ID A0A167BLZ8_9HYPO Unreviewed; 2437 AA.
AC A0A167BLZ8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BBO_06245 {ECO:0000313|EMBL:OAA40187.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA40187.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA40187.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA40187.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA40187.1}.
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DR EMBL; AZHA01000020; OAA40187.1; -; Genomic_DNA.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000076863; 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:OAA40187.1};
KW Transferase {ECO:0000313|EMBL:OAA40187.1}.
FT DOMAIN 1419..1986
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2100..2408
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2405..2437
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2437 AA; 273950 MW; F9D5A764B55F6477 CRC64;
MAPLPDIGGL GGGGGPPPST LAAQLVENIS ASSRSARSDD NAELKGLFAV IQRFKDQPEL
LRTPAQRTEH NHMLVYVYCR VVLDAVRLDD PLLNWPHVRA ETLKALTFLR FTINETPAVL
CYASATHGLL FRGAEPLWAW LLPRWLRMLG HPECEELESA IEGFLQYLLL TVARVSKLWP
MTGPLTVYYR GCLTGLVEKL QLPAINFAKT NAPTDIELPP AHVLDQVLGG PSATPSVSLI
YHIRLARQAL RQAHSLARVL AYPLICQDSA FSSIAPMSEI GPWLLDSWLD LWSAQKRHEG
DEKRSPLPLI GMAVDVVKAA KGDHAVATAT KNKACTTLVL LCSEMVSAPE ELAKADAGGD
AARTSYCLAL VAIAQAALQL PTISRLAASK LVNELSLLPA QYPALGEETD VWRCAVLLRE
VVNQDRLQTL PSATHPSLFQ DAELRRSVGS MCLTHEQPTA HGNSTKRRRL NELSERDAAS
LAIKSLYAAL ELDAPAHERE LDPTLILNAM AASNDAMKCL AIDMLSKLCC VLDSQLNDLG
EIECAICSGK DVLRENVQAH DIKTIIRSIF TELIRQSNFL ESRRPRVAAM LALRRILLHC
EDATALNLET STLGQWCLQS LNSSIRELRI AAGRVIVTFM PPKATPYIDD SLLSRNRKNT
IALLRSVSDN DQTHLVESRI LVWGQLGRVM PENELNLVLI KLLEYLGSSN SFEAAVAFNE
LLNLADSRST TPRRLLEPYW KSLAYMATKD MVHRPQRSRA IAELLQLSIN ELLLLIQTHA
LPWLVLDKRT EVIQKFAEAR QESMGWQPLM DNSNLAAILS LLMIQETDDI ESFVRTRLND
VGLHLHDRPI VELLQIEPVM IAIELLKAAG QADGARKQII TEALRWMATS ILSANPETKK
LKKGNMIGRF LQSHILGLMA RLTDVINDPA IMHPGELEQR NCIRALDEMI NLCQSHARIA
RPQISACLLA ALAQDSLRDI SLSCWASMLM NFGEEDVEAL LETTFFIVKY YWPSFSPSSI
ETARAIVSFL LDHHGAIVQN NISSLPSFEG ISALSKLEAK LQALRPKLLP EELLPLFARR
LRHENSGVVQ QALNELVPYL RANQSALYTS NITQTDNVVT VLMRALLDCA CRYNNLHGSI
SRLCVESMGL IGCLDSNQLE TVREQRSIVV LNNFESFPET TDFALFLLEE ILVPAFLSAT
DTRLQGFLCF AMQELLDRFE IKAAIAMQNT GGVAGNDIYR KWIALPENVR EVVTPFLTSK
YMVAPMLPVK VEYPIFNPAK PYGNWLRSFV IELLRNGQHP HADMLFEPLS RVIRVKDLST
AEFLLPYLVL HVLLGSKSTN QDKDQILNEL TSILEHSPSE DASYTEKEEF KRYCHAVFRV
IDYAMRWVHS KKTSGKLSSE AKEQVANIQA ILDNISAELI SQRATDCNEY ARALFHLEQH
VQKMEQHKRE PGDRDRMLQR LQDIYANIDE PDGLEGISAH LHALDINQQI LGHKKAGRWT
AAQTWYELQL AEKPDNVDVQ VELLSCLKQA GQYDVLLNHV ESMFTDSSSD VKIMPYAVEA
AWVTGRWESL EKFVERFQGD LTQDFNMSLA SVFSSLYKKR AHSGLKQTVQ GMREKIGAAM
TTSATASLQA AHDSLLKCHV LADLEVIINL KPDREDDRKQ ALGLLDNRLD IIGAYFYDKQ
YILGIRRAAM ELTRPKFSDL DISALWLTSA RLARKTDATH QSFNAVLHAS QLGDDSATIE
NAKLLWKDSH RRQAIQMLQG AIERNRFMTQ TGVSITASSS KLSPHQKLLT ARAQLLLAKW
LDTSGQTHAL ALREKYQQPP KTHSMWEKGH YYLGRYYKKI LEAEQPLKID DQSDNYVTGE
IARLVIENYL RSLTFGTKYL YQTLPRILTL WLDLGAQIGK APEGRTSLSR ELHKRRADQL
NLLHTFLDKY IKRLPAHIFY SALPQIVARI AHHNASVFER LAHIISKVVQ SYPQQALWSM
IGVMTTKQAG ERKTRGTQIL QTLRSTSRRV EGSSYDLKQL IRYAEKLAEQ LLLACTNGDF
QGTKTVHASL TRDLRFNHKC TPCPLVVPVE GTLTAALPAA SEYFKDHRPF SRDVVTIDCF
LDDVLVLSSL AKPRRLTARG SDGKLYMLLI KPKDDLRTDQ RLMEFNGQIN RSLKRDAESS
RRQLYIRTYA VVPLNEECGI IEWVPGIRTM RDTLLTLYAS QKIYPEYMAL KQLMDEASTS
ESKIRIFTDD VVGRFPPLLP LWFVQQFPNP SAWFAARLRY TRSCAVMSMV GTMLGLGDRH
GENVNLEEGN GGIFHVDFNC LFDKGLTFAK PERVPFRLTH NMVAAMGVYG YEGPFRASSE
LTLRILRQQE ETLMTILEAF IYDPTLDLQK EKRARKSDAA VRLQPQSVVD SIKRKLKGLL
PNESIPLSVE GQVEELIKQA VDPRNLTAMY IGWCPFL
//
