GAD8_SCHPO
ID GAD8_SCHPO Reviewed; 569 AA.
AC Q9P7J8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase gad8 {ECO:0000303|PubMed:12805221};
DE EC=2.7.11.1 {ECO:0000269|PubMed:12805221};
GN Name=gad8 {ECO:0000303|PubMed:12805221};
GN ORFNames=SPCC24B10.07 {ECO:0000312|PomBase:SPCC24B10.07};
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 FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-387; SER-527 AND
RP SER-546, AND MUTAGENESIS OF THR-387; SER-527 AND SER-546.
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).
CC -!- FUNCTION: Involved in a signaling module for sexual development and
CC cell growth under stressed conditions. Required for G1 arrest under
CC nitrogen starvation and for growth at high temperature and osmolarity.
CC {ECO:0000269|PubMed:12805221}.
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};
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 -!- PTM: Phosphorylated by ksg1 and target of rapamycin complex 2 (TORC2),
CC affecting the kinase activity of gad8 in a nutrient-dependent manner.
CC {ECO:0000269|PubMed:12805221}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; CU329672; CAB76216.1; -; Genomic_DNA.
DR PIR; T50414; T50414.
DR RefSeq; NP_588010.1; NM_001023001.2.
DR AlphaFoldDB; Q9P7J8; -.
DR SMR; Q9P7J8; -.
DR BioGRID; 275776; 49.
DR STRING; 4896.SPCC24B10.07.1; -.
DR iPTMnet; Q9P7J8; -.
DR MaxQB; Q9P7J8; -.
DR PaxDb; Q9P7J8; -.
DR PRIDE; Q9P7J8; -.
DR EnsemblFungi; SPCC24B10.07.1; SPCC24B10.07.1:pep; SPCC24B10.07.
DR GeneID; 2539206; -.
DR KEGG; spo:SPCC24B10.07; -.
DR PomBase; SPCC24B10.07; gad8.
DR VEuPathDB; FungiDB:SPCC24B10.07; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_120_1_1; -.
DR InParanoid; Q9P7J8; -.
DR OMA; HPRFEEA; -.
DR PhylomeDB; Q9P7J8; -.
DR PRO; PR:Q9P7J8; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; ISM: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:1903940; P:negative regulation of TORC2 signaling; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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..569
FT /note="Serine/threonine-protein kinase gad8"
FT /id="PRO_0000085957"
FT DOMAIN 45..202
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 230..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 486..557
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 19..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 236..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 387
FT /note="Phosphothreonine; by ksg1"
FT /evidence="ECO:0000269|PubMed:12805221"
FT MOD_RES 527
FT /note="Phosphoserine; by TORC2"
FT /evidence="ECO:0000269|PubMed:12805221"
FT MOD_RES 546
FT /note="Phosphoserine; by TORC2"
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 387
FT /note="T->A: Sterile and no growth under stressed
FT conditions."
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 387
FT /note="T->D,E: No activity."
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 527
FT /note="S->A: Sterile and no growth under stressed
FT conditions."
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 527
FT /note="S->D: Function compromised."
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 546
FT /note="S->A: Fertile and no growth defects."
FT /evidence="ECO:0000269|PubMed:12805221"
FT MUTAGEN 546
FT /note="S->D: Function compromised."
FT /evidence="ECO:0000269|PubMed:12805221"
SQ SEQUENCE 569 AA; 63770 MW; B2A510D5266D0BE8 CRC64;
MSWKLTKKLK ETHLASAIGL NSGGSSFTRG LKNSTLSSTS SRKSSDEKSR KSSEDKRSPQ
STVVQPGLLQ VTIIEARNLK LPSGHVPANY GVSIDNSLLA PPLSNGSGHA RSRSHAWWLP
YIVVEFDKNE ILVDALNTAS LENPCWDYQA TFDVSRYSKL SLNIYLRSSS SRSRNGMGND
AFLGGIKLSP SFIVNKLTDE WVPLHGGSGE LRVQMLYKPN QSTPLTIDAF ELLKVVGKGS
FGKVMQVRKR DTSRIYALKT MKKAHIVSRS EVDHTLAERT VLAQVNNPFI VPLKFSFQSP
GKLYLVLAFV NGGELFHHLQ REGCFDTYRA KFYIAELLVA LECLHEFNVI YRDLKPENIL
LDYTGHIALC DFGLCKLNMA KTDRTNTFCG TPEYLAPELL LGHGYTKVVD WWTLGVLLYE
MITGLPPFYD ENINEMYRKI LQDPLRFPDN IDEKAKDLLS GLLTRAPEKR LGSGGAQEIK
NHPFFDDIDW KKLCAKKIQP PFKPSVESAI DTSNFDSEFT SEIPMDSVVA DSHLSETVQQ
RFANWSYQRP TTIDTSDDIN TIAPGSVIR
