ID U1FXU0_ENDPU Unreviewed; 2433 AA.
AC U1FXU0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, 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};
GN ORFNames=EPUS_03704 {ECO:0000313|EMBL:ERF69712.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF69712.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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}.
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DR EMBL; KE721401; ERF69712.1; -; Genomic_DNA.
DR RefSeq; XP_007804742.1; XM_007806551.1.
DR GeneID; 19238743; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_1_1; -.
DR OMA; SMYIGWC; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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: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; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; 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 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:UP000019373};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1418..1979
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2095..2406
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2401..2433
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2433 AA; 272686 MW; D754D7B6074B3D52 CRC64;
MPSIVSVSRQ RRWPAGTVNG SQPPPSSLIA THLAPTNGST IPHFDPSDFA LLLQESLGSD
DDGQPNLGTD VTLNHKLICV IIKAGIDTID LGSNDPFRQD NECHDQIQKC LEVFDLAVER
TPEALFLSSK PEDLGSGAEN VPLFIWFIPK VLSLLVLDHT ESKLIAGIVW PLLGKILSAA
KQCSNNFDLC ISVSSYMEEL IGGLLSHFER VDISDGRSQK SSSMATLDLT ELLTSSLATT
NLRDGRFPGA LCLGTVPQGI DTTCRLLRLL VNSVFSRSTM SVTAMKRCVF SIIDQYQRLW
KVLMRVLDGY SEAENQSSKL VEYVFQGMQD LVMYLVQPLG QRSASSFNIL TNEIISVLDI
TIKISTQIPG FASTVCETVQ STVKRMADEE NVVTVVYAKI QASLSQLRSL ATQDDHAHLT
DGLATSQNQP EHDTLSWPDE GRPRKRLRLS SAEHHLPPVS QGQQLCRQLN SLVGGKDTAE
IHELEKTAPD KFQSLTEVDR SRVFELLGQI ACGNSRLSHS NSSIPVSYPT CSICDLDIKT
NMAQLISGDE PDTLIQIFAA LIPLVQRSAK VRVVAMLALR RLLAHTSSPT NLDISNCGVG
EWCLQSLRSS SRELRIAAAV TLKFFLAPIS QVGYQLVHKN RVTTLDFLHS LWLRNVPSLQ
ETTILALSEV AAVGGDEELN IVLVRFVEFL GHPNLYISGL VFAQLQKLAR NMKLTPGSLL
KPFWRTIAVV VVKSIQTRPI IAQSLCDFLG ADMNVDVLLM FIEEYALPYL VLTRKQDLVL
RIALAHGQTM SPFDLCTKSN NFAAILSYLL AQSGVEAENL VMSLLLDTSP EFRQRDISAW
AKLEPILVAC ELLKSIVDAG GERSSKAYHG LQLLAKLDLR RGTMSSGLKK GEVVATFLEN
HVLGIITQFT ATFNDLQSRQ PNLEKRRCLA AIGELLRLGQ HRMSSALPQI CACLRSAMEN
RELCDKAFES WALMMNHIPQ NDIEPLIDQT LAVIVRNWNV FQDSTQHAAH DLIAKIWDDH
KDSVLAILDS MPSLSSVPLL SRFESDISDS KKQMNHRRQM IAFSRRLLSE NVALVEQALK
ELVETLGNGQ EWLHQSLLHE QPEPVVTELI RSVLDCCVRF NSDSAIAGAC GKALGKIGCL
DPNRIETVKD RRTVMAISNF GRADETVDFI MFFLEEVLVK AFLCAPNTRA QGFLAWAMQE
LLKICGLEET VGLRPRTALN AGKYRGWWDL DESVRNTLTP FLNSRYCVNV AMMETRCSYP
LFSSKEMSHK DWLQSIVLDL LTRAPGDNIQ LIFTICLRII RFQDISIPIF LLPYAALNLF
VAGSEKQKEE KQNLLNEMIA ILRQPLSGSQ QHRENIKLCS QRVFDILDYM SKWLQQRRKQ
FQAAVAHNER GTADPATEIV QAQTRNIENI LQEIPPDLIS SRAIECRSYS RALFHWEQYI
RKMTEQEGES DDLLARLQEI YTQIDEPDGI EGISAQMHTL NIDQQILEQQ KAGNWTAAQN
WYEIQLQERP DDGTVQVNLL TCLKETGQSD ALLNQFDTFN KTHSFAHVVP FAVEAAWTNN
NWAKLNQIVD EAANRSNDFN VGIGRILQAL HQKDHHQAVN IVAELRLANA SSLTSTSASS
LQSCHDILLR LHVLDDLESI VSASEDNGPI VLTNLDRRIE AIGADVSTKQ YLLSLRRAAI
ALSPYFNDLD VASGWLATAK LARKSSLSNQ SFNAILRATA LGDESATIEH AKLMWRDGFH
RKAIHSLEGA IDSSVFLSHN FDAEDMSLTS DQIHKQNVVI AKAHLMLAKW LDSAGQTQSE
VIKRQYRKAT EFHKRWDKGW YYLGKHYNKI LDSEKAKPVG KEAQSYLTGE ASKLVIENYL
RALGFGSKYV FQALPKVLTL WLELVAIAEQ PQDARRGNEK FTAHMTAQRK KVVEDTNAQV
KKYVERLQPV MLYTILSQVV ARIGHSNKTV TEILIGIVVK VLKAFPQQAI WTVLALAKSS
SKERASRGIS ILVKVIEVQK RSGRDASTAE LRKVIEQGQR LSDELLRIAD HELKDAKGTH
VSLSKELKFN HKLAPCRLVV PIEACLIPSM PNSQDAWPPK NFRAFSREPV TIAAVLDDAL
VLSSLQKPRK LSIRGSDGKL YAVLAKPKDD LRKDQRLMEF NTMINRFLKR DVEASKRRLY
IRTYAVVPLN EECGLIEWVN NLKTFRDILI RLYKERGINP NYAQIRALLD EASNCAPDKT
AELFESRILT MFPTLFHDWF VETFPDPSAW FAARIRYTRS CAVMSMVGHV LGLGDRHGEN
ILFEEDNGGT LHVDFNCLFD KGLTFEKPEM VPFRLTNNMV DAFGAYGYDG PFRRCCEITL
TLLRGNEDAL MTILETFLYD PTTDFIGGKK KRTHPNVPNT PQEVLEGVRS KTRGMLDGES
VPLSVGGYVE EMIKRATDRN LLARMYIGWC AFF
//
