SPO4_SCHPO
ID SPO4_SCHPO Reviewed; 429 AA.
AC Q9UQY9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cell cycle protein kinase spo4;
DE EC=2.7.11.1;
DE AltName: Full=Sporulation-specific protein 4;
GN Name=spo4; ORFNames=SPBC21C3.18;
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 [MRNA], FUNCTION, INTERACTION WITH SPO6, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF THR-264.
RX PubMed=11739743; DOI=10.1128/mcb.22.1.309-320.2002;
RA Nakamura T., Nakamura-Kubo M., Nakamura M., Shimoda C.;
RT "Novel fission yeast Cdc7-Dbf4-like kinase complex required for the
RT initiation and progression of meiotic second division.";
RL Mol. Cell. Biol. 22:309-320(2002).
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).
CC -!- FUNCTION: Required for the initiation of meiosis II and progression
CC through anaphase II. {ECO:0000269|PubMed:11739743}.
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 -!- SUBUNIT: Interacts with spo6. {ECO:0000269|PubMed:11739743}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739743}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB036343; BAA88630.1; -; mRNA.
DR EMBL; AB036342; BAA88629.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB76054.1; -; Genomic_DNA.
DR PIR; T50362; T50362.
DR RefSeq; NP_596598.1; NM_001022518.2.
DR AlphaFoldDB; Q9UQY9; -.
DR SMR; Q9UQY9; -.
DR BioGRID; 277268; 10.
DR STRING; 4896.SPBC21C3.18.1; -.
DR PaxDb; Q9UQY9; -.
DR EnsemblFungi; SPBC21C3.18.1; SPBC21C3.18.1:pep; SPBC21C3.18.
DR GeneID; 2540745; -.
DR KEGG; spo:SPBC21C3.18; -.
DR PomBase; SPBC21C3.18; spo4.
DR VEuPathDB; FungiDB:SPBC21C3.18; -.
DR eggNOG; KOG1167; Eukaryota.
DR HOGENOM; CLU_000288_118_2_1; -.
DR InParanoid; Q9UQY9; -.
DR OMA; VELAHIF; -.
DR PhylomeDB; Q9UQY9; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:Q9UQY9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; ISM:PomBase.
DR GO; GO:0031322; P:ascospore-type prospore-specific spindle pole body remodeling; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007135; P:meiosis II; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:PomBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Meiosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Sporulation; Transferase.
FT CHAIN 1..429
FT /note="Cell cycle protein kinase spo4"
FT /id="PRO_0000086673"
FT DOMAIN 40..402
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
FT MUTAGEN 264
FT /note="T->A,E: No activity."
FT /evidence="ECO:0000269|PubMed:11739743"
SQ SEQUENCE 429 AA; 49155 MW; B0E5E4EDEA2247EB CRC64;
MLSMLLPFGN SGVYASDVDR EDRPEIAKLV QAFPTIEEDY HVVKLVGAGS FSSVFKAVDR
HFDSYDNSYW ISSQIEDQMP HDKTKRPKNH FVALKRIYAT VLPSRIQTEL EMLHELRGSD
CVLNMITAVR HQDQVLIVLP FIQHAEFRDF YMKYSLPEIG AYLRDLLKGL AHIDAKGIIH
RDIKPGNFAW NPYTQRGVIL DFGLAQWQEA DAPTENCCVD KLRKLKQEGK YYDYFPFEKT
IADPPEGYLL HDPRPTKRAD RAGTRGFRAP EVLFRCQNQT SSIDVWSVGV ILLCFLTHRY
PFFRCEDDID AIVELAHIFG RNGMSNCALL HGQIWSDNIP TLLDQKHNWL DLIASITKND
ENLILETSSD YQVALAIDLL DKLLELHPSK RVKAKTALQH EFFNACGVTR SGFEAENPFR
SDFPSTVEQ
