ID   MAK2_SCHPO              Reviewed;        2310 AA.
AC   O14002;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Peroxide stress-activated histidine kinase mak2;
DE            EC=2.7.13.3;
DE   AltName: Full=His-Asp phosphorelay kinase phk1;
DE   AltName: Full=Mcs4-associated kinase 2;
GN   Name=mak2; Synonyms=phk1; ORFNames=SPAC27E2.09;
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=11179424; DOI=10.1091/mbc.12.2.407;
RA   Buck V., Quinn J., Soto Pino T., Martin H., Saldanha J., Makino K.,
RA   Morgan B.A., Millar J.B.A.;
RT   "Peroxide sensors for the fission yeast stress-activated mitogen-activated
RT   protein kinase pathway.";
RL   Mol. Biol. Cell 12:407-419(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=11758939; DOI=10.1271/bbb.65.2347;
RA   Aoyama K., Aiba H., Mizuno T.;
RT   "Genetic analysis of the His-to-Asp phosphorelay implicated in mitotic cell
RT   cycle control: involvement of histidine-kinase genes of Schizosaccharomyces
RT   pombe.";
RL   Biosci. Biotechnol. Biochem. 65:2347-2352(2001).
CC   -!- FUNCTION: Involved in the control of the SAPK-dependent transcriptional
CC       response to peroxide stress. Regulates sty1 activity.
CC       {ECO:0000269|PubMed:11179424, ECO:0000269|PubMed:11758939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11179424}.
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DR   EMBL; CU329670; CAB11683.1; -; Genomic_DNA.
DR   PIR; T38457; T38457.
DR   RefSeq; NP_594410.1; NM_001019841.2.
DR   AlphaFoldDB; O14002; -.
DR   SMR; O14002; -.
DR   BioGRID; 278522; 4.
DR   STRING; 4896.SPAC27E2.09.1; -.
DR   MaxQB; O14002; -.
DR   PaxDb; O14002; -.
DR   PRIDE; O14002; -.
DR   EnsemblFungi; SPAC27E2.09.1; SPAC27E2.09.1:pep; SPAC27E2.09.
DR   GeneID; 2542041; -.
DR   KEGG; spo:SPAC27E2.09; -.
DR   PomBase; SPAC27E2.09; mak2.
DR   VEuPathDB; FungiDB:SPAC27E2.09; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000400_0_0_1; -.
DR   InParanoid; O14002; -.
DR   OMA; ICKIMDG; -.
DR   PhylomeDB; O14002; -.
DR   PRO; PR:O14002; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0009365; C:protein histidine kinase complex; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140442; F:peroxide sensor activity; EXP:PomBase.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:PomBase.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IDA:PomBase.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IMP:PomBase.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Two-component regulatory system.
FT   CHAIN           1..2310
FT                   /note="Peroxide stress-activated histidine kinase mak2"
FT                   /id="PRO_0000081409"
FT   DOMAIN          12..292
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1450..1592
FT                   /note="GAF"
FT   DOMAIN          1760..1986
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          2180..2303
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1763
