ID S3CTB1_OPHP1 Unreviewed; 2117 AA.
AC S3CTB1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=F503_01825 {ECO:0000313|EMBL:EPE03935.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE03935.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE03935.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE03935.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148164; EPE03935.1; -; Genomic_DNA.
DR STRING; 1262450.S3CTB1; -.
DR VEuPathDB; FungiDB:F503_01825; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_1_1; -.
DR OMA; IEYCKKW; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; 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; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000313|EMBL:EPE03935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Transferase {ECO:0000313|EMBL:EPE03935.1}.
FT DOMAIN 1016..1604
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1762..2080
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2085..2117
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2117 AA; 237687 MW; 17EB15536F8DA412 CRC64;
MSLPPHNASL QPDGGEPADA LVVAQHQQDD PFDNRERNSK RRKTEAAAPV TVQVALRTRI
CTKFNIEMGD GLWETTRNMI DTICDRREYN SDESSLLAAM RFLAESLCVF DHTASLADPD
DDGSEIKCTR CKVFNPTAQL SRHREKDREG VSSIFRAFHT IATNFLPPEG PLTVRALVIL
RRMALHANTR DHLDYESSDA CKWCASQLYS TDRAVRIQAA KTIAAYCRER TDGFNETMEK
NRQRFYRGLE LLMNSDDCIT QELSAFTWTQ LGMVVCENQL EPMLCGLLRH LDSEHMPVWN
MAISEIRYLA SWFHRTPNEI FEPYWRTTAH LIVKHVADRP AVATAIANLF GTTAPKLTLR
LQAQAIPELL FRKQLEPISK IAEYRGDGEE VWPTIMDKSN LTSILAYWVQ LPQSVATLDD
LMELLQAFSA RMGPATIREV MGVAAIPVLG ELFIRLTYEV GRIPDHFTSI VDGIGFRPIL
TIAKLLKNEG GKRQTDDEIV IDFLSQHVLG FTTRLSDVRG HDGKKHLCHW INGIEALEIL
IKYLRTEIRV ARPQVTAFLL DALCSDANYA TCWQVGVRRA AISCWAALVQ NVGDESVHTL
VETTFAVIRK NWDQFGDWER TKCRELFAWL LAKPGGQHRE CIIEKIDVLP HLNIPDLQKS
VDSKIDKLRK PLGGMQTIDL FAQRIAHENL DVVWVALEDA IDFLKNNQDV LQAPAQGEKS
DSAVAHFVRA LLDCAAKYNA SEPTLAADCL TCIGLVGCLD ANRLGAVRKD PPFVVIYNFH
ASGESVDFIM YMLEHVLTRA FLSATNSTSQ GMIAYSVQNL LMKCGISNAV RSQGREMKEI
YEKWKAFPEL VQVVLSPLLV SRYHIALPGP MQIRYPIFRP GRTYADWLKI LVADLLAKTQ
NAYGEILYES LARAVKGQDL AVAEFLLPYM VVYVVTGTRS SAKDREQITL ELQRIAEYQP
PDEAPAVEKE QAKLFYDAVF RVIEYAFVWL RSCLHYDKPI GVPHLETFIE AFPAEALSQK
ALYCRDYARA MFFLEPVAMA SVPDDAADDI ARRDKAESDM IDIYAKIDDP DCLSGIMSKV
GSFVEMTPYR KALLEQKAGR WESATTWHLS DLSAEPDNVD IQARVIKCFL EAGHHDALLA
RVDNMNLGEA PATTINKVLP LALEASWATL QWTKLDSLVP IYKGDVTDIF NVGIASALSQ
LQKNNMDDFN NTLTTIVNRV ASSMSYSTTS SLQACHEAML RAHVITDLRL ITSVTTASDT
EAMERRSSDH SPKKTRTALA TLIQRLDLLQ DVSDKRYLLA LQRAAMESLR PVYGDREISA
LWLLDARLAR KTGYNGECLK AIAHARQLGD PAAEVENAKR QWAWGGKHQA IADLRLAISK
GLPGGDNGPG GDDSYAKRWS IQEAAPLAAR ARLLLTRWLD ASGETSRSAI RDDYRDLTSK
YSEWEKSFFF LGRHYKKWLE SEEALKPDEQ SDLYLTGDLA RFEIETYLRA ARLGTKYLHM
TLPRFLTVWL SLGSQIDTAP EGKLDLSDEL RKRRYEVLAS LHRRLLRQVA RLPPFIFYTT
LPQLVARINH PHADVCRVLD EIISKVVQAY PQQALWSVFG VMTVRKNNQT KKAAERLIMA
ICKHSGQQPV VVGTKLPSLQ TMLRRGVSFA DDLVKVGRRG NYRAHNTSKA VSLQRDMNFN
PREGIPPLVV PIARCLTAAM PSRLSPRAAH TAGAASASST AGVSSLGGTA AGGAGSSTDS
ASMMAFAAHN AFASDVITIH AFQDEVLILG SLAQPRKLTI RGSDGRLYDI LLKPKDDMRT
DQRIMEVNAQ VNQALRKDTE ATRRELSIRT YAVTPLNEDC GIIEWVLGLK TLREILRPYY
DIRRSKVQPR PPDPMEIQKM LTEAAHTRGR QHQIFTQTVL PAYPPVLQEW FMRRFPYPAV
WFTARLRFTR SVAVMSMTGA VLGLGDRHCE NVLVDQDSGG VMHVDFNCLF EKGRLFTQPE
TVPFRLTQNM RAAMGIYDHR GPFRRSCELT LQMMREQEET LLAVLEAFIH DPTLDLQAEA
RGAGQQHLPG GAARVKPAPV VKLDPQSVVK NIKRRINGLL FEETIPLGVE GQAWELIKQA
TDPANLAAMY IGWAPHW
//
