PIT1_SCHPO
ID PIT1_SCHPO Reviewed; 650 AA.
AC O14132;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sporulation protein kinase pit1;
DE EC=2.7.11.1;
GN Name=pit1; ORFNames=SPAC3C7.06c;
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.
RX PubMed=10747048; DOI=10.1093/genetics/154.4.1497;
RA Abe H., Shimoda C.;
RT "Autoregulated expression of Schizosaccharomyces pombe meiosis-specific
RT transcription factor Mei4 and a genome-wide search for its target genes.";
RL Genetics 154:1497-1508(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-200 AND THR-469, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Protein kinase which is essential for spore formation.
CC {ECO:0000269|PubMed:10747048}.
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 -!- 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; CAB16737.1; -; Genomic_DNA.
DR PIR; T38692; T38692.
DR RefSeq; NP_593607.1; NM_001019038.2.
DR AlphaFoldDB; O14132; -.
DR SMR; O14132; -.
DR BioGRID; 279504; 47.
DR STRING; 4896.SPAC3C7.06c.1; -.
DR iPTMnet; O14132; -.
DR MaxQB; O14132; -.
DR PaxDb; O14132; -.
DR PRIDE; O14132; -.
DR EnsemblFungi; SPAC3C7.06c.1; SPAC3C7.06c.1:pep; SPAC3C7.06c.
DR GeneID; 2543071; -.
DR KEGG; spo:SPAC3C7.06c; -.
DR PomBase; SPAC3C7.06c; pit1.
DR VEuPathDB; FungiDB:SPAC3C7.06c; -.
DR eggNOG; KOG0661; Eukaryota.
DR HOGENOM; CLU_422816_0_0_1; -.
DR InParanoid; O14132; -.
DR OMA; CMAFEIA; -.
DR PhylomeDB; O14132; -.
DR PRO; PR:O14132; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
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; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:PomBase.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Meiosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Sporulation;
KW Transferase.
FT CHAIN 1..650
FT /note="Sporulation protein kinase pit1"
FT /id="PRO_0000086538"
FT DOMAIN 36..336
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 397..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 650 AA; 72826 MW; BB1EDF43F441114C CRC64;
MKKYLWGTPT TNTVFTGKQP KYTKEVRKCI SIDEVYNVVR KVGDGTFGSV YLATTKTPSK
EVVAIKSMKK KLAKVSDATR LREVHSLLRL SENENIVNIF DLYIDQFRCL HIVMEFLDCN
LYQLISTRKN DPLTLEQVQD IMRQIFKGLN HIHTNGFFHR DMKPENILIS SNSDSSSFNV
KIADFGLARE INSRPPYTEY VSTRWYRAPE LLLRDSYYSF PVDIYAAGCM AFEIATLQPI
FPGNDDFDQL YKMCEILGSP DEQSQNTGDK GGGIWDRAEL LANKLGISLP KMAPLDFGDL
FSPPWNLAFA SMLSQLLKWD PAKRPTAEMC LDLEFCRVSA PADAVASKEE VNKNTDFRVS
ISYFPSSSSI PDECNTEEES RINPSTSKFL KQLNKGFNGF TKPFRKSRKQ SKNRKNKSSV
ATQFSEESED IADSITSSTF FPVLPQIRPS TPLNLKLRNF IISSSEDSTS PKAKEFDRPL
PSTEFLVAIN KSQEALLNNS PNSKSGSTQL SASTCLSDLI SPQLSILSHE DKRENQSVNS
ESSKYSPRSS NHSPTLHSKD LHRDMATVNN YAKSPPSFHA TQDLLRKTLA YTNSSGTSTV
LSNDSSAISS TFLDRDFPDF GITSLAGSLT LPDSKIIDRS KTHVSTQLLP