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         2232
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2310 AA;  264622 MW;  5A49120DB37E299D CRC64;
     MSLYKSLDVA IDYAISQLGE FQFQPIRTQS NPSSLLSACL VRAVHVETRR KVIFKFSQQT
     FKLENEYFLL RQLSSHPNGR NYAIAPAYIL LLNETLGALI YDDPGPNILD EWLGNPNPLD
     LKLFLKFALG VSYVLCFLHE KKIVHGEIRL DTFHYDLNAP IHAKLLTIGS SVSPIRFTLS
     SLNWKRLYQV QNICHKLQFF SPEQIGNVGR PLDSRSDIYS LGILFYVILT KQYPWGGQSM
     RIVQSIHMRQ FPSVLPRRPD AFPALDQLIQ KMTAKSMNSR ISSATDLCYT IVELMQEFST
     ITSSPLLDQK LLSINKPQQE KLKFPKLLLT NSSDYVRIFH ELVAFSSKRD LLTSAKRVDK
     LPKQHLFKYR PVDNEATYCQ VVTVTGEKGS GKSNLLNAVA DEARKFGYFA MSSFKGHHFS
     PYSAIFKCVS LIMQQTLREE KQLVTDYFTS LWEFLGFQLI YMGELFEYVP ELNSLLSPKY
     NLHCKRENYF KLKKRDPQQF RSASGRLGFM VCLLEILSFT SRVRPVIIIL DELHLADHPS
     LSLIIGMISH RLPILLILAW DEPVMFKDFS KCLHEAPYAM VTDIRMNLFD RKNITEFLDS
     TLESPTQALG PLVLLMQKLS KGNPLVLKSL LLIAFANNGF AFHPKSSSWT YDLPVINRSF
     EALSSYDIPP LLASLLDALL PARCIEFLLW AALLVEPFPF ELLRLITTSM HLFIPKEEIL
     DFPLNVLQFD NDNESCQFSE TFFREGILSK ISLRRAESMH AQIAKELITG TAKEFYDIRT
     VHHILKGLGV IKKFDNTKPY ILALKESADA LMQFGSYEYA TELLKSCLFL LPRNFWNSKL
     YTRKDLISIH ISLAMCYWWS KDHENAIKVL KNPKLSSSNV YDYLPAFRLL TKIEYYKYQS
     LRSIDKAQEL LSNLGLKLKE PTDDVLREFY DRLSTKFLEC DFLVKQSEPL DRKRIDAISV
     ILSECGFVLF NFSQPYYYYF SFLLAEMYLR YGNPSLRYSV MFLASYCFVT RRKPEFLLRI
     SQVDSDLFVI KDRSAVAHAE LIYWGLKREL CSTETGSAVT LESILLQCVM FGDKIYGAYC
     LACLMAQRVF RGDHIHQLLL DQENSETLLL LWDCEPPFTY YLMLIRNSLL ALFGLTNNDD
     PNNILTTKQR TQKDLHDKLT SKKVPCTFCC WYYAGIIFLN TLFHHYEYVM SIAQEVRKLV
     DGKLYERYYL ITRSFIGVAA LQLLFYKKNI SEFEREKVED VAHWAQSSLS EMAKCFHAEL
     YKLWVCLLEG LRQRNLGNYM EALRLFEKVT SMGASVFSPI EFPFVLELIG EFYYGRGHKF
     LAKSYITRAL SCLKNIGCYG VENKLRSRYS DLISDVESRG TTVVSIATTT GDYAEKLKLL
     RNQDINDFSL GLASYSDIFD KPLVTLPVKK SSAVDESEND FYDRNDEESF DIVSLVSVIK
     CGQLLSSKLR LGPLLTTVIK LVIEYSQAKH AAIILKDASN YTLAAHGNVE KAESFEPPVI
     LSQSDVKIPD SLLSEVFDHC RIVSLYTVSA SQDAELLRWL QEEHDMDFFA IIPLQFKESV
     IGALYLCLSR RAIRTGNVTF LKLLSQQIAI SVSNALLFQS LRRTITDNVT LIELQRLSYQ
     RYKAIEEKCI TLLDSLPCIV WTLDSDIGEI EYTNASKRNY FGVPEDCHDS LSWKTFIHPD
     HHHQFQEKLL NLKTLELGDI ELLLRMEDGN YHWHLCRGLS FKEDANAKKW IVVCIDINDE
     KEAREAAMHA VNLKTNFLAN MSHELRTPFS SFYGMLSLLS DTKLNEEQYD IVSTAKQSCT
     SLVQIIDDLL NFSELKSGKM KLEPDKVFDV EENIADCIEL VYPSLSSKPV QISYDIYPNV
     PALLAGDSAK LRQVITNLLG NSVKFTTEGH ILLRCMAIDE EINAEENQCK LRFEIEDTGI
     GLKEEQLKLL FNPFTQVDGS TTRIYGGSGL GLSICLQICK IMDGDIGVQS VYGEGSTFWF
     HVQLRNVTSK LSQKHFEESH ERFANIRQSL KNAKILVVKS FTTSRSIFRS LFSLAVVDTT
     TIYSDIEQQL IDSLDKRQPY DFLCIEAASG QTEQIITQIL SNQKLNKVLL IVLLPSIQRT
     KVRSDGDPFI TSLNKNQSRI FCFREPIRIS KLLQNFPALL SKWSTPTKLV EPSQFRASPR
     KVDQAVVLSS EEKEILQKKY ALIAEDNLIA RKLLTKQLSN LGFQVHAAVD GVELVKMYEA
     KQFGFYSVIF ADYHMPIRDG AEAVMDIRAY ERENNCSTPI PVIALTADIQ KSAKQRCLEV
     GMNFYLTKPF TQKQLVNAVR EFVLLEKSAR