ID   PPK21_SCHPO             Reviewed;         551 AA.
AC   Q9Y7J6; O43064;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Serine/threonine-protein kinase ppk21;
DE            EC=2.7.11.1;
GN   Name=ppk21; ORFNames=SPBC1778.10c, SPBC4C3.11;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY
RP   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}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
CC       Note=Located at the cell tips and septum.
CC   -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC       by the enzyme for the binding to the hydrophobic motif of its
CC       substrates. It is an allosteric regulatory site that can accommodate
CC       small compounds acting as allosteric inhibitors.
CC       {ECO:0000250|UniProtKB:O15530}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PDPK1 subfamily. {ECO:0000305}.
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DR   EMBL; CU329671; CAB39805.3; -; Genomic_DNA.
DR   PIR; T40486; T40486.
DR   RefSeq; XP_001713142.2; XM_001713090.2.
DR   AlphaFoldDB; Q9Y7J6; -.
DR   SMR; Q9Y7J6; -.
DR   BioGRID; 276357; 53.
DR   STRING; 284812.Q9Y7J6; -.
DR   iPTMnet; Q9Y7J6; -.
DR   MaxQB; Q9Y7J6; -.
DR   PaxDb; 4896-SPBC1778-10c-1; -.
DR   EnsemblFungi; SPBC1778.10c.1; SPBC1778.10c.1:pep; SPBC1778.10c.
DR   PomBase; SPBC1778.10c; ppk21.
DR   VEuPathDB; FungiDB:SPBC1778.10c; -.
DR   eggNOG; KOG0592; Eukaryota.
DR   HOGENOM; CLU_000288_63_9_1; -.
DR   InParanoid; Q9Y7J6; -.
DR   OMA; FACVVYQ; -.
DR   PRO; PR:Q9Y7J6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR   GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IMP:PomBase.
DR   GO; GO:0090520; P:sphingolipid mediated signaling pathway; ISO:PomBase.
DR   CDD; cd05581; STKc_PDK1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR039046; PDPK1.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF411; SERINE_THREONINE-PROTEIN KINASE PPK21; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..551
FT                   /note="Serine/threonine-protein kinase ppk21"
FT                   /id="PRO_0000086157"
FT   DOMAIN          55..315
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          24..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..131
FT                   /note="PIF-pocket"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         65..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         134..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   MOD_RES         220
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   551 AA;  62716 MW;  C591925366133DCF CRC64;
     MMDLEHKRIS RSTLPDYADP DYFEARGERN PVKPQSSNVV PGTSHIGSIK SPADYVFGDI
     IGDGSFSKVR RATDKKSWKE YAIKVLDKKY IVKENKVKYV NIERDSMMRL NGFPGISRLF
     HTFQDDLKLY YVLELAPNGE LLQYIKKYRF LDENCVRFYA AEILSSIEYM HSCGIIHRDL
     KPENILFDGN MHVKITDFGT AKILPPKYVN SPDYTTFPSS FVGTAEYVAP ELLSRQVVSK
     SSDLWAFACV VYQMIVGSPP FHGSNPNNIF KKIMSLEYEL PKLLPPDIVP LFSHLFRIQP
     SDRSTTQQIK QFPFFATITW DNLWTQDPPP MQSFRPNYNI AIPNAPAYYR SNVTAAAAAN
     AAAAFASASI VKHQETARRQ ELPTVNRFTA PTAHYGYASL RSHQMPVDRL YYKLVPSSES
     IIESTSVFVS PIPSVPEGNK FPSGLSKMFL KRKQRVMLLT DVGRCAFVCK GKHERLFIEM
     EVNLKDSSVV VIFDENSSKR FLIEDKVQSW IIEDSSGDVT KYKDKILKFA DVASSHQSRS
     SEENVEENEE E
//