ID A0A0C4DR96_MAGP6 Unreviewed; 2480 AA.
AC A0A0C4DR96;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MAPG_02402 {ECO:0000313|EMBL:KLU83340.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_02402T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU83340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU83340.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU83340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU83340.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_02402T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_02402T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_02402T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_02402T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of
CC DNA damage, involved in the regulation of DNA damage response
CC mechanism. Required for the control of telomere length and genome
CC stability. {ECO:0000256|ARBA:ARBA00025079}.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR EMBL; ADBL01000601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876967; KLU83340.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4DR96; -.
DR EnsemblFungi; MAPG_02402T0; MAPG_02402T0; MAPG_02402.
DR VEuPathDB; FungiDB:MAPG_02402; -.
DR eggNOG; KOG0890; Eukaryota.
DR OMA; SMYIGWC; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF124; SERINE_THREONINE-PROTEIN KINASE MEC1; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000313|EMBL:KLU83340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011715};
KW Transferase {ECO:0000313|EMBL:KLU83340.1}.
FT DOMAIN 1452..2027
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2141..2451
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2448..2480
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2480 AA; 278060 MW; 547B64B1910E7BD4 CRC64;
MAPESYGRGG FAEQRGAAAR MAPEMVAAGH AGIGCNNPPP STLAAQLVEN IAVSSVRSSR
SDETQELQKF FTVIERFKND PNLLKTAAER VEHNHMLIYV YCRVALDGLK WDDPFADRTR
LKAEALKTTN FIRVTIRETP AVLAFVPDEG AFLFRRSEPL WLWILPKILK LLGSERCLEI
SSVIESLCEY ILATVNQSSS LWGETGPIIC YFQTSVNSLL SHLATRSPNN VHSAISLELP
SKTTSPDTPS RAGSSPFRGC TYRVTSVKHA TRHAWSLLNL LGTAASSART SPALSAAFRQ
TVPWLIDSLQ AFHAIRARWS HEGNLETHTA SIIHCLIKLV TLQENVDVVQ ADVHHKILSV
LALICGRCLD STSELLLPDE NGAVTRKAFC LAMVQISHSA MRYKPVSRLA TSQFVNHLNN
LATQHEILRA GTDFSRCLRL LTNAVSCADV SSFRPDVTLE EFVDIDIRQT VSRLKLHAPA
QLASQPLAKR RKLSSEPAML RSVIAHICKI FKADILEDYE RLQNLVVLGY PALEGNDASR
MIDLIAHVAC AADNTLALVS EPMTQSSGFR CSFCSGLAKP QRTPQSLDRA AKLMAVTVFT
RIIKLPIFLN SRKPRVVAMM ALRRLVAHFQ EPDLLDLEKS APGHWCLQSL NSSIRELRIA
AGRALATFLR DRESAAPRTR GVINGNQSIA LGVLKTLSDK DVAHLNETCI MAWGQMGIIV
SDKELNLVLV QLLDFLGHRN TIVSAFAFNE ILNLASARNT TPRRLFEPFW RSIAFATVKD
MITRPQTTRL TAEILQISVT EHLLLVQQHA LPWLVLTRKK EVVQKIAEAR GETEAWKPCL
HNANLSYILA LLLVQDAPNI QEFVLSTLQH ISSHFNNITF QALIGSETVL TVLELLRDAG
EANDERKERI RLALHTMAYV LMDGKQMKLK KKVLVAKFLQ LHALGLTANL AEVINDGSAR
HYPVHEQKRS IRAMEEMIKM CTSLIRIARP QISAFLLSAL SYDELRACAF SCWAALLTNL
DDEDVDALIE TTFFIIGNYW ETLDDPTQGV CRSILDRLLT KNHGLLEAKI NELPSFSHLS
GLADAEARLN KLRKPLDSRA SFMIFSKRLG NENPGVVLQA LTELSSFLRE HQAFLQTSAI
GEQPDTAVTA LLRALLDCAS RYNGVQPEIG SLCVQCLGSI GCLDSNRLEA VRERRQFVVL
QNFEEASETT DFVLFILEEV LVKAFLSATD TAFQGYLSYA MQELLDRTDF KAAFTSNGAE
GAQVLEKYVK LPENVREVLA PFMTSRFRVN PMAQQKVEYP IFRPIRPYAI WLRSIVTDLL
HKGQNPFAQI LFEPLCRVIR VKDLAVAEFL LPYLVVHIVV GDDNVKTDRD RVLNELRSIL
LLELPENASY AERENMRLYC EAVFRVLDYS TRWLQMRKAQ HSQRDPRQRD PPAPSPEIKR
VEQLIKAIPA DLIARRAMDC GQYARALFNL EPHATKMRNN PKADKEETSR LLSELQYIYT
QIDEPDGLEG ISARLGVVDL NQQILSHRKA GRWSQAQAWY ELRLAEEPNN VEVQLDLLTC
LKESGQYDVL LNYVEGISTT PATINRIAPF AVEASWATGR WETVQKYLNS YNAGDVTEVF
NLGIGQALMC LREGRRDQFA QYVHLLRDKV SASLSYSATS SLQACHDAML KAHVLNDLEL
IAERSAQAAD QTQGLDQQEI STVLSRRLEV IGAYVNDKQY LLGIRRAAME LMRPQFGDGD
ISSLWLTSAR LARKAGSMHQ SFNAVLHAHR LGDDSATIDN ARLLWKEGNH RKAIQVLQSA
ISSNNFIGHS LGTSVPTSSK SQETQKQLVT AQAHLLLAKW QDSAGQTHAS ALRQQYQLAA
KTHSRWEKGH YYLGRHYKKV LESEQALKPM DQSDEFLSGE TAKLVIENYI RSLNYGTKYL
YQTLPRVLTL WLELGSQVDK PTLEGKISPS RELQQRRKIT LEALHKYLER HLDKIPAYIF
YTALPQIVAR IAHPNGGVFR VLQAIIVKVV EAHPRQALWS LFGIMTTKTT SDRKARGLQI
IQSLNKASKK VDGTGYDLRQ LIRSGEKLAD QLLLACQNGD FQSNRTTTAS LSKDLRFNPK
CTPCPLVVPI ETCLTPTLPA LTDNVRRHAA FSQDLVSIHN FLDEVLVLSS LAKPRKLLAR
GSDGRTYGLM VKPKDDLRTD QRLMEFNGMI NRSLKRDAES SRRQLYIRTY AVTPLNEECG
IIEWVDGLKT LREILLSFYR AMGITPNYNM IGQMMKDAAA MDGRNVRIFS HEILGMFPAV
LPLWFTSQFP DPSAWFAARL KYTRSCAVMS MVGTILGLGD RHGENVLLQQ GDGGVFHVDF
NCLFDKGLTF ATPERVPFRL THNMQAAMGM CGHEGPFRKS SELTLSILRQ QEETLMTILE
AFVHDPTLDL QKEKKHRANA GGGVRLNPQS VVESIRRKVR GLLPEESIPL GVEGQVEELI
KQAIDHKNLT AMYIGWCPFL
//
