PPK31_SCHPO
ID PPK31_SCHPO Reviewed; 1032 AA.
AC O94324;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine-protein kinase ppk31;
DE EC=2.7.11.1;
DE AltName: Full=Meiotically up-regulated gene 25 protein;
GN Name=ppk31; Synonyms=mug25; ORFNames=SPBC725.06c;
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 IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
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 -!- FUNCTION: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA22178.1; -; Genomic_DNA.
DR PIR; T40658; T40658.
DR RefSeq; NP_595486.1; NM_001021397.2.
DR AlphaFoldDB; O94324; -.
DR SMR; O94324; -.
DR BioGRID; 277610; 24.
DR STRING; 4896.SPBC725.06c.1; -.
DR PaxDb; O94324; -.
DR PRIDE; O94324; -.
DR EnsemblFungi; SPBC725.06c.1; SPBC725.06c.1:pep; SPBC725.06c.
DR GeneID; 2541095; -.
DR KEGG; spo:SPBC725.06c; -.
DR PomBase; SPBC725.06c; ppk31.
DR VEuPathDB; FungiDB:SPBC725.06c; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_306328_0_0_1; -.
DR InParanoid; O94324; -.
DR OMA; EKANMEI; -.
DR PhylomeDB; O94324; -.
DR PRO; PR:O94324; -.
DR Proteomes; UP000002485; Chromosome II.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:PomBase.
DR CDD; cd00130; PAS; 1.
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 Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Meiosis; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1032
FT /note="Serine/threonine-protein kinase ppk31"
FT /id="PRO_0000256828"
FT DOMAIN 3..72
FT /note="PAS"
FT DOMAIN 528..877
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 938..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 652
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 534..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1032 AA; 120269 MW; 3E3E3620E22A75BE CRC64;
MTNPEQLKRI LSHEVLLKIE MSKNGIVEYA NPAFFELIGY EGDLFQCSFY EYLQSDDEHL
MKKATDNLFR KSISVAHVFA FLRCNPIRSP NYYIQQAKAP FEGKTYIRML FRGILVDSLY
GKDTRVLWAG KYLYPQRSVI NEMDFILFNT LGIGAFILHD HLLGIIKYNY IHVPPPSGKL
CSLCEDNLPE WYFEVHSDFC LVWNDLVRRV FAVQQLINCK KLEIEDIVNK LPTGSNHMVE
ETFLSLPVIT VFNGKKNRKQ RFRIRSWRSS LNFLVKELDK SIKNFAYLEH RTFLTISNSA
AKDMKREIYE KSLVNWEYDF LVPSKIQDYF YDVHSLLLKN LSSKIKLCNH ILMYQATFNE
VKNFLQTYSL NMLSIEMENI EGSLYFGNAQ LSNLICVNQY LSEQRPVFFN RLLALGNVEN
NNSIYDDIQK RTERISTIKR HKKYFEIGER LTEKDLIVSK TFKTTRIDYF KAVKGSIEDL
DVRPLKNRQK FVNKFYASIV HFLTESMQFP SHNDRRFGDN TPHSLDEFIL LKEINRGAYG
RVYLAKKRSS GKYFALKMIP KSSLDSLKKI KGLLLEKRNM HIQRYGPNTV KLYYAFDSGD
YLCLVMDYFN GGDCETLIQK LGPLPEQWVC QYAAELLNAI ELLHQDGIIH HDIKPANMLV
DETGHIRLTD FGLSENVEEK KEVYKLTKRM SFEQKHGNLY EQLQPKKFEF VRYVRNYRGN
IDELEKAESP QQNSDYANDS VQHLLDFDIN NMDETAIHML MNQLEKKENR TFIKKDISGT
PNYMAPEILM GVDTQMGDIW AMGCVIFEML TGTRPFEANT VKAIWARIER NDIGWTKRVK
ESCSKEAVDL ITKLMDPDCN KRLGSNGYQE IKKHPFFRTI KWDNLNSGPG PFVPQTENVE
DLTYFEKNIS GSDNINKNNC QTSATLILNG IFAFHPPPKA TPADSGTETS NSAAFSASEE
ETTNLTDQKR KDLFSLITKA FKGIDLKALN YNNKATLLRM YDEVDFPKNQ QRNKEKFRIQ
KRPNKKYRYH LF
