ID W9YD46_9EURO Unreviewed; 2303 AA.
AC W9YD46;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=A1O1_03519 {ECO:0000313|EMBL:EXJ90418.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ90418.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ90418.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ90418.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ90418.1}.
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DR EMBL; AMWN01000003; EXJ90418.1; -; Genomic_DNA.
DR RefSeq; XP_007722612.1; XM_007724422.1.
DR STRING; 1182541.W9YD46; -.
DR GeneID; 19158411; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000019484; 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: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; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
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:UP000019484};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1285..1847
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1964..2274
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2271..2303
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 290..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2303 AA; 258423 MW; E057167017613E4F CRC64;
MALAPGARQP HGFEPPPSSI LATHVVRGQG VPDLDRHHFN QLLTEVLGSN DEGQPNLGDD
VSVNHKLICI IFQVGIEPAL EENPFRAAAA SGKVDAQLRR CLAVLQVAIE RSPQVLFMIS
DPPGKDVTGP PCPLYYWLIP RLLPVIPLCQ EVEARDAVLD VFNAMLEVDK KCATAYSCGN
VLEFLRRCIS GLVKITASLH IRHPRKAIII DPEDFATAVS DVTRGTPVTI PALKFPSLRL
LFMTLARSLK VVSKHSETAQ DKLQFWKVFT RFRQFVDDYS DLTIEKDPSE ELSHEIRSLN
NTPRRPRSKP ATSNIAETWP ESDRARKRLR LSTDTEDGLP NQSSQQKVCR RITMELTGRA
VPDLDGLSQA ASANFRRLSE DKQCAALEAL GTAACQLALQ SQESHCQICD EGSDSANTSE
IPVAATSEEL LKTLVALVQS ISRQSRARVA AMSALRRVLM HTDSASDLKL SQTPAGDWCL
QSLKSSSRDL RITATRTLQA YVMRRRSVDV SLIRENRITA LDLLHILWEK AEVAVQETSV
MALVQMAQVV GDEELNIILV RLIEYLGHSN PYLSGVVYAE IQHLAVAMHM SVWLLFRPFW
RTLGVVLAKS LTNRPNVADQ LCDLLGMDMT GLMGHTAEYA LPYLVLHKEL DTIRRFAEAN
GSSTTPFDLC TQGKNLIAIL SFLLVQPFSD AEQSIISLLS EVSEDFGKND LASWVALDPI
HITCELLKVI GDSGQGKSSR VYQALQLLAQ LVARQRGQSS GSKRSDSMGS FLENNVLAIV
THFTVLLNDL EAKEPKVEKR RCLAALGEVV KLGKSRVVRA LPQICACLRS GLDDKELCNA
AFSSWVAMIR SLKKDDLAPL IDQTLAIIVR TWDVLDSPSQ QLAHDVVGEL LRNHTALIRE
QFSTMPSLAS IPLLAKYEAE ISALKRQMDE RRQLAAFIPR LQDENLVVVQ QALNELPPLL
AQKQDLLQRS ILREQPDEFV ANLTRALLEC CVRFNTSIEI GTLCGQCLGQ IGCLDSSKIE
SVKERKTMVV LSNFGKADEV IEWVFFFLQH VLVNAFLSAT TTRAQGFLAW AMQEYLKTCE
QDNPSRHGEG NLASRLWAKL PDSIQNTLTP FLSSKYTVQE IRPPEKSQYP VYRPGMRHRD
WLRTVTLDFL HRGSGDNVDI MFGIACRIIH GQDSSIPAFL LPYTVVNLIV SGIERDSEDI
LEEITCILSL SLDGQERRVQ DDIKLCSQTV FEILDYVSTW HQQKRKQYAM GVARSDRGHN
DPLLENAAAQ IRSIERVLER IPPDILAKRA LECKSYSRAL FHWEQHIRKS KADDMETELQ
RMQDIYAQID EPDGIEGISS RMYVLDIEQQ VLEHKKAGRW TAAQNWYEMK LLADPDNNDV
QKNLMDCLKE SGQYDVLLHH FEGIKRRGTT SGTLLAPYAL EAAWATGQWD RLSSYVPKSG
GYDFASHLAE LMLAVKNNDT AKVTQLFEEL YGTAVSELTP ATISSFQASH DTLLKMHVLS
DVQLITSSGK DDRSSVLETL RGRLDVLGSN VADKQYVLGV RRALMSLRQD TFTSDDVAAA
WLSSARLARK ARSTTQAFNA VLKASALGDK SAAIEQAKLM WLEGHHRKAI QILEGAIESG
AFIAHDYIAE NGPVTMTVEQ RHSQNELIAK AHVLLGKWLD QAGQTQSDAI LKTFRKATES
FRRWEKGWYN VGRYYNKILD LEKTMPPGKE SQTYLTGETA KLVIDNYLKS LTSGSKYIFQ
TLPKILTLWL ELAEMADLPK DPRRGNDSFH MHNSAQRKRV IEDTNNLIKR YIDRLQPVLF
YTILPQVVAR ICHRDHTISG MLGSIIVKVV RAFPQQAMWT LLAVVQSKQK DRAKRGIELL
RQIYETEKKS SKGGTASAVE LRNLSTKGQT FITELIRISE EPINEKVSRI SLSAKLGFKH
EIAPPKLVVP NQASLIPSMP TNFEAAQLKA FRPFAKEPVT ISGFLDEALV LSSLQKPRRL
TIRGSDGALY NVLAKPKDDL RKDQRLMEFN TMINRVLKRD VEAAKRRLYI RTYAVVPLNE
ECGLIEWVDN LKTFRDIILK LYKDKSIQPN YIEIRNLLDE ACSGDPDKIQ IFPTRVLSKF
PPVFHEWFVE SFPDPSAWFN ARLRYTRSAA VMSIVGHVLG LGDRHGENIL FEEDNGGTLH
VDFNCLFDKG LTFEKPEMVP FRLTHNMVDA MGVYGYEGPF RRCCEITLTL LRSNEDALMT
ILETFLHDPT TDFINSGGRK KKQVNGVPNT PVEVLEGVRA KVRGMLPGES VPLSVGGYVD
EQIRRATDMA NLARMYIGWC AFF
//
