PPK18_SCHPO
ID PPK18_SCHPO Reviewed; 1318 AA.
AC Q8TFG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein kinase ppk18;
DE EC=2.7.11.1;
GN Name=ppk18; ORFNames=SPAPB18E9.02c;
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).
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}.
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; CAD27468.2; -; Genomic_DNA.
DR RefSeq; NP_001018270.2; NM_001019825.2.
DR AlphaFoldDB; Q8TFG6; -.
DR SMR; Q8TFG6; -.
DR BioGRID; 280611; 6.
DR STRING; 4896.SPAPB18E9.02c.1; -.
DR iPTMnet; Q8TFG6; -.
DR MaxQB; Q8TFG6; -.
DR PaxDb; Q8TFG6; -.
DR PRIDE; Q8TFG6; -.
DR EnsemblFungi; SPAPB18E9.02c.1; SPAPB18E9.02c.1:pep; SPAPB18E9.02c.
DR GeneID; 3361535; -.
DR KEGG; spo:SPAPB18E9.02c; -.
DR PomBase; SPAPB18E9.02c; ppk18.
DR VEuPathDB; FungiDB:SPAPB18E9.02c; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000709_4_1_1; -.
DR InParanoid; Q8TFG6; -.
DR OMA; QFDIIMT; -.
DR PRO; PR:Q8TFG6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; 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; IDA:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1905287; P:positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation; IMP:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1902471; P:regulation of mitotic actomyosin contractile ring localization; IGI:PomBase.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1318
FT /note="Serine/threonine-protein kinase ppk18"
FT /id="PRO_0000256819"
FT DOMAIN 566..934
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 935..1044
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1200..1316
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 431..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 690
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 572..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1318 AA; 146995 MW; 62634DAF0EB289CF CRC64;
MVMQERNSNE DNKVNHGIDN IYVLELDLDG SVLFASTNFS QITGISSLEL TGKPAALLSS
DQEIFNAAIE QLLDDDSHSV KIHTVISKLP SLEENVFVQD EEMELQSKSV ELDCVGVLIR
DPLTSRPSHT LWVLQPLKPT RITRQEIGQQ LTETLGFGAQ LLAQHLEKLQ TVPSTDSLPP
FETVLCRVCD HEIQNWYFEH HTELCLLIHH AEARAQEAND LLNEQRNALQ SLLDSLDDQI
EPDVSYLGVP LAAVLPSSIT SSAKSNSRSS LSQKIRNYIS NMLFDAISYT DSCLAIHLPF
IPESTTREDN QPFSEIRLLS PASEVFNAKT LSWCLPHIDD PGLQLMFENT DALVKKKLDA
INRLSNIIYY SERVRCEIED QVQTIIEQSI QVDGYDEPLS TTTPTLIEPI QETLMTQSPI
IECEPFNTVK PSVSPEEVHD ISQFNHRNDP PITAASVDSS NSFSVHRSST NHSSTNSGSP
NLSRRNNLAI PIASRRKSVS AVNTLYGVGS SYTSESFPFS KLTVPVERNS FRETESPKPF
LSRQIGISTL SSNISSGKGT PSIQDYEIIK PISKGTFGTV YLSRKNTTGE IYAIKVLRKV
DMISKNQVAN VKAERAVLMA QEESAFVAKL YYAFQSRDYL YLVMEFMNGG DCASLLKSLY
TIPESWAKIY IAEVALGLEH LHRLGIIHRD IKPDNILMSI TGHLKLADFG LSQLGLTTRQ
LRLQKGKNNI LSPPSFQSPT ALGDPGDNIA SSPLILPTSV SAFSYDEKSQ KQKTELATFT
TYKEDDTTTT TRTSIDSISS KYLESPVDSQ KVNRTPNLQS VPFFRQPDAP KRFVGTPDYL
APETLRGSTQ DDMVDWWALG CVLFEFLFGY PPFHAETPEK VFENILANNI AWPDLEMYPC
SEEALDLING FLQPNPERRL GFSDINEIKE HPFFNGINWD DIFSHEAPFI PAPETPLDTA
YFDSRGAGAA ESNMSSSVNS GEEVSKDNNV SQERGSQFLR SSHGRSRERS TSARRSRRFS
EANSEFDEFG PFSYKNLSVL ERANRNAIEK IRSEIAGKLH ISPPDPHIGY TPGSDMPSAK
LYDQQLTLSP SLMTNQGSNF SSTDSTPRKS INSSDVESRS KTDGPKSMHD LIKQLHMRKH
SSHTNQSTGS SESDDLFNLD LPISNLETSY PFKIEEGQAS PLSSPLSKTP PFFSSSVPLK
ALICVSKLNL FSELIKLLKS YKFQVSIVTD EDKMLRTLMA DEKFSIIFLQ LDLTRVSGVS
ILKIVRSSNC ANRNTPAIAL TPTRIDINAA IPRMFDGRLY LPINAFLLRG YIARLCNK
