PRP4_SCHPO
ID PRP4_SCHPO Reviewed; 477 AA.
AC Q07538; P87202;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase prp4;
DE EC=2.7.11.1;
GN Name=prp4; ORFNames=SPCC777.14;
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].
RX PubMed=8371982; DOI=10.1093/nar/21.17.4079;
RA Alahari S.K., Schmidt H., Kaeufer N.F.;
RT "The fission yeast prp4+ gene involved in pre-mRNA splicing codes for a
RT predicted serine/threonine kinase and is essential for growth.";
RL Nucleic Acids Res. 21:4079-4083(1993).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Kaeufer N.F.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND TYR-320, 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: Has a role in pre-mRNA splicing and is essential for growth.
CC Phosphorylates srp1.
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. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; L10739; AAB48343.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20718.1; -; Genomic_DNA.
DR PIR; T11720; T11720.
DR RefSeq; NP_588261.1; NM_001023251.2.
DR AlphaFoldDB; Q07538; -.
DR SMR; Q07538; -.
DR BioGRID; 275879; 237.
DR STRING; 4896.SPCC777.14.1; -.
DR iPTMnet; Q07538; -.
DR MaxQB; Q07538; -.
DR PaxDb; Q07538; -.
DR PRIDE; Q07538; -.
DR EnsemblFungi; SPCC777.14.1; SPCC777.14.1:pep; SPCC777.14.
DR GeneID; 2539312; -.
DR KEGG; spo:SPCC777.14; -.
DR PomBase; SPCC777.14; prp4.
DR VEuPathDB; FungiDB:SPCC777.14; -.
DR eggNOG; KOG0670; Eukaryota.
DR HOGENOM; CLU_000288_5_5_1; -.
DR InParanoid; Q07538; -.
DR OMA; VFMVFES; -.
DR PhylomeDB; Q07538; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:Q07538; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14135; STKc_PRP4; 1.
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 InterPro; IPR044092; STKc_PRP4.
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; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..477
FT /note="Serine/threonine-protein kinase prp4"
FT /id="PRO_0000086585"
FT DOMAIN 159..477
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 165..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 320
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 477 AA; 55222 MW; F08979F0A0CEA350 CRC64;
MSDDRFAEDE IIQQRRKRRL EILKKYQQTG NGHSDLSIPE KKLKEDVDQV STTKPIEAVP
KMKTNASKIE INKEGSNSNT KLDVTNSTTS DSPSIKSSVQ IEDTEDDMFA DSPSPSVKRQ
NTGKGISTLT RSFADMQDNW DDIEGYYKVV LMEELDSRYI VQSNLGKGMF STVVSALDRN
RNQTFAIKII RNNEVMYKEG LKEVSILERL QAADREGKQH IIHYERHFMH KNHLCMVFEM
LSLNLRDILK KFGRNVGLSI KAVRLYAYQM FMALDLLKQC NVIHSDIKPD NMLVNEKRNI
LKICDLGSAS DASENEITPY LVSRFYRAPE IILGFPYSCP IDTWSVGCSL YELYTGQILF
PGRTNNQMLR YMMECKGKFS HKMLKRSQFL NDHFDADFNF IQIDHDPITN QETRKPVKFS
KPTKDIRSRL KEVPTSTDEE FIIRQELMDL LEKCLELNPE KRVPPEVALK HPFFIKK
