PPK1_SCHPO
ID PPK1_SCHPO Reviewed; 1023 AA.
AC Q9HFF4; Q7Z993;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein kinase ppk1;
DE EC=2.7.11.1;
GN Name=ppk1; ORFNames=SPAC110.01, SPAC140.05;
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 TYR-492, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CU329670; CAB86416.2; -; Genomic_DNA.
DR RefSeq; NP_593534.2; NM_001018968.2.
DR AlphaFoldDB; Q9HFF4; -.
DR SMR; Q9HFF4; -.
DR BioGRID; 278210; 3.
DR STRING; 4896.SPAC110.01.1; -.
DR iPTMnet; Q9HFF4; -.
DR MaxQB; Q9HFF4; -.
DR PaxDb; Q9HFF4; -.
DR PRIDE; Q9HFF4; -.
DR EnsemblFungi; SPAC110.01.1; SPAC110.01.1:pep; SPAC110.01.
DR GeneID; 2541715; -.
DR KEGG; spo:SPAC110.01; -.
DR PomBase; SPAC110.01; ppk1.
DR VEuPathDB; FungiDB:SPAC110.01; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_295627_0_0_1; -.
DR InParanoid; Q9HFF4; -.
DR OMA; APELVNC; -.
DR PhylomeDB; Q9HFF4; -.
DR PRO; PR:Q9HFF4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14076; STKc_Kin4; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR034674; STK_Kin4/ppk1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1023
FT /note="Serine/threonine-protein kinase ppk1"
FT /id="PRO_0000086139"
FT DOMAIN 492..774
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 55..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 498..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1023 AA; 114012 MW; A11E9B17292915D7 CRC64;
MNAQPFHNNT SDVQSFQDII SNSYQKPLSL VDSTDRALPD SSLSSLSRST FQFHKHHLSG
NENPQPSSES PYFTNNERLN SSSFPQIHDN QLSPSFNTSY QAIPSSSSNR SRGGPYTPSI
RDDSLLALLS FSSNHRLHSM PSQLQPFNNA SSYTTPMAPF TASFSNKVSH SAYPTRRLPS
QAKKTSAIER VPVNLNFLQS DNLVVQSSPQ TNFENFEFPK KIPSKEDLET REVLLLPPQT
SKLSNKNLDT KSFTDVNKIS QQGFVEISSN SSKVTPNTSL HQSFGIASSS SNNYMQTSSE
LTSSTEKMNG SHPLQLSNKS LLSIHLMQSK NQGHVSMTGS DKLSSHVQSE TENAPVSKPS
KPNTLTEDEK PLQSTKLPGN SLTVGELYQE PKSIQLPELS VSRTTYSAQS SSVKNCNERI
PSAKALKKQK HLVPENKSKL QYVWQKKESL PYANLTSASN THFFLSENQN DTSERLTRTL
RKSTKNYTFG SYILGRTIGT GEFGKVKLGW PLPKANSTIH RSTPQVVIKI VLSTKQNCQT
SRLMREVAIL KGLGNNHPHI VKYLDFVKTK HHFGIVLDYV NGGELFDYIL ARRRLEDSVA
CRLFAQLISG VAYLHSRGVV HRDLKLENIL LDTNRNIVIA DFGFATTFGH FNTLSEHSLP
TEKPDLFSTS CGSPCYAAPE LVNCKSGMYA GTQADIWSCG VILYAMLAGY LPFDDDPHNP
NGENVPRLYR YICSTPLIFP EFFKSKARDI LKKILVPDPA KRVRMSAIMN HAYLRSHVSL
FETYNDDEAT SLRPSPIRLL SQKSLASVSS VSSISTYSSS IELTPQITKT SLNREKPALH
GSINLKHSTR PVVPIADGIY ASTTLHPIDN AKNRLVSLLR RPKHKVKHAK VETRESPMKN
KPTKKQHKRA FSMFERPTSQ KAPLSPVESK INLMVAPKRV LNCASDSLRA LLAGKTDKSF
WGSRIPFLFN KLKSKQKAVS SSFNTENSFL ILQAVSPLTF GGCFKEENAY GQKKQHMRHA
TVF
