ID G9NPI3_HYPAI Unreviewed; 2441 AA.
AC G9NPI3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=TRIATDRAFT_181231 {ECO:0000313|EMBL:EHK47452.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK47452.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK47452.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK47452.1}.
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DR EMBL; ABDG02000020; EHK47452.1; -; Genomic_DNA.
DR RefSeq; XP_013945657.1; XM_014090182.1.
DR STRING; 452589.G9NPI3; -.
DR GeneID; 25777117; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_1_1; -.
DR OMA; SMYIGWC; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000005426; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT DOMAIN 1420..1990
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2104..2412
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2409..2441
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK47452.1"
FT NON_TER 2441
FT /evidence="ECO:0000313|EMBL:EHK47452.1"
SQ SEQUENCE 2441 AA; 275864 MW; 74F43BF7D620E51F CRC64;
PPPSTLAAQL VENIASSTKV SRSDENSELK GLLAIIQRVK DNPDLLKTPN DRIEHNHMLI
YVYCRVVLEN IKLDDPFLDR ATVRAESQKA INFLRFTIKE TPSVLLHRNG NRGLLFRSQE
PLWVWLLPQL LRLLGHPQCL DLDSSIEGFL QYILLLVART GSLWKVAPYL GLYLRASLAS
LLDHLQSPTL ATSHTELNTN LELPPPFALD QILDKDWEHA SKRISYSIHI ASQGLRLASS
LARVLAYPLI SPDPAFSSSV SLLENGPWLI DSFLDLRHIQ KRLELSSQCT PLPLIELTMD
IIKSAITNDH PSASLVEKSC ALLILLCSEM ISPPDELVQS TPAGEQARST YGMALLIITR
ASFKCYTIGR FAASKLVQEL ILLSSQFLVI GEDTDIWRCV TFLRQAIGSL PQESIQDHVH
PSKFQDDELR KCVQDLSLDY KASNETIHAK KRRKLSEEKT DSLEILTHGI FETLQVAQPS
DDDVVLLEQI FLDGYEKCSQ PNQSLALDLL SRICCVADNS ARVRNSTESL APPITCPVCD
EGSSSSPTIS PHNAKSEARQ IFSKLIRLPE FLESRKPRVA AMIALRRLVL HCEDAAFLNL
ETSGPGQWCL QSLNSSIREL RISAGRTLAL FMPSKPTYYM EEALLSRNRK NSIALLRSAS
EADQPLMRET RILAWGQLGR VVTEEELNLV LIKLLEYLGS SNNIESAFAF NELLSLAEAR
RTTPRRLFEP FWKNLAYMAT KDIVQRPQRS RAIAELLQIS VNELLLLIQS HALPWLVLDK
RKDVIQKIAE ARQETEIWRP LMDSHNTASV LSLLLLQESE NIEEFVKSSL DEISPHFHAL
RLADIVQSEP VLTAIELLKA AAGADESRKR QIQKALTMMA SMVLGSVKET RNRKTDLVGR
FLQSHILGLM ARFTDVINDS TSIHPRVMEQ ISCIRALEEM IRICQSYARI ARPQVRRKRA
ILLRISACLL SAASQDSLRE PALSCWAAML KYFDEEDVEA QLEATFFIVK RYGPQLEPPA
MTILKDMLKN LLQKYEHVVE KFITRLPSLS HVAALSDIEA KLNTFRPSLV FEENLDIFSQ
RINHDYSGVV HQALIDLAPY LRSNQNALYT SAISQRPDNV IATLLRTLLD CASKYNGAQA
DITRLCVECV GLIGCLDSNR IEAVREQRSI IVLDNFEVME EATDFVLFLL QEVLVPSFLS
TTDMKLQGFL SYAMQELLER CEIRSACSNH AAGLAGGSDI YRKWMTLPEY VREVVAPFLN
SRYMVAPMNP QAVEYPIFHP GRLYGNWLRA FVVDLLRKGQ HPYADMIFEP LTRIIRVKDL
STAEFLFPYL VLHVLLGPRS SQTEKDQILG EILHILNYQP SPDASYQERE DMKRFCHVVF
QTLDYAMRWI HAKRSSRLTE AAKQNVSRIQ RLLDSIPAEL IAQRAIDCNE YARALFHLEQ
HAQKTEQAKR EPGDRTRLLQ QLQDIYANID EPDGLEGISA HLHVLDINQQ ILSHKKAGRW
AAAQTWYEMQ LAEKPDNAEV QIDLLNCLKQ AGQHVDVLLN HVEGMRTDSL SNDNRIMPFA
VEAAWVTGRW ENLDRFINRF QGNVLQDFNM SLGVLLEALY KGAAKETFIE TAKMMKENIA
LSMTSSTTAS LQAAHDIMLK CHVLTDLEII IGTKPENDEE RMKTMSLLEG RCEVIGAYFS
DRQYVLGIQR AAMQLLRPTF SDIDISGLWL ASSRLARKAN SLNQSFNAVL HASQLGDDAA
TIENAKLLFR DSQHRKAIQF LQGAIEQNRF MTKTNSSLSM GSASNLNNHQ KLLTARAQLL
LAKWLDAAGQ THAGALREKY QQPPKTYSTW EKGHYYLGRH YKKILESEQP LKVDDQSDNY
VTGEIARLVI ENYVRSLNSG TKYLYQTLPR ILTLWLELGA QVDKAPEGKV SLSRELHKRR
LEQLGLLHSF LDKYIHRLPA YIFYTALSQI VARIAHPNAN VFERLTHIIV KVVEAHPRQA
LWSLIGIMTT RQASERKARG SQVLQTLKSV SKKADGGSYD LKYLIRAGEK LAEQLLLACH
NGDFRGNKTV HASLTKDLRF NQKCTPCPLV VPVESGLTAT LPAVSEHVKK HKAFSRDVVS
IDCFLDDVLV LSSIAKPRRL TARGSDGKSY MLLIKPKDDL RTDQRLMEFN GIINRSLKRD
AESSKRQLYI RTYAVVPLNE ECGIIEWVPG IKTMRDILIG LYASQKIHPD YNSLRQLMEE
ASTSESKIGL FTNDVLGRFP PVLPLWFIQQ FPNPSAWFSA RLRYTRSCAV MSMVGTILGL
GDRHGENVNL EEGSGGIFHV DFNCLFDKGL TFQKPERVPF RLTHNMVAAM GIYGYEGPFR
KSSELTLSIL RQQEETLVTI LEAFVYDPTL DLQKDKGKSK RDVGVRLQPQ SVVDSIKRKV
KGLLPNESIP LGVEGQVEEL IKQAVNPRNL AAMYIGWCPF L
//
