ID A0A0B2WZ44_METAS Unreviewed; 2432 AA.
AC A0A0B2WZ44;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=MAM_00573 {ECO:0000313|EMBL:KHO01572.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO01572.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHO01572.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO01572.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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 -!- 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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHO01572.1}.
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DR EMBL; AZHE01000001; KHO01572.1; -; Genomic_DNA.
DR STRING; 1081103.A0A0B2WZ44; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000030816; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KHO01572.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 704..736
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1244..1846
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2021..2337
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2400..2432
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2336..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2351..2375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2432 AA; 275461 MW; 3403F578545E2E85 CRC64;
MAQQQQVALE RLEQATKGLR SRNGDDVRKR AAIQLRDLVV VCHRDLSQEQ FLAFYNAVNN
KITQLITHGS DSAERLGGIY ALDALVEFDG VDVAAKYTRF TQNIKTILRG KDINPMKPAA
IALGKLCRPG GSLISELVDS EVNTALEWLQ NDRVEERRYS AVLVLRELAR NAPTLMYQYI
PTIFDWIWVG LRDPRQLIRE TSADTVGACF RIIRERDQEM KQIWMSKIYN EARQGLKVNT
VESIHASLLV LKELLEQGGM YMQEHYHEAC EIVFKHKDHR DPTTRRTVVS LIPDLASYSP
ADFAHTWLHK FMVYLSGMLK RDKERNDAFL AIGNIANSVK SAIAPYLDGV LIYVREGLSV
QSRKRGSVDP VFDCISRLAV AVGQTLSKYM EALLDPIFAC DLTPKLTQAL VDMAFYIPPV
KPTIQERLLD MLSVVLCGEP FKPLGAPQPN TLSSVPAITK DVKDPQAYEN RRSEVKLALN
TLGSFDFSGH VLNEFVRDVA IKYVEDEDPE IREAAALTCC QLYVRDPIVN QTSYHALQVV
GDVIEKLLTV GISDPEHHIR QTVLAALDER FDRHLAKAEN IRILFFALND EVFAIREVAI
SIIGRLARFN PAYVIPSLRK TLIQMLTELE FSDVARNKEE SAKLLSLLVQ NAQSLIKPYV
EPMISVLLPK AKDSSPSVAA TILKALGDLA TVGGEDMLPY KDRLMPLIID ALQDQSSNIK
REAALNALGQ LASNSGYVIE PYLEYPQLLE ILQGIIRTED QRGPLRQQTI KLMGILGALD
PYKHQQVEER TPETQRRVDS NQMTDISLMM TGLTPSNKEY FPTVVINALL QILKDTSLAQ
HHAAVIEAIM NIFRTLGLEC VSFLDRIIPA FLQVIRSSAS NRLESYFNQL ATLVSIVRQH
IRNYLPDIIQ ILQDYWDKSP SLQTTILSLV EAISRSLEGE FKVYLAGILP NMLGVLDKDS
SAKRVPSERV LHAFLVFGAS AEEYMHLIIP VIVRTFEKQG QPVFIRKHAI DTIGKISRQV
NLNDYAAKII HPLTRVLESG DPALRVTALD TLCALIQQLG KDYVHFMRTV NKVITQHQIQ
HQNYELLVSK LQKGEVLPQD LTSESRYADI ADETQFADLG TKKLEMNAIH LKAAWDTRGK
STKEDWQEWL RRFSTTLLTE SPNHALRACA SLASVYLPLA RELFNSAFVS CWSELYEQFQ
DELIQNIESA IKSENVPPDL LGLLLNLAEF MEHDDKALPI DIRVLGREAG RCHAYAKALH
YKELEFLQDQ SSGAVEALIV INNQLQQSDA AIGILRKAQL YKEGIQLRET WFEKLERWEE
ALAFYNKRER EIPADQATPI EIVMGKMRCL HALGEWDALA SLTGSTWVNS APEVQRMIAP
LATAAAWGQN KWDHMDNYLS SLKRHSPDRS FFGAILALHR NQFREAVACI EQAREGLDTE
LSALVSESYN RAYQVVVRVQ MLAELEELIV YKQCDEKKQA TMRKTWETRL QGCQRNVEVW
HRMLRLRALV ISPAENMRMW IKFANLCRKS GRMGLAEKSL KQLIGTDAPL ETIIPYWPDN
RSERSGSTPP RNIPAQVTYA MLKYEWELGQ QPLGRRQGIS ERTLYCLQRF TNETAHRLDV
AKAHLAAQAG STDGNLPTDY GIQGQIDPSL MSPQTQRALY DQTVLLAKCY LRQGEWLIAL
NKNDWQHSKV HEILNSYSQA TKYNPRWYKA WHAWALANFE IVQTLSARNE SQLSRADQTL
LIEHVVPAIQ GFFKSIALSV GSSLQDTLRL LTMWFSHGGS AEVNAAVMEG ISNVSVDTWL
EVIPQLIARI NQPNKRVQQA VHNLLADVGR AHPQALVYPL TVAMKSWKNT RRSRSAAQIM
DSMRQHSANL VAQADIVSHE LIRVAVLWHE LWHEGLEEAS RLYFGDHNIE GMFGCLGPLH
DLLERGPETL REISFAQAFG RDLKEAHEWC RQYESSKDVN DLNQAWDLYY QVFRRVSRQL
PQVTSLELTY CSPKLLNCKD LDLAVPGTYK SGQPVVRIMS FDTTLSVINS KQRPRKLILS
GSDGVSYGFL LKGHEDIRQD ERVMQLFGLC NTLLANDSEC SKRHLNIQRY PAIPLSQNSG
LFGWLPNTDT LHILIREYRE SRKILLNIEH RIMLQMAPDY DNLTLMQKVE VFGYALDNTT
GQDLYRVLWL KSKSSEAWLE RRTNYTRSLG VMSMVGYILG LGDRHPSNLM LDRITGKIIH
IDFGDCFEVA MKREKYPEKV PFRLTRMLTY AMEVSNIEGS FRITCEHVMR VLRENKESVL
AVLEAFIHDP LLTWRLTSTA SPAGPNFQSE REVALAGPTV GRARRHSILN ADVAPSELLA
NGEPSGPPAS RARARTNSSA APDGNAVNGA QETESRNARA VEVLDRVQQK LTGRDFKNNE
ELDVISQVSK LIVEATKLEN LCQHYIGWCS FW
//
