ID   MAK1_SCHPO              Reviewed;        1639 AA.
AC   Q9P7Q7;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Peroxide stress-activated histidine kinase mak1;
DE            EC=2.7.13.3;
DE   AltName: Full=His-Asp phosphorelay kinase phk3;
DE   AltName: Full=Mcs4-associated kinase 1;
GN   Name=mak1; Synonyms=phk3; ORFNames=SPAC1834.08;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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).
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).
CC   -!- FUNCTION: Involved in the control of the SAPK-dependent transcriptional
CC       response to peroxide stress. Also has a role in G2/M regulation.
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}.
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DR   EMBL; CU329670; CAB75776.1; -; Genomic_DNA.
DR   PIR; T50119; T50119.
DR   RefSeq; NP_594687.1; NM_001020116.2.
DR   AlphaFoldDB; Q9P7Q7; -.
DR   SMR; Q9P7Q7; -.
DR   BioGRID; 278595; 31.
DR   STRING; 4896.SPAC1834.08.1; -.
DR   iPTMnet; Q9P7Q7; -.
DR   MaxQB; Q9P7Q7; -.
DR   PaxDb; Q9P7Q7; -.
DR   PRIDE; Q9P7Q7; -.
DR   EnsemblFungi; SPAC1834.08.1; SPAC1834.08.1:pep; SPAC1834.08.
DR   GeneID; 2542119; -.
DR   KEGG; spo:SPAC1834.08; -.
DR   PomBase; SPAC1834.08; mak1.
DR   VEuPathDB; FungiDB:SPAC1834.08; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000263_2_0_1; -.
DR   InParanoid; Q9P7Q7; -.
DR   OMA; WGQKATF; -.
DR   PhylomeDB; Q9P7Q7; -.
DR   PRO; PR:Q9P7Q7; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; TAS:PomBase.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IMP:PomBase.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Two-component regulatory system.
FT   CHAIN           1..1639
FT                   /note="Peroxide stress-activated histidine kinase mak1"
FT                   /id="PRO_0000081408"
FT   DOMAIN          716..786
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          789..841
FT                   /note="PAC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          848..920
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          929..982
FT                   /note="PAC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          1000..1223
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          1507..1629
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   REGION          38..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1003
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         1559
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1639 AA;  184580 MW;  6A653BA0F3B357B5 CRC64;
     MRPPDDQINN NVGSNSHLEK LKEAMDHQLQ KSSKIVGSFT NSQNSSVGSV HSPILESPTS
     LNRQHRNSFS FNNVSSPSLE DERLINFPRV NPNRLMTSKR PNELFKTSSM SSDCYSPQKS
     RESLNSLCHS PAPSVSSCGN ALNNDNTSAS HSLTDEQPFE TDSSANLFKQ LQEKRNRTIG
     NVYEMACLLV FKTGLMNFWK NIIDFFAQQF FSTQISVVEP RDLSDIYNTP WQLRCYYDGG
     SHYDPYSNPI SVNDNLASSS YVTVVASDGS KGIIYKDPAS LKHEGDLLID SKVVQTVLER
     ATLLVYTRKQ QHIVKNTKVH DNDYFSSIPN VDDIRSIKNS WKVFHDEKLN ELKKQVEISA
     SAAQLNGLYP QKKRAFVSHF SQNRKPYSQS DISKAQSSSF SEEPSNIYDE YEQNLLSPWS
     RSPVASPSIQ TDPNRNPFFQ NCLQESSFAT ESSTEKSASE SVSETAVNDD CKGMNFSGNR
     RQEDHLNDFT SFPTETAVSI VHVPLMFPCS DQTSSRGRAP IAILSFKSNL VPYPENLIAS
     IERLIPFIFS SYSNSQSVPL LPCPTQRHLL FNTSSTDNTK ELSMSASSEN SDCPHKEGEC
     VGSFCNINAK GSSLNNIPKL PRFVPVPSEF FKKNQRSWVT LKKHRLLARL KSRISKKNSK
     VNENLRFSLN DGENYSNETI TLKKDEIVLD KSKSYACCTS ESHKYVQGHC GGQAPPFPLL
     KVIIDSIPVH VFTADPGSGK LTWVNRKTLL YCGLNMNEQI ELQFSRIHPD DLPNFLNDWK
     SSLFSGSGFY HEIRLQRFDN VYRYFICRAV PLRDCTGSVL HFFGTMTDVH DQKLAERELQ
     KQSAIAANEN SYRSLAEASP QIVFAANGKN GIIYANAQWL SYSGLSLESS LGLGFLSAVY
     HADRKKCLLP ESLEGTFNNQ DESNGTKTFA AEIRFRSTDG HYRWHLVKSV CVNNSADTST
     NLWLGTCTDI HDHKMLEEKL QESNIEAQRI VRSKMQYLSN MSHEIRTPLI GITGMVSFLL
     ETQMSAEQLS YARIIQQSAK SLLTVINDIL DLSKVRAGMM KLTSQRFSVR AMMEDANETL
     GTLAFSKGIE LNYTVDIDVP DIVFGDNMRM RQVALNVIGN AIKFTNVGEV FTRCSVEKID
     YSTNTVVLKW ECIDTGQGFN RDDQLQMFKP FSQVESSTLP RHGGSGLGLV ISKELVELHN
     GSMSCQSRRG VGTRFMWTAT FTMDKTPLKF EPPDGCCPVC FCPYEKSKQS TEDYYCADDG
     NDKSATNFVK LAVNKADPGR ESNRRKLESD KNVQSNKYVN PFASESEFCR CGASADPYTV
     LFWRLYRNKP SGIKLDKSAL AVVVSHTKYS SEAIGNMLQS IIDISSFKDI VRYGNTYEAF
     EELLENPMQS KVTHIILNLP DIEAYVLFVK SLQLCSLYKD TKFILVTSTR QKESLSKIFS
     DSEDCNSESI HYVLKLVKPS KFFPLFYSDS EEKGKIGALN DMTRKAAMEQ KADAETLRYN
     LAKSGFSVLL AEDNIINIKV ISRYLERIGV KFKVTMDGLQ CVEEWKREKP NFYSLILMDL
     QMPVMDGYQA CNEIRKYELE NDYPKVPIVA LSANALPHVV LSCKDSGFDS YLAKPITLQH
     LSLIISGILN YTNQSKLHK