MAK3_SCHPO
ID MAK3_SCHPO Reviewed; 2344 AA.
AC O74539;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Peroxide stress-activated histidine kinase mak3;
DE EC=2.7.13.3;
DE AltName: Full=His-Asp phosphorelay kinase phk2;
DE AltName: Full=Mcs4-associated kinase 3;
GN Name=mak3; Synonyms=phk2; ORFNames=SPCC74.06;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-16 AND SER-17, 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: 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; CU329672; CAA20836.1; -; Genomic_DNA.
DR PIR; T41590; T41590.
DR RefSeq; NP_588379.1; NM_001023370.2.
DR AlphaFoldDB; O74539; -.
DR SMR; O74539; -.
DR BioGRID; 275689; 48.
DR IntAct; O74539; 1.
DR STRING; 4896.SPCC74.06.1; -.
DR iPTMnet; O74539; -.
DR MaxQB; O74539; -.
DR PaxDb; O74539; -.
DR PRIDE; O74539; -.
DR EnsemblFungi; SPCC74.06.1; SPCC74.06.1:pep; SPCC74.06.
DR GeneID; 2539117; -.
DR KEGG; spo:SPCC74.06; -.
DR PomBase; SPCC74.06; mak3.
DR VEuPathDB; FungiDB:SPCC74.06; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000400_0_0_1; -.
DR InParanoid; O74539; -.
DR OMA; EGYMAIT; -.
DR PhylomeDB; O74539; -.
DR PRO; PR:O74539; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0000155; F:phosphorelay sensor kinase activity; IGI:PomBase.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IGI: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; 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; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47384; SSF47384; 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; PS50113; PAC; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..2344
FT /note="Peroxide stress-activated histidine kinase mak3"
FT /id="PRO_0000081410"
FT DOMAIN 1..295
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 829..862
FT /note="TPR 1"
FT REPEAT 1340..1373
FT /note="TPR 2"
FT DOMAIN 1730..1781
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 1792..2018
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 2211..2333
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 486..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1795
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 2263
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2344 AA; 266850 MW; 8032B9DBD3E1BF5C CRC64;
MYSQHELRNK VSLALSSLLR YTFELTPFFE LYEADFAYAL YAGFELATNR KVVGKFSFQN
VHLENEYNIL TEIAKDERAS KFSPTPIEFT SFPHIDLSAC IAYDFGHGAE LSTSYAYFRE
