ID M2PUS5_CERS8 Unreviewed; 2019 AA.
AC M2PUS5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CERSUDRAFT_44292 {ECO:0000313|EMBL:EMD40504.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD40504.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD40504.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD40504.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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; KB445792; EMD40504.1; -; Genomic_DNA.
DR STRING; 914234.M2PUS5; -.
DR HOGENOM; CLU_000178_2_5_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000016930; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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:UP000016930};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 992..1556
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1661..1978
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1987..2019
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2019 AA; 227103 MW; A8BE2FC87623CFFD CRC64;
MDRISDQGGT PFASLLEALT RHDHVVSAAP NTAAALNSDD TRPSWRSIAR TKVQNIIQPD
DIPWMDDDGT LSNTQYMARA LAQIETRFQR PLYNPDPKAR SALAEDFSAM LCGMAHPDSL
RCKPCSLPAG VPTIPAYMAI FNNVLDNSDQ VTAPVRKAMF KALTRLIQHT SGFGGGMLTR
FADHVSGGLK DLDRNVRLGA GHSLVELIRF HQSLGGGAWR RTEQLFTTLY RLLDAPDNRI
RETTLITVGR VALVAQGEIL GQSLCCLISQ LGNSSPIVRG LVSIQLRNTA LAQKKTPYNF
VSPFMDQIAP FVVTRLSTHP TLILEFCRFL SVSPLDFVSI TLNRTLPQVF ASCDSRILQA
ISHETEEKSS SLFLKHAPEI LAHAFRLQAP GQTHKVLMFI IGVLQEAAGD STIDVATVVG
SCIVPLLAEL VVSLGHDDPE EVNTAMQALM KVERTVSAKP NRRVAPPQNI GAFLRSYMLG
VITHINDMLQ DVQGKRPIEA KKRIIKSLGP FMTEVGPGVS HVAPQIMATL QTMLPIQELV
DATLESWFTF LTTLERRDIG PHVGPTSAAF VAFWSTFSLN GRDICRRAME YIICDKGEEL
GSHLDEVVDL GSIPLLKDAN QKLAMLRSAW SPRDKLQKIL ERSLSESTTV AIQSLIELKH
FILDDQEAFV RDLTTGDVFD PLIGRMMYAL FSAACRDGDG NEKLRLLAYE CIGAIGALDP
DRFTLGMTDS RIVVMNNFAD ENECMIFAIH LIRDVLVGAF RSTSDIKYQS HLAYAIQELL
RFCKFTPALV TPGPSNSVSL KVRNRWNTLP KYVLESVTPL LESRFRLEVR VPAQVQLPIY
PIKTTYREWI QSWTSYLITR VSAERARCIF DVFQSVVRNK DVGVAHHLLP HLVLSILLSG
QEDDAHNIRS ELLVVLEDQV RRDTESTDDK RILSAQTVFM LLDHLNQWAR AVRQEMNKKK
SESKRSRTNH VSEAEEQLLR IDSVLSSIDQ GLMAQAALQC KAYARSLMNF EQQVVMLKEN
DSSSSQLQGH YERLHEIYAH LDEPDGMEGI STLILSPSLE HQIREHESTG RWTSAQSCWE
VRLQQSPDKL EFHLGLLRCL RNLGHYDTLR THVKGVLTRN PEWEPQLVGY QVESESMVGN
WEEVATLVEK TNMQTSAILL AQVLLALRTG DASAISESLA AARKTLGGPV VASGAKGYRR
SYDSVLDLHL LHELEIIEKT ASFCSGLGHS PERGEIYQRL SHRLDARLDS TFPAFRTREP
ILSMRRTAFA LSRAGDDNFR LAIGQSWLAS AKIARKAGYW QTAYSAVLQG RQSNAPFSFM
ESAKLIKASG EHLRALQDLD NSMKMSGIFD EQPNEQPRDA ADSSRDAIDD ILKAKVSLPH
RAHLLRARWM NESDRFEATV VLRAFQCPVE IQQKWENGYY HLGKFQDDCF KALSSKDKLG
RGMKMNLQTV RCFIKAIKHG TKYIYQTVPR LLTIWLDIGE NPTLASTDMY RRINQEVARA
LKSVPVYKWY IAFPQIVSRV GHTNNEVYDL LSQLVSMVIS EYPRQALWLF VSVVKSTKAQ
RSQRGKLILD KLRAHNVNEV STLIGYSLRM TEELLGLCDH PIRDEKKMLA MSKDFPGLYR
LAPSLLMIPL QESLTASLPP SSSSGAIHPP FPLDAPTFLR FHDEVEVMRS LAKPRKITIT
GSDGQTYMFL GKPKDDLRKD ARLMEFNGII NKLLKSNSDS RRRQLHIRTY GVVTLNEECG
FIQWVPNTTP VRPILLSGYE RRKAKHWSPE MSSLFAKIKE VADKDAAHIF VNQVLPSFPP
IFHEWFTETF PEPSAWLSSR LSYSRTAAVM SMIGFILGLG DRHCENILLD INTGDVVHVD
FNCLFEKASQ FRGKTLETPE RVPFRLTQNI VDGLGVTGVE GVFRIACEVT LQLLRDNKDI
LMSVLDAFVH DPLVEWEDEK RKLEREAQRR NVVRSSVDLR ELAKHALQPI EKKLNGIYTT
SRERPEKETS TSNLVQMLIQ EATSSANLAK MYPGWAPWH
//
