ID A0A1Y2MBB2_EPING Unreviewed; 2407 AA.
AC A0A1Y2MBB2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=B5807_00347 {ECO:0000313|EMBL:OSS53416.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS53416.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS53416.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS53416.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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 -!- 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 -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; KZ107838; OSS53416.1; -; Genomic_DNA.
DR STRING; 105696.A0A1Y2MBB2; -.
DR InParanoid; A0A1Y2MBB2; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000193240; Unassembled WGS sequence.
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:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
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; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF13513; HEAT_EZ; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 704..736
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1243..1851
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2025..2346
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2375..2407
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2407 AA; 272252 MW; D67452A7986398E0 CRC64;
MAQQSALSSA LDRIVQELRS RHDDIRQKGA HNLRQTVEAA HRELAPAVFT NFYGEVYGKI
SSLVVGGSDS NERIGGIHAL NALIDFRGDD AGTKTTRFAS YLRAVMRGQD TTSMVVAAKA
LGRLAKPGGT LTAELVEAEV KGALEWLQLE RLENRRFAAV LILRELAKNS PTLMYQWIAQ
IFEVIWVALR DPKVLIRESA AEAISACFEI ISPRDSAMRQ LWFGKVYDEI FRGFTIGTNE
AVHGSLLTMK ELLDKSAYFM NEARFKETAE TVLKYREHKD TLVRREVVLI IPRLASYSPT
EFAAKYLHQC MLHLQGLIRK DRDRDKAFVA IGQVANAVGV AISPYLEGIL GFIQEGLTAK
ARNKSVVNEA PIFQCLSMIA AAVGQALTKS VERLLDPIFS CGLSDSLFQA LVDMAHYVPP
SRPMIQEKLL DLLSQILAQR QFLPLGSPYQ VSQPPQIWTR DRQDPAIVQA REAEIALALH
TLGSFDFTGH VLNEFVRDVA IRYVEADNPE IRKRAALTCC QLFVKDPIVH QTSTHATKVV
GDIIEKLLTV GVGDVDWEIR WEVLLALDAR FDRHLGKADN VRTLFLALND EIFVIRQAAM
SIIGRLTAVN PAYVFPSLRK VLLQLLTEVN YANSPRSKEE SAKLISSLVG AADSLIKPLV
DPIVTVLLPK AKDPNPEVAS TTLKAIGDLA SVGGESMVKY IPELMPVILD FMQDMSSDSK
RFSALKALGQ LATNAGYVIE PYRDYPELMN ILMNIVKTEP EGDLRRETVR LMGTLGALDP
DEYQKIMEQS PDQQLIMEAQ AVTDVSLIMQ GITPSNEEYY PTIVISTLMG LLKDSSLMQF
HSAVVDAVMN IYATMGLKCV PFLSQVVPGF LQVIRSTPAG RSEGYFNQLS QLVRIVRQHI
RPYLPSILTC VKEFWGTNPQ LQATILSLIE AIARSLEGEF KVYLADVLPL MLSVLDSDTT
GKRLPSERVL HAFLIFGSSA EEYMHLIIPI MVKMFDKPGQ PQHIRRSAIE TLGRLSKQVN
VSEFAARIIH PLCRVLQGSD PALRQTALET LCALIFQLGP DYIHFVPTVN KILIANKVPH
ENYGRIVSKL QKGEPLPQDL SPDERYGEDD EDLNPAEILT KKLAVNQQHL KAAWEASSKT
TKEDWVEWMR RFSVELLRES PQQALRACTP LGSIYNPLAR SLFNSAFVSC WTELYDQYQE
ELVRSIEAAL TSPNIPPEIL QILLNLAEFM EHDDKALPID VRILGMYAGK CHAFAKALHY
KELEFNAEQN SSAVEALISI NNQLQQTDAA FGILRKAQGY TDVELKETWF EKLQRWDEAL
HSYQRRELEE PDSFEITMGK MRCLHALGEW DLLSSLSKEK WANASQEYRK AIAPLAATAA
WGLGKFADMD SYLSVMKEQS PDRAFFASIL NIHNNRFEIA IEEIAKARKG LDTELSSLLG
ESYQRAYLPM IRVQMLAELE EIMLYKQLGI KENHEKQASM RKTWMKRLKG LQPNPEVWQR
MMKVRQLVIS PDEGTDMWIK YTNLCRKNNR MNLANKALQK LLNIEGVGDQ NVVEYVRENS
HKISHTVAYA TYKYMWADQH TQQEALDSMK DFTSRLSDDL NMRTRAAAHP MMGQNGMNGM
NGMTNGHPQL FNNMNPFAAT NGVNGMSASG TMNGSAMGVS PADLAECHRL LAKCYLKQGD
WHQELQGGEW EHEYVHEILS AYAAATRYNH NWYKAWHAWA LANFEVINSI TSKADRESTD
VPSNMVHDHV VPAIHGFFRS IALSSTSSLQ DTLRLLTLWF SHGGLPEVNR TISDGTKSVP
IDTWLEVIPQ LLARINQPNP TVRQSIHQLL IEVGKAHPQA LVFPLTVSMK SDVSRRQRSA
KELMEAMREH SPRLVEQADL VSHELIRIAV LWHEQWHEGL EEASRLYFGD HNIDGMFTTL
APLHAMLDKG PETLREISFI QSFGRELQEA RDWCNTFRTS GEIGDLNQAW DLYYQVFRKI
ARQLPSLMSL ELQYVSPKLK DAHDLELAVP GTYQVGKPVI RIMSFDPLAS VIQSKQRPRK
LEMQGSDGKP HTHILKGHED IRQDERVMQL FGLCNTLLSN DVESRKRHLN IQRYAAVPLS
TQSGLLGFVP NSDTLHVLIR EYRDSRKILL NIEHRIMLQM APDYDCLTLM QKVEVFGYAL
DNTTGQDLYR VLWLKSKSSE SWLDRRTNYT RSLAVMSMVG YILGLGDRHP SNLMLDRVTG
KIVHIDFGDC FEVAMHREKY PERVPFRLTR MLTYAMEVSN IEGSYRTTCE HVMRVLRDNK
ESVMAVLEAF IHDPLLTWRL GNRGDSPPEP NYPSERRQSI MGDISDMGSL VRNRHRSSIA
PPNEAEAKEV QNARALQVLS RVKEKLTGKD FRPGEELNFQ MQVDRLIKEA TNLENLCQHY
IGWCSFW
//
