ID   PPK19_SCHPO             Reviewed;        1706 AA.
AC   O42900;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Serine/threonine-protein kinase ppk19;
DE            EC=2.7.11.1;
GN   Name=ppk19; ORFNames=SPBC119.07;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957 AND TYR-958, 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   -!- 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; CAA17922.1; -; Genomic_DNA.
DR   PIR; T39305; T39305.
DR   RefSeq; NP_595288.1; NM_001021195.2.
DR   AlphaFoldDB; O42900; -.
DR   SMR; O42900; -.
DR   BioGRID; 276540; 6.
DR   STRING; 4896.SPBC119.07.1; -.
DR   iPTMnet; O42900; -.
DR   MaxQB; O42900; -.
DR   PaxDb; O42900; -.
DR   PRIDE; O42900; -.
DR   EnsemblFungi; SPBC119.07.1; SPBC119.07.1:pep; SPBC119.07.
DR   GeneID; 2539996; -.
DR   KEGG; spo:SPBC119.07; -.
DR   PomBase; SPBC119.07; ppk19.
DR   VEuPathDB; FungiDB:SPBC119.07; -.
DR   eggNOG; KOG1240; Eukaryota.
DR   HOGENOM; CLU_001696_0_1_1; -.
DR   InParanoid; O42900; -.
DR   OMA; FPESEYE; -.
DR   PhylomeDB; O42900; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-SPO-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; R-SPO-1660517; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR   PRO; PR:O42900; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0071561; C:nucleus-vacuole junction; IBA:GO_Central.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:PomBase.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IDA: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; ISO:PomBase.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISO:PomBase.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   Gene3D; 1.25.10.10; -; 2.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045162; Vps15-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR17583; PTHR17583; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW   WD repeat.
FT   CHAIN           1..1706
FT                   /note="Serine/threonine-protein kinase ppk19"
FT                   /id="PRO_0000256820"
FT   DOMAIN          24..293
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          56..94
FT                   /note="HEAT 1"
FT   REPEAT          426..465
FT                   /note="HEAT 2"
FT   REPEAT          466..504
FT                   /note="HEAT 3"
FT   REPEAT          511..549
FT                   /note="HEAT 4"
FT   REPEAT          587..625
FT                   /note="HEAT 5"
FT   REPEAT          626..664
FT                   /note="HEAT 6"
FT   REPEAT          665..703
FT                   /note="HEAT 7"
FT   REPEAT          705..743
FT                   /note="HEAT 8"
FT   REPEAT          1213..1252
FT                   /note="WD 1"
FT   REPEAT          1368..1407
FT                   /note="WD 2"
FT   REPEAT          1577..1622
FT                   /note="WD 3"
FT   REGION          982..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1431..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1076
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         30..38
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"
FT   MOD_RES         957
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         958
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1706 AA;  191094 MW;  BFB1676379C74634 CRC64;
     MGIQLSTIQT PQFHELFEEE LPEYHNERSL GDSHFLRTFR MQDRKGYDVL IKVFVNKLPE
     ISLSSIVNLL KEEQENISYR VPNAVPYIKT LVTLRAAYLV RPYVTHNLYD RISTRPFLEL
     TEKKWIMFQL LKGISDCHRL GVCHGDIKSE NILITSWNWA YLSDFSSFKP TYLPEDNPAD
     YGYFFDTSSR RVCNIAPERF VPASQLQPAP LSPAMDIFSL GCVFAELLLE ESPLFTLSQL
     FSYKAHGSYD LQSVLEQIED KSTQNMILSM LDRDPSQRLS ADAYLQKYRG TVFPACFYDT
     LYDYCIGLVD PSGILSAKQP NDACSLYGSR IDDIYRDIMP PNNNDISNLM HTPHEYNGID
     SYSVPLFTTL DEFYNKNPAA KNWYLRLYNT MQEKKGFEDK EQGSTPAPSP SVIEDISSIE
     TDENHLYGAA VLLPIVLSTI RHVNTRESKI NALSLVQILS RNICDESKLD TVLPFVMTLL
     RDQYADVRIS ALITITRLVS NVTSIAPINA FLFQEYLFPD LQHFLFDMNS RTRATYASCL
     PILAKQASKF LNLAQSLRNA GILSFPESEY ENINHGKAEL LFETGRHDLV VTVERHVSTL
     LADSSSIVRR SLLNALAPLC VFFGKAKSND LILSHLITYL NDTDWMLRCA FFESITGLSI
     FIGPRSVDEY ILPLMLQALV DPEPAVLESV LGSFSGLIEL HLFEKLVVVD ILQLVLPLVA
     VPNAYIRRAA LSVIYSAYQS FDDIDRDCIV TPLLRPYLMS NLCDINSLEK LDQFILPMVS
     DSVWSTLTRW YEESENSSFW KCDKDASYSS LDVSNDSLLG RTKNLQKREI MHHAEVYTHK
     KISLTGHVII TSTEMLELSE DDQKWADIIK EMGVDVKHLW VLANLRDYVK KTKINLNGIN
     YKRQSGLREL NTYPNAPLHI LPETIFWNPE RPPSSSIANE TFLDRNSYAE SIQTSRSYND
     DLIARDPIAY VGTDMTNAFG TTTKPKDVSQ SDIKVDINRE SNSDNGETIT GTHDVYRQTD
     NPEIKLPSDT ASSKVDTHNP TVTQPTDDTG GLNSYNTENP LLTNNTLEPS SVEAIVSSKD
     SDKHAKESKG KSLAPLISSR VSTNDTTNVA GIRSQRSFTT HIDLKKLTTR QNGAKKSSYT
     GTNPCVLNYL NKIYAEAAAS TLNVGAAVSP SWASNIPLRR RTKVSAKAAN KIVQTHEWHP
     EGSRVAQIYL GSLLDGGTKK VLVSPDSSFF VTLGSDGVVR AWQLVESVRH ISTMRCECRL
     SYGHTRRNGE RNRFSVVNGC FLGNTYAFAS VTQDGSVEVH RLDVNNQRHT LISAGRIPNL
     DFSDSVTSME ASTFHDGSIR LVVVTKWSRI VYLDVGMMRV LSSDQLPLQC GSATSVVVSE
     GCNWALIGTT KGWLLLWDLR FGTLSCSWHM PARIDQMHLL LDVTKKRSNV NEYTSGNNNS
     PVTKVPGSSS TSSSSTQPIN STIPINPLEN HGMLNSFGST TVSISFSVLT NLDNKEVNLE
     DAVPASHRSA SGIVNFDVEK GKTEEVFLEN WNSSLTSPIP VSVGIDAFNE KKKFDIDSGN
     DMGLRDLNTK FDSPWPCISS PIYRYRGPSA GSVEREPLFL IAASGSPHAF IWNPHNVSAS
     SSVTNDSESS KLSLIHNKPP IYQKVSEQQN VRPKSSGVSR PLLFLQQQKN LPSENRLHPI
     VDMAFLYQPY AIVLIVDAFG SLELWT