SID1_SCHPO
ID SID1_SCHPO Reviewed; 471 AA.
AC O14305;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Serine/threonine-protein kinase sid1;
DE EC=2.7.11.1;
DE AltName: Full=STE20-like kinase sid1;
GN Name=sid1; ORFNames=SPAC9G1.09;
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], FUNCTION, INTERACTION WITH CDC14, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11384993; DOI=10.1074/jbc.m103802200;
RA Guertin D.A., McCollum D.;
RT "Interaction between the noncatalytic region of Sid1p kinase and Cdc14p is
RT required for full catalytic activity and localization of Sid1p.";
RL J. Biol. Chem. 276:28185-28189(2001).
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, INTERACTION WITH CDC14, AND SUBCELLULAR LOCATION.
RX PubMed=10775265; DOI=10.1093/emboj/19.8.1803;
RA Guertin D.A., Chang L., Irshad F., Gould K.L., McCollum D.;
RT "The role of the sid1p kinase and cdc14p in regulating the onset of
RT cytokinesis in fission yeast.";
RL EMBO J. 19:1803-1815(2000).
CC -!- FUNCTION: Has a role in the septation initiation network (SIN) required
CC for cytokinesis. {ECO:0000269|PubMed:10775265,
CC ECO:0000269|PubMed:11384993}.
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 cdc14. {ECO:0000269|PubMed:10775265,
CC ECO:0000269|PubMed:11384993}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:10775265,
CC ECO:0000269|PubMed:11384993}. Note=Localizes to the SPB prior to
CC cytokinesis and leaves once septation is complete.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11493.1; -; Genomic_DNA.
DR PIR; T39232; T39232.
DR RefSeq; NP_593564.1; NM_001018997.2.
DR AlphaFoldDB; O14305; -.
DR SMR; O14305; -.
DR BioGRID; 279196; 17.
DR STRING; 4896.SPAC9G1.09.1; -.
DR iPTMnet; O14305; -.
DR MaxQB; O14305; -.
DR PaxDb; O14305; -.
DR EnsemblFungi; SPAC9G1.09.1; SPAC9G1.09.1:pep; SPAC9G1.09.
DR GeneID; 2542746; -.
DR KEGG; spo:SPAC9G1.09; -.
DR PomBase; SPAC9G1.09; sid1.
DR VEuPathDB; FungiDB:SPAC9G1.09; -.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O14305; -.
DR OMA; LWILMEH; -.
DR PhylomeDB; O14305; -.
DR Reactome; R-SPO-75153; Apoptotic execution phase.
DR PRO; PR:O14305; -.
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:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0071958; C:new mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0031028; P:septation initiation signaling; IMP:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..471
FT /note="Serine/threonine-protein kinase sid1"
FT /id="PRO_0000086653"
FT DOMAIN 9..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 471 AA; 52969 MW; 7332F7B103AA5BE6 CRC64;
MYPLNANSYT LLRKLGSGSF GVVWKARENV SGDIIAIKQI DLETGIDDIT DIEQEVFMLS
NCNSSNVIQY YGCFVDGYTL WILMEHMDGG SVSGLLKMGR LNEQVISIIL REVLYGLNYL
HGQNKIHRDI KAANILLSSS TGNVKLADFG VAAQLSNAAS RRHTFVGTPF WMAPEVIQQT
SYGLAADIWS LGITAIEMAN GIPPRATMHP MRVIFEIPQS EPPKLDDHFS PTFRDFVSCC
LDLNPNMRWS AKELLQHPFI KSAGTVKDII PLLVQKENKL FDDSDQSVLE ETINNTLKPF
EEPIAEGNAD IEDWTFETVK KSDSTVLGNT SIPKNSIISS QNKEELPSSI KYLEKTIMSD
QATPHPFSKS LSEKGSSYHK SLTSDFAMKH YIKSTIRSML LNDKLSATQR SSLESFYTSF
ISLDKNLSSK FVNQITPDNR LHHKKQKRSP ISQLLFSRWL EETEKRRSLN G
