FIN1_SCHPO
ID FIN1_SCHPO Reviewed; 722 AA.
AC O13839;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=G2-specific protein kinase fin1;
DE EC=2.7.11.1;
GN Name=fin1; ORFNames=SPAC19E9.02;
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, AND SUBCELLULAR LOCATION.
RX PubMed=11927555; DOI=10.1093/emboj/21.7.1713;
RA Krien M.J.E., West R.R., John U.P., Koniaras K., McIntosh J.R.,
RA O'Connell M.J.;
RT "The fission yeast NIMA kinase Fin1p is required for spindle function and
RT nuclear envelope integrity.";
RL EMBO J. 21:1713-1722(2002).
CC -!- FUNCTION: Promotes chromosome condensation and nuclear envelope
CC dynamics during mitosis. Activity appears at metaphase-anaphase
CC transition. {ECO:0000269|PubMed:11927555}.
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, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:11927555}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. NIMA subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CU329670; CAB11653.1; -; Genomic_DNA.
DR PIR; T37970; T37970.
DR RefSeq; NP_593305.1; NM_001018735.2.
DR AlphaFoldDB; O13839; -.
DR SMR; O13839; -.
DR BioGRID; 278709; 134.
DR STRING; 4896.SPAC19E9.02.1; -.
DR iPTMnet; O13839; -.
DR MaxQB; O13839; -.
DR PaxDb; O13839; -.
DR PRIDE; O13839; -.
DR EnsemblFungi; SPAC19E9.02.1; SPAC19E9.02.1:pep; SPAC19E9.02.
DR GeneID; 2542237; -.
DR KEGG; spo:SPAC19E9.02; -.
DR PomBase; SPAC19E9.02; fin1.
DR VEuPathDB; FungiDB:SPAC19E9.02; -.
DR eggNOG; KOG0591; Eukaryota.
DR HOGENOM; CLU_404982_0_0_1; -.
DR InParanoid; O13839; -.
DR OMA; ILECIGH; -.
DR PhylomeDB; O13839; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:O13839; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA: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:0004712; F:protein serine/threonine/tyrosine kinase activity; EXP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; EXP:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
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 3: Inferred from homology;
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..722
FT /note="G2-specific protein kinase fin1"
FT /id="PRO_0000085952"
FT DOMAIN 4..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 528..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 722 AA; 82689 MW; 20C7E304DAD7C440 CRC64;
MEKYKILECI GHGSFGRIYK VQRLKDGALL AQKEIHFGNI TRQEKQYIAD EVNILRNLKH
PNIVQYCGEE LNRSAQVINL YMEYCGHGDL ANLIQRYKEE KKRFTEQEVL KFFTQLLLAL
YRCHYGENAP ACDSQWPREI FHPKQSVLHR DIKPANIFLD ENNSVKLGDF GLSKLLDNTR
VFTQSYVGTP YYMSPEIIRS SPYSAKSDVW ALGCVIFEIC MLTHPFEGRS YLELQRNICQ
GNLSCWDHHY SDDVFLLIRH CLEVNSDLRP TTYQLLRSPI LSDIRSKLES ERVVLEQSDL
LHKKHQMLIQ LENDLQFREQ RLSARESELE NVIASRLAQR EEILRRELEK QLRDMDARYQ
RHMQTVVNSM QKMRVTSPVD HNEQPESSTA EMFVDCTIEA SQSPLLHIPK LGISKPLQTL
SCPGFTLTTQ QPILKRPTLR KELSSRALHT TATLMKYRAN ASSLRTTPID KDGQITSLQQ
KNGTSNQVAD CMNKLLHTSL DGKKLSPSEL CNKFSDGEGL PNRKVSKLSV ESDETAVSAS
SGESVPTDST LTDTKSKSVF VHPPSPQSLY VEKLEKLNIR SDEVSKPSKA SKTLHGYALP
SLASPYDVHA EEKIARENEM DGNFKTMKIN QHPDEYVLRT PKKIQLLEGQ KRSPVKQLGR
LGYNKLRRSA MDNAGLELRK AASTSNYTSL QSRTLPGSWR DDEEEIPRPF LRKMLDARMM
RA
