ID M5GBA8_DACPD Unreviewed; 2415 AA.
AC M5GBA8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DACRYDRAFT_112961 {ECO:0000313|EMBL:EJU06214.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU06214.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU06214.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU06214.1,
RC ECO:0000313|Proteomes:UP000030653};
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 -!- 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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH795855; EJU06214.1; -; Genomic_DNA.
DR STRING; 1858805.M5GBA8; -.
DR HOGENOM; CLU_000178_2_5_1; -.
DR OMA; SMYIGWC; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF69; SERINE/THREONINE-PROTEIN KINASE ATR; 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; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1389..1950
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2058..2363
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2383..2415
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2326..2352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2415 AA; 270025 MW; 3ACBF5AD03E45FA8 CRC64;
MSTEDVNDYF TNLVSSLESD LAQPPLAGDA LVEFSNDDIT KFRTYALQLS AFLILDVSVW
EDDSFKLAKI ALKYLHRTAG RIPAVLQKED DAEPLHLLVF VRLVTFSVHI FNWSYSSAQE
ERQDAARNLG EVAVGIAAHV LCTLPGSMSR RAMEMGLEWS ELRRCLSLCA TYVNDLLNGR
KNETYPLQMA FDVVQTDPYV LGVKNAPQSA VIILSGTHEA DIAAVSLIDI FVGVLHHSSD
ASGLLAGFEV QTHDLALLAW ERIRRFPAPG SKGAARSTAL TCRLLQLSHR ILQDRVAAPL
PLSMGDVCSH IERLTGRRLL DGYSPTLEEL DHNLGIVWEV LPTQYISHPT HAIDVCWRTD
WSDVQKTEGL RSALYSYLLR ALPFCTAVDL SRLKGSLPEQ DSIALLARLR AAIEVKLQAS
LSPSGTLSSV KKRKRDESSV GVETLAFLKV FDMGEFAIND FDEEHRVVLV DNVSAMFTKP
LETSPDQRYA LAEAVAWLPC FLCHDIHSCI PTSGTENAAS SFLSLYVHAC LRLLAGKTED
VPSRVWTKLL HGMRKAVRHS NIDTLSYSDQ ELFGLVKRAL ERAERSVRIA AGNVIAVVLA
RHMEVDSFVL PKSNVWISVL IDIANGHGKP SIRETALVGL GSVGKVVSEA LIERILTCLI
SHLADQNTLL RALAYTQLQA IVQAKSTTAY MLLMPHMSHV SVILVENLPV APNMLSEACQ
FMGRSPTDFL SLTLHHTLPP LFAAGRKDVL QILARDLGKS IPQLAMGHES RVLAQIFLCP
TEVQTDAGIE FLRGVISEAA KGAPIDLTGM VKGWIVELVS ELVIVLGDHE AKKSKMAIEA
LKKVEKLLAT PAKGQRRAPT SDLSSFLKSY MLGIISRLND MLHELHGRKP DSFKCQVVRG
IGSLIELVGP SVSSISPQIM ATLQGALPKE ALRESVLATW RTFITRLSPD DIGPYIGQTS
AAFVTEWANF SNVERNLAYH TLDHIIEHGH QFPDHIKDVV SLQGIPDLRD LEQRLVQAQA
EWDIQAHLHK LLHRTMNENS VVGLRALEEL KTFMLANAGL ISSLSSGDTF DPVIGLMVNA
LLKASTRDGD SNEATRHAAY ECFGILGAMD PDRFEFSFPD ATIVMLRNFS DEDENIKFVL
YLLQDLLVGA YRSTSDTKYQ SHLAFAIQEL LKICHFGPDL VISGAQSAIS GPIRGRWNSL
PKYVLETVTP LLEGRFSLEN RSSDPQIRHP VYPNAPTYRE WIQVWTTHLI SRISAPEAKK
IFAVFRSAVR NQDVGVAHRL LPHIVLNILL TGHDSDRDRV REEIISVLDD QVHPKLGVAA
DRRMLCAQTI FSLMDHISRW IRLLRQDTSQ RRAESTRQRH GGHVTAVGHE ADEQLACVES
LLSSIDPELM ARAALNCKYY ARSLLSFEQR IVALKENEKS SRDLQPYYEC LHQIYAELDE
PDGMAGISTM VLSPSLEHQI REHEAVGNWT SAQSCWEVKL QSAPDDLASH IGLLRCLRNL
GHYDTLRTHV KGVLSRIPDW TSALAGFQIE GAWIVGDWLD VKALSETACD SSELYVARLL
LAIQMDDQPG ILSALSSARE YLGDHILSAG RQSYRGSYDV VIGLHVLQEL DMICITGEHS
RSATLRSALG MADLSTRLAK RFDSILPTFR AREPIQSMRR TAFALKKTTQ PSLAVEIGKS
WLTTARIARK AGYLQTAYSA TLQAQKYNAP FAFIQTSKLL RVNGEPVRAL QDLENAMEIY
KNVSTGPPNE RISTADPETT TLAKAFSLQA RWMVEADRFT VTEIANKFSE ASKQAQRLES
PYFHVGHFWD ETYTQFSADD KLKNSHFPFN TCKAYGKALS YGSKYIYQTM PRMLSLWLDL
ADQDRSNAMG RLGESTQQIV LSTREKITEM IDKIHRRLPA WQWLTAFPQL ISRIIHPSSS
VFQVLLKIMA GVLVTYPQQA LWLLTSASKS KREERAQRCK AVYSRAQAAP GPSRDHVGKL
IAESIKMTTE LLNLADYNLG DNVYTMSISR QCRELRKITP SHLILPLQES MTVTLPPASA
DQDQHKPFPH QAPIIHEFLD EVEVMKSLAK PRKLTIKAND GRTYWFLCKP KDDLRKDARL
MDFNSMINKL LKKDSESRRR KLHIRTYGVI PLNEECGLLE WVPNTTGLRH ILAKSYEARK
MKIYNNDIAT MLDKERYNGK PGIMFEKQLL PMFPPVFHEW FLAMFPEPTA WLNSRLSYGR
TAAVMSMVGY VLGLGDRHGE NILFDSTNGD AVHVDFNCLF EKGTTLEVPE RVPFRLTQNM
VDGLGVTGVE GVFRIACELT MGILRNHKDS LMSVLEAFVH DPLSEFEEEK RRQDQQAKQG
RSRRGANVSA ATTADGRAMQ LRDYALKSLL PIESKLKGVY SSKQMTTRNQ VDVLIREATD
PTNLGMMYVG WAAWL
//