KSG1_SCHPO
ID KSG1_SCHPO Reviewed; 592 AA.
AC Q12701;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase ksg1 {ECO:0000305|PubMed:10071224};
DE EC=2.7.11.1 {ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:22976295};
DE AltName: Full=PDK1-like kinase ksg1 {ECO:0000303|PubMed:10071224};
GN Name=ksg1 {ECO:0000303|PubMed:10071224};
GN ORFNames=SPCC576.15c {ECO:0000312|PomBase:SPCC576.15c};
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10071224; DOI=10.1007/s004380050955;
RA Niederberger C., Schweingruber M.E.;
RT "A Schizosaccharomyces pombe gene, ksg1, that shows structural homology to
RT the human phosphoinositide-dependent protein kinase PDK1, is essential for
RT growth, mating and sporulation.";
RL Mol. Gen. Genet. 261:177-183(1999).
RN [2]
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12805221; DOI=10.1093/emboj/cdg298;
RA Matsuo T., Kubo Y., Watanabe Y., Yamamoto M.;
RT "Schizosaccharomyces pombe AGC family kinase Gad8p forms a conserved
RT signaling module with TOR and PDK1-like kinases.";
RL EMBO J. 22:3073-3083(2003).
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-64 AND SER-69, 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).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22976295; DOI=10.1242/jcs.111146;
RA Nakashima A., Otsubo Y., Yamashita A., Sato T., Yamamoto M., Tamanoi F.;
RT "Psk1, an AGC kinase family member in fission yeast, is directly
RT phosphorylated and controlled by TORC1 and functions as S6 kinase.";
RL J. Cell Sci. 125:5840-5849(2012).
CC -!- FUNCTION: Involved in the control of sexual development and cell growth
CC under stressed conditions. Phosphorylates AGC kinase gad8 at 'Thr-387',
CC activating gad8 kinase activity and promoting sexual development
CC (PubMed:12805221). Phosphorylates AGC kinase psk1 at 'Ser-248',
CC activating psk1 kinase activity and promoting phosphorylation of
CC ribosomal protein S6 (PubMed:22976295). {ECO:0000269|PubMed:10071224,
CC ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:22976295}.
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 Evidence={ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:22976295};
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; Evidence={ECO:0000269|PubMed:12805221,
CC ECO:0000269|PubMed:22976295};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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; X99280; CAA67672.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21194.1; -; Genomic_DNA.
DR PIR; T43402; T43402.
DR RefSeq; NP_588442.1; NM_001023433.2.
DR AlphaFoldDB; Q12701; -.
DR SMR; Q12701; -.
DR BioGRID; 276079; 14.
DR STRING; 4896.SPCC576.15c.1; -.
DR iPTMnet; Q12701; -.
DR MaxQB; Q12701; -.
DR PaxDb; Q12701; -.
DR PRIDE; Q12701; -.
DR EnsemblFungi; SPCC576.15c.1; SPCC576.15c.1:pep; SPCC576.15c.
DR GeneID; 2539517; -.
DR KEGG; spo:SPCC576.15c; -.
DR PomBase; SPCC576.15c; ksg1.
DR VEuPathDB; FungiDB:SPCC576.15c; -.
DR eggNOG; KOG0592; Eukaryota.
DR HOGENOM; CLU_000288_63_9_1; -.
DR InParanoid; Q12701; -.
DR OMA; HEAVRFF; -.
DR PhylomeDB; Q12701; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-114604; GPVI-mediated activation cascade.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SPO-165158; Activation of AKT2.
DR Reactome; R-SPO-202424; Downstream TCR signaling.
DR Reactome; R-SPO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-SPO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:Q12701; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR CDD; cd05581; STKc_PDK1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033931; PDK1-typ_PH.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF14593; PH_3; 1.
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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..592
FT /note="Serine/threonine-protein kinase ksg1"
FT /id="PRO_0000086226"
FT DOMAIN 99..366
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 461..572
FT /note="PH"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..175
FT /note="PIF-pocket"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT COMPBIAS 33..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 109..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 178..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 592 AA; 65662 MW; B9A857D1989F2C61 CRC64;
MRNTHNPNET EASEDAENDT QSESDLSFDH GSSEKLNRAS LPKTQNSAIP QSNALNTTPN
ESTSQIDSSP KIPSAVPHIS TPNPSSGAST PNIKRVSDFK FGEILGEGSY STVLTATENS
TKREYAIKVL DKRHIIKEKK EKYVNIEKEA LCILSKHPGF IKLFYTFQDA HNLYFVLSLA
RNGELLDYIN KLGRFNEICA QYYAALIVDS IDYMHGRGVI HRDLKPENIL LDDNMRTKIT
DFGSAKILNS SHGSHEEDTH HADKPQAHSR SFVGTARYVS PEVLSDKIAG TASDIWAFGC
ILFQMLAGKP PFVAGNEYLT FQSILHLSYE IPPDISDVAS DLIKKLLVLD PKDRLTVDEI
HQHPFFNGIK FDNTLWELPP PRLKPFGHTS VLSLSVPNAS NKHENGDLTS PLGVPSMVSA
STNAAPSPVG TFNRGTLLPC QSNLEEENKE WSSILQDDEK ISKIGTLNVY SMSGINGNDA
FRFFSSLFRK RKPRTFILTN FGRYLCVASD GEGRKTVKEE IPIKSVGMRC RMVKNNEHGW
VVETPTKSWS FEDPNGPASA WVELLDKASS ISLPFGNHSV TSFSRSIARS AV