NPAEFVRFCI AICKCIEYLH SKGMVHGEIR LDSFIPISSY DNVYMLTVGS GASYFHNCLQ
AHNWRKYSED SESMSRILFI SPEQTGRTSY SVGYRTDIYS LGVLFFHYLS DCSPYTGSFV
QRIRSILTEP LPDISKSCPK LPHLIFKIIE KMTRKNPDER YTSCSGIVND LEACLDDIDK
GLILNDHVLE KTGRTSLFYL PCSIYGREHE IKLIRKILRN SPRAINHQDK KDLETFNPYY
LNAIESESSS QSLSLSQRAS EVMPLVILIT GCEGIGESSL IQTICDRREG YMAITKFEVS
QSIVYSAIVS AVAEFIRQIL AEDQLLLNNF FEELKNKLES DLYLLDSVFD LVPEIRSLLQ
QFSTSSGNTR KTSLLGSNHS SYSDKLGSPT ILSTSFSLAR PYPEPALVSP STERPPRSSF
SAALMTLLNI IASFKKVTMV IENIHLADES SLIILQKIVY SDLPLTLMIT CDKENDHVIN
RFRLANDRIH EIELKPLSFN AVNSYVQATL HRTDDGLARF SSYVYHISKG VPLLVRNVLL
SIYENKIIYF DWKKNRWEVN YDEMYTLDND YSEPDAFMTA KKKISKLNDS SRAILGWASL
LGPSFSFATV KKLCKDTDNI ELNVEALQSA LREGIIYATS SDDTYTFSRS IYVKAMRDLL
NEAKIQIMHA CLIDVCLKNR DRYNIFDIAF HINAAFDFVK GDKRSVEYCH YLHLAAEEAL
KIGANQEALD LYNRCIKMIP HEIPEESDDS YIRCQLIGMY VGCAEAYWVN DNFDTASEML
KLAEEKACNN SEVFPARFLY SRILFEGVHI EECTQYVLSC LKPLGYELKR HSLEDSKSII
SALIPRIIDK ITKSSEESQS STDDDDRRIF EILSFLYVGS VATSYFSETA EMAIDFGIAQ
VEFFLSTVVN SFSAFALVYF AILANSLLEP SEDILFIGNY GEKLNREAEN PIIFSRTEYL
YVQSLGFIDS TTKERRLTID YLDRNCVTCS DKHVIISLLL VSSWEKFLTS NNYSNYLADF
ETTHAQIMEM KPWVGDTSLI TQLKRFLMCL QDNIKLDLIK SKSFLSDHNI QLSSPAAQES
AKLAFSLHGW INSWYLLALV MHGEWDMAIS YGENFKREFK NALLTSSRVF GIFMFTWSLV
NKMLICPEFT KQKKYYEQYK ENLGFFDSLC IGDNECITRV YFLLLKACGL IMNGLNFEAS
VMLEEVISLT EKLELFLLQA FAFETVGSIF VSMELYTSAT QYLEEAIRNY AALGVKQKAR
HLRDKFGDLL VSNNLQVSID EATQTDFPLV FSPERSSIDI NASSMRSEKA SFEIPFPEEQ
IDDDVSPVAQ DSSLEELLIS LDIIDLTSVM RSCQTIASEI ELTGLLSTMT QRMLEDSSAN
AAVIAIRDDV GFKIAAYRTG ELNEVFAPPM PITEDQTYVP SRVINYVVHT QKALFSNNIN
HEFDLQQERW NIENHMGRSV IAIPLYQKKE VFAILYLQGP PSAFHSRHMS VLSILGAQAS
FAIVNISLFH KVKEATNVNT IIIKAQREAL NLVQKSEAKY RSFVDTMPCL LSKLEFDEEL
RIELFGSFWK EYCGELNIND PNTWKEYVHL DDHLKLQDFL LSHLHNPLPF ELEIRIKRKD
GVYRWNLTRC TPTTNEKNRT SFLCATIDID DQKKARATAL ELARLRSNFL ANISHELRTP
FSGFYGMLSL LDDTNLDSEQ RDIVSAARIS CEMLLRVIND LLNFSKLEAG KVTLESDLEF
SLESVVCDCM QSVYSACAEK GINLSYNVSP DIPFFTAGDG MKIGQMLKSI LDNSVKTVNN
GFIRVRAFLA GSSKKNDRDQ LQIAFIVEDT REESNAIFLA NMINSLNRGC NDYLPMDLSG
TALGMSTCLQ LCKIMGGSVS VEVSQNNPTF KICYDLKIHE LGKERYDIIA TPLFQNLTEF
NDLIKSKVAI RVSKTSTEYD NITTYLQAAR KVLHVFKGLQ DLASIFDLSP DSALLRCSVV
VVDVYSMDDV KAVEKILKSY PDVHVIYLCC DPSRLNIEQE LQKPSGRSFA CKKRWGFLQM
PCTRENFLKV TLQVFKSNED TCNFYSYVNE YGESPKPDDD MDRLNKCVGS KILIAEDNPI
VRMTLKKQLE HLGMDVDAAE DGKETLQIFE SHPDNYYQVC FVDYHMPVYD GLEVTRRMRK
IERKHGCAPL PIFALTADMQ PTMETQFQEV GITHYLSKPF KKETLIKMLL QYLVNGTDGN
ANTS
