ID A0A2H3JT05_WOLCO Unreviewed; 2015 AA.
AC A0A2H3JT05;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=WOLCODRAFT_69995 {ECO:0000313|EMBL:PCH40938.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH40938.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH40938.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH40938.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR EMBL; KB468113; PCH40938.1; -; Genomic_DNA.
DR STRING; 742152.A0A2H3JT05; -.
DR OMA; SMYIGWC; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000218811; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
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; IPR011009; Kinase-like_dom_sf.
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; IPR011990; TPR-like_helical_dom_sf.
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 SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1000..1552
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1657..1974
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1983..2015
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2015 AA; 227468 MW; 211D0F5644D2F50A CRC64;
MLTECTKVEI YSGVIKAIED LLSQPRYPAE GAIIVTDTSQ LTYTSWRTSI KDCVQAIIEP
HELNWTVEND SFPDGEFISQ ALRTVKERFE HPLYNRAASA RISLAQTLGK LPCMVVHASR
SDCSSASKPD VDFLSPFVPV VDRLCNGPAN EVTAGVRKAV FQCLSHALRH HTSGYEDRKF
DRLTNSISQS LQDDDRSVRL SAGSALTELI RLYLATGRSA WEQTEGVYVM MHRLFETAED
CVKETALITL GRIGRIATAD ALGQTLCCLI AQLGQRSTIL RGTARIQLTA LAKYHRKTPW
LLFSPYMDDV APYLVSRLQS QPNLLREACG FFSKEPYDFV SINLHCILPK LFITCDAAAL
HAVADILDRT ASHLFIEYAH NVLALTFRLR EPGQTDKTIR FIQELLEQTA GCRVETSRFV
GGYIVPLLAE LVMFLGHEDP DEAASAREAL KKVERTMSPS STPALTRSRS SISQNTSQTT
SNFLKPYMLG IITHLNDLLC DVMGKLPVAS KKMIIRCLGS FAEEVGPTVI NVAPQVMATL
QSMIAIPEFA DATLQSWYAF LTTLDEHDLG PYVGSTSASL LTFWPTFSQH GQRMAKQCLD
FIVRDRGGAL GAYLDEVADL EAIPELSTTH QALRAMRETW EPRDKLRKIL DRLNSESTTV
SVQSLKELRS FMLFKEEEDI RSLTSGDMFD PLIGRMIMSL FSAASRDGEG TETLRMLALD
CIGILGAVDP DRLEIGTAAS RMVVSSNFQD EDESVLFALH LIKDVLVDAY RSTSDTQYQI
LLAYAIQELL RFCKFSSALI ASRPSGSVGI KVRNRWNSLP KHVLETVSPL LDFKLTMEPR
APTAVEHPIY PSRATYREWI QAWTGHLITK VSGEHAKAIF QLFSAPVRNK DVGVAHHILP
HLVLNVLLSG SEEEVHNIRQ ELLAVLDDRP TSESQIVSDK KLLSSQTVFM LLDHLNQWVR
IVGRDIRNKK AEKKPRRTKS QEEEQLLRID SVLSSIDVGL MAKAALQCKA YARSLMNFER
QILVLQSRGT PAHDLHEYHE RLHEIYAHLE EPDGMEGVST LLLSPSLEVQ IRQHESTGRW
TSAQSCWEVR LQQSPDNLDF HLGLLRCLRN LGHHDTLRTH VKGVLTRNPG WQTHLVGYQV
ESEWMIGNWV EVRNLIEDTT SKSAPVLLAR VLLACRTGDD SLISDALAVA RRSLGAPITA
TDIRGYRRSY DTVLNLHLIH ELEVIHNAIG AHSTGDRPNL QATIERLTRR LSTRLDSTLP
NFRIREPILS MRRTAFGLRP IDDENARENI AQCWLTSAKT ARKAGHWQTA HSAILQAQQC
NATFYSSIES AKLKKASGDA VRALQELESS MRLSGLLSSG GDELVGSTGS NQKVEAKAHT
LRARWMAESD RFDSNQNMMA FRQGIKLSPK WESGYFHLGR WYDEYCKGLP PREKHERGLL
MNFQTVLHYA KAMRFGSKYI YQTIPRLLTI WLDMGEDETL AKHEIFEKIN LVVSNTIKSA
PVYKWYTAFP QIVSRVGHTN KEVYVVLSQL ISMVIREYPK QALWLFTSVV ESTKEQRRRW
GKTILDKLRV KDLGELAELI NESLKMTAEL LALCDRRVKD DKKMLSMVKD VPGLWNMVPS
RLIIPLQESL VASLPPNSSS DSGHQPFPVD VPTFHKFLDE VEIMRTMAKP RKISIEGSNG
QTYMFLGKPK DDLRKDARLM DFNAIINKLL KSSSESRRRQ LRIRTYGVVT LNEECGFIQW
VPNTVPLRPI LLHLYERRGL RHYTPEMASV FALIKTTNHN RDAAKLFRDK ILKLYPPVFH
EWLLETFPEP NAWLAARLTY SRTTAVMSMV GFILGLGDRH CENILLDTCN GDMVHVDFNC
LFDKASRARL GKALEVPELV PFRLTQNIVD GFGVTGVEGP YRLACEVTMQ LLRDNRDTLM
SVLDAFVHDP LVEWEDEKRK KVRRMPRANS APMDARELAK NALKPIELKL NGIYTTSRDK
PAKELVTSSL VELLIQEASS DNNLARMYAG WAPWQ
//
