ID A0A3E2GXW0_SCYLI Unreviewed; 2299 AA.
AC A0A3E2GXW0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=B7463_g10366 {ECO:0000313|EMBL:RFU25966.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU25966.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU25966.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU25966.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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:RFU25966.1}.
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DR EMBL; NCSJ02000293; RFU25966.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2GXW0; -.
DR OMA; SMYIGWC; -.
DR Proteomes; UP000258309; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 1268..1841
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1955..2262
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2267..2299
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU25966.1"
FT NON_TER 2299
FT /evidence="ECO:0000313|EMBL:RFU25966.1"
SQ SEQUENCE 2299 AA; 259674 MW; DB8936B5B7257F8F CRC64;
MAPNSRGAGV KDHENGATGP YAPPPSTSAV QLINNLSTVT KPIRQVEQDD LQKLMSEVSS
LENGIAEFKN SEAKIEHQHK LIYVFTLAVL DRLSKDDPFM DVDQLTLQAS EALEIFISII
KETPSILSYI VKPDSRLHSR GQEPFWIWLF PRVLTLLGRR CCDSLTDKIT SFFVGCFKAV
SRIHKLWGLT VSFFCYLKEC ANTILSQVQD YAGGIHHNRV EFVLPSDTGD ESLFSYQKGE
SNLSPLRCRT VSLYLIPTII AKVEADETQK SLDHDFQKAA VVLLNVCKVP VPKSFSEIPD
ASTKFERTVL DTEFRSLNIV SFQDVNHSDE PAPPPPKRRK ITNDPDLCDQ LVEDLFQLLK
PHGIANLNSL SEAIDISYAQ LDPDMRCEVI NRLGRLACAG AGSLTIERDR DRAIVNRRCS
ICDNMSQIAL HSDPSTKKIH EEALPALAKL IKLPTFVDSR KPRVLAMLAL KRFALHVKIR
DFIDLEISPL GQWCLQSLKS SVRELRIAAG VSGDEELNIV LLKLVEYLGH TNPVISGVAF
DEILKLANTK GITVERLLSP YWASIAIVAV RDLLTRPQAS QMIADLLEIT VPGFLVLTQS
YTLPWLVLAK KTDIINSICK AQQQDDPWNV CCRDSSNLVP ILSLLLVQNV PDIEKFICSQ
LRSVSPRFNE LRFTELMRFE PSPLGLYLLK ASADADDSKK SRIRIALQIL ATHACSLSKD
DIDNSKKKNL IGSFLEQHIL GYVAQLSEIV NDVRDEQSIS EKKRCVKAVE EMVRTSKTRA
RIARPQICAC LQSALDQKEL QSSAYSAWHA MLMSLEDDDV EMMLESTFSI IIQRWEAFDR
ATQHRAKDSL SYLLKSRSEL LRRAIVNLPS LSQFPELAEI EAQLSKLRMP TDTREAFQIF
SQRISHENSG VVAQAMSELK TYLRVQQSFL QASAVSDQPD QVVGQLIRSI LDSCVKFNES
HHDIAMLSAE CVGLIGCLDS HRVESVREQR QMVVVSNFHD PLETTDFVLF ILEEVIVKVF
LSATDTGMQG FLSYVMQELL EKCDFTQHCG HVMMTGDHNY DNEIYRKWLK LPENVRATLT
PFLTSKYAVR EMAITTAEYP IFRPDRFRSD KIYNSWLKSF VLDLLQKPLN TNTAFIFPPL
CRAIRIKDVS IASFLLPYVV LHVVVEGTDE QRREVGGELL AVLEHQPISD SNIRKEDLKL
CSEAVFRVLD YLSRWKQELL DDFAKSRNEK ESKSGQPRNS GLSSFVSNKM NEILDRVDSV
LDMIPAEIVS NRAVECKSYA RALFYWEQYI RTVKDNASHN AIPVNLLERL QEIYTQIDEP
DGIEGISAHL PVLNIEQQVL GHRKAGRWSA AQSWYEIKLA QEPEDFEAQL NLLTCMKESG
QHDVLLNYIE GLQTATTTIP KILPYATEAS WATEKWSALE KYVSLSRKIP GEDFNVNIGR
ALLELRNGDI TSFMSTIQAT REQIACSLSS SMTSSLGSFH EPMLRFHILT ELEMISGANK
SEDISVQQVL ESLDRRLEVL GAYRNDKQYV LGIRRAAMRL SSLDFKSEDI ASAWLTTAKI
ARKDNAINQS FNAVLHASQL GDRSATIEHA RLLWMEGQHR NAIQSLQGAI NNDAFISHNV
NIKITTLIND EEAEQQQNLL TARAHLLLAK WQDSAGQTHS NAVRSQYQLA ASKHRAWEKG
HYYLGRHYNK LLESEKTLAP EQQAEVYLTG EMARLVIENY LRALLYGTKY IYQTLPRIIT
LWLDLGTQVN KPLDPKYGVG KEFVAKITNL RKEQLSMIHT RFTKYISRMP AYIFYTALPQ
IVARIAHPNI EVYNYLQQII YKVVSAHPQH ALWALLAVST STQPERKHRG TLLLNALRNN
SKKNGASDFD LKLMVKVGER LTAELLMVCT AGDFPGNRNV KASISKDLKF NHKVCTPSLL
AVPIESVLAA TLPTLTDNVN THKAFSREVI TITGFQDEVL VLGSLQRPRK ITARGSDGKD
YGLLCKPKDD LRKDQRLMEF NGMINRLLKK DAESSRRKLY IKTYSVTPLN EECGLIEWVD
GLKTLRDILL SLYRPMGISP NYREIEVFCE EACKAPDKLP FFTEKVLSQF PPVFHLWFVQ
QFPEPSAWFA ARLRYTRSCA VMSMVGTILG LGDRHGENIL FEEGNGGTFH VDFNCLFDKG
LTFQKPERVP FRLTHNMVDA MGAYGYEGPF RKSSELTLNL LRQNGETLMT ILDAFVHDPT
LDLIARKDKK RKDPVVGVNG VVVPTTAQGV LDSIQRKVKG LLPGESVPLS VEGQVDELIK
QATNAKFLAS MYIGWCPFF
//
