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..380
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         657
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   872 AA;  96126 MW;  CFB18B3A19A2D867 CRC64;
     MSVASFLTGE KLLAGSKFVI GKYNVTIEKY IAEGGFSHVY LVQTNSKTDG SPITAVLKRM
     YSPDENALRF VKTEIETMEL LKSNPHVVSY IDSCIFPLEK AGVNTGFEIL LLMEYCAGGG
     LIDFMNQRLQ TRLSEHEVLK IISDIVQGVA SLHYLRPPLI HRDLKVENVL LSFNTFKLCD
     FGSVTEPMHA AENSSEIQAL EKSINTFTTY QYRAPEMINL YSGLGIDEKS DMWALGVLLY
     KLCYYTTPFE TQGPNAILTA SYSFPPFPPY SHSLKNVIIA LLQPNPCLRP NIFQLMCEIC
     RLRGTALPFR DIYSGRESSF YDLHNRKIMS LLRQTTTTPF AGNQVMPTPQ VQGSRPPPPP
     PMPAPIYNVP NVPTVPTVSP NPFLQPTFSG TSQASAHPSI HSQSATFNNT QDVNRQSVSS
     PKVVSSSSVT GSGASGRKVY TPQSKNPFPI SQGVTGTSSK FSASEVTEDN GSPNAGLDAD
     NVDVEEVVNQ RYPDLNELES QLTSHTNITT SSHHNPREQE IAKLADDAFA SFRQTAGTST
     ANSTHTTGTQ DISAFDTNFS EGVGSVRSSF DFPDRPVSRR PSSTSRSSVK ITGPSSPNAR
     SMAYEQHSFN LDDLSNTNFG SNNSLRHAKS FSKYYSPSHK DSNKTSRNTS KEGLPSSPTM
     LYRTTSNTRG DYIVQRTQQS ANPLTNIEPQ DMSNLSTDIN ASDVVADSTN SILYPTSTAS
     SVANTIASDV DDFGTFNGLQ RTVSLHSERA SLDKKRPSFH DKNPYFKFSP SKYVDEGLEG
     ESELRERVRS YANRSSSSFH NPDLTDTEIQ ETSFNNDLRP VASIQSAETS RSVSDRPANF
     PEELNDTLFE QKYPGIVDYE EPNSNAEKNV NI