BYR2_SCHPO
ID BYR2_SCHPO Reviewed; 659 AA.
AC P28829; Q7LGJ0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein kinase byr2;
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:O94547};
DE AltName: Full=MAPK kinase kinase;
DE Short=MAPKKK;
DE AltName: Full=Protein kinase ste8;
GN Name=byr2 {ECO:0000303|PubMed:2046669, ECO:0000312|PomBase:SPBC1D7.05};
GN Synonyms=ste8 {ECO:0000303|PubMed:1435723};
GN ORFNames=SPBC1D7.05 {ECO:0000312|PomBase:SPBC1D7.05}, SPBC2F12.01;
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], AND FUNCTION.
RX PubMed=2046669; DOI=10.1128/mcb.11.7.3554-3563.1991;
RA Wang Y., Xu H.P., Riggs M., Rodgers L., Wigler M.;
RT "byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable
RT of partial suppression of the ras1 mutant phenotype.";
RL Mol. Cell. Biol. 11:3554-3563(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1435723; DOI=10.1007/bf00286189;
RA Styrkarsdottir U., Egel R., Nielsen O.;
RT "Functional conservation between Schizosaccharomyces pombe ste8 and
RT Saccharomyces cerevisiae STE11 protein kinases in yeast signal
RT transduction.";
RL Mol. Gen. Genet. 235:122-130(1992).
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 INTERACTION WITH RAD24 AND RAD25, AND SUBCELLULAR LOCATION.
RX PubMed=12242289; DOI=10.1128/mcb.22.20.7105-7119.2002;
RA Ozoe F., Kurokawa R., Kobayashi Y., Jeong H.T., Tanaka K., Sen K.,
RA Nakagawa T., Matsuda H., Kawamukai M.;
RT "The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting
RT its localization in Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 22:7105-7119(2002).
RN [5]
RP STRUCTURE BY NMR OF 71-165.
RX PubMed=11369865; DOI=10.1110/ps.43201;
RA Gronwald W., Brunner E., Huber F., Wenzler M., Herrmann C., Kalbitzer H.R.;
RT "Overcoming the problems associated with poor spectra quality of the
RT protein kinase Byr2 using residual dipolar couplings.";
RL Protein Sci. 10:1260-1263(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 81-180.
RX PubMed=11709168; DOI=10.1016/s0969-2126(01)00674-8;
RA Scheffzek K., Grunewald P., Wohlgemuth S., Kabsch W., Tu H., Wigler M.,
RA Wittinghofer A., Herrmann C.;
RT "The Ras-Byr2RBD complex: structural basis for Ras effector recognition in
RT yeast.";
RL Structure 9:1043-1050(2001).
CC -!- FUNCTION: Serine/threonine protein kinase involved in conjugation and
CC sporulation (PubMed:2046669, PubMed:1435723). It is thought that it
CC phosphorylates the byr1 protein kinase which itself phosphorylate the
CC spk1 kinase (PubMed:2046669, PubMed:1435723).
CC {ECO:0000269|PubMed:1435723, ECO:0000269|PubMed:2046669}.
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=2.7.11.25;
CC Evidence={ECO:0000250|UniProtKB:O94547};
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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O94547};
CC -!- SUBUNIT: Interacts with rad24 and rad25; these prevent its
CC translocation to the cell membrane during nitrogen starvation.
CC {ECO:0000269|PubMed:12242289}.
CC -!- INTERACTION:
CC P28829; P08647: ras1; NbExp=2; IntAct=EBI-1032333, EBI-15585264;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242289}. Cell
CC membrane {ECO:0000269|PubMed:12242289}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; M74293; AAA35289.1; -; Genomic_DNA.
DR EMBL; X68851; CAA48731.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB10150.1; -; Genomic_DNA.
DR PIR; A39723; A39723.
DR RefSeq; NP_595714.2; NM_001021611.3.
DR PDB; 1I35; NMR; -; A=71-165.
DR PDB; 1K8R; X-ray; 3.00 A; B=71-180.
DR PDBsum; 1I35; -.
DR PDBsum; 1K8R; -.
DR AlphaFoldDB; P28829; -.
DR BMRB; P28829; -.
DR SMR; P28829; -.
DR BioGRID; 277138; 51.
DR DIP; DIP-136N; -.
DR IntAct; P28829; 4.
DR MINT; P28829; -.
DR STRING; 4896.SPBC1D7.05.1; -.
DR PaxDb; P28829; -.
DR PRIDE; P28829; -.
DR EnsemblFungi; SPBC1D7.05.1; SPBC1D7.05.1:pep; SPBC1D7.05.
DR GeneID; 2540612; -.
DR KEGG; spo:SPBC1D7.05; -.
DR PomBase; SPBC1D7.05; byr2.
DR VEuPathDB; FungiDB:SPBC1D7.05; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_003051_2_0_1; -.
DR InParanoid; P28829; -.
DR OMA; RFIACNG; -.
DR PhylomeDB; P28829; -.
DR BRENDA; 2.7.11.25; 5613.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR EvolutionaryTrace; P28829; -.
DR PRO; PR:P28829; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF54236; SSF54236; 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.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Pheromone response; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..659
FT /note="Protein kinase byr2"
FT /id="PRO_0000085689"
FT DOMAIN 4..67
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 394..658
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 180..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 522
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 400..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1K8R"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1I35"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1K8R"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1K8R"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1K8R"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1K8R"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:1I35"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1I35"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1K8R"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:1K8R"
SQ SEQUENCE 659 AA; 73633 MW; 18CD78F1D1FABBCD CRC64;
MEYYTSKEVA EWLKSIGLEK YIEQFSQNNI EGRHLNHLTL PLLKDLGIEN TAKGKQFLKQ
RDYLREFPRP CILRFIACNG QTRAVQSRGD YQKTLAIALK KFSLEDASKF IVCVSQSSRI
KLITEEEFKQ ICFNSSSPER DRLIIVPKEK PCPSFEDLRR SWEIELAQPA ALSSQSSLSP
KLSSVLPTST QKRSVRSNNA KPFESYQRPP SELINSRISD FFPDHQPKLL EKTISNSLRR
NLSIRTSQGH NLGNFGQEIL PRSSRRARPS ELVCPLSSLR ISVAEDVNRL PRIDRGFDPP
LTVSSTQRIS RPPSLQKSIT MVGVEPLYQS NGNEKSSKYN VFSESAHGNH QVLSFSPGSS
PSFIEQPSPI SPTSTTSEDT NTLEEDTDDQ SIKWIRGALI GSGSFGQVYL GMNASSGELM
AVKQVILDSV SESKDRHAKL LDALAGEIAL LQELSHEHIV QYLGSNLNSD HLNIFLEYVP
GGSVAGLLTM YGSFEETLVK NFIKQTLKGL EYLHSRGIVH RDIKGANILV DNKGKIKISD
FGISKKLELN STSTKTGGAR PSFQGSSFWM APEVVKQTMH TEKTDIWSLG CLVIEMLTSK
HPYPNCDQMQ AIFRIGENIL PEFPSNISSS AIDFLEKTFA IDCNLRPTAS ELLSHPFVS
