MDE3_SCHPO
ID MDE3_SCHPO Reviewed; 559 AA.
AC O43077; O13638;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sporulation protein kinase mde3;
DE EC=2.7.11.1;
DE AltName: Full=Mei4-dependent protein 3;
GN Name=mde3; ORFNames=pi046, SPBC8D2.19;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
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.
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).
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; AB004537; BAA21426.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17834.1; -; Genomic_DNA.
DR PIR; T40764; T40764.
DR RefSeq; NP_595581.1; NM_001021476.1.
DR AlphaFoldDB; O43077; -.
DR SMR; O43077; -.
DR BioGRID; 277768; 9.
DR STRING; 4896.SPBC8D2.19.1; -.
DR PaxDb; O43077; -.
DR PRIDE; O43077; -.
DR EnsemblFungi; SPBC8D2.19.1; SPBC8D2.19.1:pep; SPBC8D2.19.
DR GeneID; 2541254; -.
DR KEGG; spo:SPBC8D2.19; -.
DR PomBase; SPBC8D2.19; mde3.
DR VEuPathDB; FungiDB:SPBC8D2.19; -.
DR eggNOG; KOG0661; Eukaryota.
DR HOGENOM; CLU_011172_1_0_1; -.
DR InParanoid; O43077; -.
DR OMA; MECMEAN; -.
DR PhylomeDB; O43077; -.
DR PRO; PR:O43077; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISO:PomBase.
DR GO; GO:0030437; P:ascospore formation; IGI:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..559
FT /note="Sporulation protein kinase mde3"
FT /id="PRO_0000086318"
FT DOMAIN 21..323
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 50..74
FT /note="Missing (in Ref. 2; BAA21426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 63224 MW; 0171B1437B7A4C63 CRC64;
MSNESIYSVL DLTQVIFEDR YLVKQKLGDG SFGTVYLAQR KEKNGLYETV AVKKLKNSSK
PKPKHELLKL RESLALRKIS KHPCLIDLLE TFMDPYRNIF LVMEFMDCNL FQLFKRRQGR
LFTKETAFNI LLQIISGIEH IHKHGFMHRD IKPENILVKR ISPKPISSRY SIKLGDFGLA
RPSVSSDPLT EYVSTRWYRA PELLLRSGSY NHSVDLYAFG CIVFEIYSLK PLFPGRNETD
QLNRVCEILG NPGIDELDTL HYWSQAKELA KRLGFMLPPT KPYPIQKLLP QNCPEGHAKM
IPCLLAWNPD VRPTAKYCKE VFFPLPPSAS KSNSVPQKIS NPKVEQNLGF PISREDKKST
RRVGWLKKNL SEFVSSVKSV FPDSHGSQPH VKTEKPINAK ESTGHLANPI ASSNVPAISL
KPGELHESVF FSENEQIDYL LTSIDYLPSY KPPSNGSNIA INAFNETVGD RIPSSKDILI
TEKIPFKKEN EIRDSIVPSC SQPDESNKEG VASCLLLQKS GMEMTSVLEY STPNPAEVQN
ICNDHAKFET SKSLHLSSP
