ID L2G222_COLFN Unreviewed; 2883 AA.
AC L2G222;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Serine/threonine-protein kinase Tel1 {ECO:0000256|ARBA:ARBA00014619, ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|RuleBase:RU365027};
GN ORFNames=CGGC5_7832 {ECO:0000313|EMBL:ELA32058.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA32058.1};
RN [1] {ECO:0000313|EMBL:ELA32058.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA32058.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) 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 ECO:0000256|RuleBase:RU365027}.
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 ECO:0000256|RuleBase:RU365027};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB020723; ELA32058.1; -; Genomic_DNA.
DR RefSeq; XP_007278865.1; XM_007278803.1.
DR STRING; 1213859.L2G222; -.
DR EnsemblFungi; ELA32058; ELA32058; CGGC5_7832.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OrthoDB; 8448at2759; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
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; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR37079:SF6; -; 1.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 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; 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, ECO:0000256|RuleBase:RU365027};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365027}; Chromosome {ECO:0000256|RuleBase:RU365027};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027}; Telomere {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1856..2428
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2533..2843
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2851..2883
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 184..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2883 AA; 321690 MW; E657A45959CBF8DF CRC64;
MAPPKLKTGE ITVNDALNAI SGGTLKERGT GLDDLIFLLD KKGKTAALTD LGDKHYHRIF
EGLFRCAIAE KQNFYGGKRT TAAAAGSRLS KCAEALRLAV AHGASKLKRK TLIAVIDHIT
QTLPGPGEDA DFVEPLLKDY VRSLAALLGH QPNSEHLAIL DADGWLACVD FCIDTVSRYL
ENADRDSVSR ASPAPGTASM GFSTGRSTNP SQRVTGQIHR GTVQDLLHCM YLLVIPPNAP
LWRRTKDLSK TLIQILHVRH VGLGQITQLA FASINVLLAA TRTDDLSRAS SLARDLVPLV
SHWWQGRTVS QDEMLNSVRD EMLKTIFLTH LHLECLVFQE DDHVLKDIED LIDALWQEYS
RRDLRSQLQL EDLTFVTHRL PQDYFTIELF GLRPHNRDGE RRWALVQNLA ILERILWKAR
KQQRSQSPDE QPRKKRKTHT SRIQEYLQSH NSATQRTALQ LVPFLLNLGT YTTTEIAELL
PNVIAFISDK DATIASWAML ACTSCTQTDC VDSTVWKHIW QIAARAISLP GTSRAACVFL
HTVLEAKTEL LSYHDVSDEV NSIVTTADVN GPVLLVDSSI TLMLHLLFLR NVKLPNASQA
TCHHIIRWIF LKWNPTEMSY AALYSLHAPV TELVNLIRAC CGSALLHHTS QEAVSGGSIC
QTWRVQYHAS VLTRYLLLLE EPKPQTREAT SCGQAVASVE LIKAGDSAAF HASKKLVLEL
LFPKIESLQD LCESWSKKGS EGGTQISSDR FHSLFSAVVA GTMLVSQLTD LNSGQSRDIE
STVAKLTSTS LEAATASDDS QQFFEILFKI MRPILPSLET ESINAILKDD PPLLKLITKI
AEAYRDQSSR QSSGQNQDFM DLDDEFDSQE SKASIATKPA DVPRLNTSLS LDLGAFYLAT
EQRMYFFEAM HNDSGQVGLV PHDFLEQLLD LSDEGFLMCA ALTSEIFGSD LNIGPDVAEQ
VVEKIGYIIG EAEYNCCEVA HSTTLRILEG LMQIWVDEKL EVSKMVGDLY DHLVGSMSKN
SLSPNSQIAL ASLLLALLRN ETQYADKLGS ASCRTTLLSI MKQGTLAVKH FIGVALPDIF
GVYVLKMHDE LFVDVLNSLP TDPEAIEGIA FRLFVLSQLA CRWPTLLRRS TYHIFETPGK
IAQSAKYAKR CLDNVSTALQ LTSSKELFQI FSPQLLYTWL ELDAMDDIPF EIFGFASLNA
LLQEAQAETA ALEIMRGRYD SVRTLSERLG MPLAEMVKQS FTKIMAYTIA HETSISASET
QNDGSENWVK KLLGGEQFLD QIYLNFVDIV ALLFDIFDQE DPIEKQLSRD KNFQYASINM
EEMKTFAMSP TNLPANQQPM FRSKFLLREL FHLCSQTEYE LQTLWTPALV IAVTRKLLNT
IHPALGSLHA CSVLRKVRVV IALAGPVALE AYPLEMLLSS IRPFIVDSEC ADDTLGISRY
LLSKGHGHLL NTPSFLAGYA LSTLASLRVF LESSQSSTTQ ESQFKATMSK AQQFHSWFST
YLAGYESPIL ADEEQRQAFR SITQSASKIR SSGNAEKGTS ESILLLEILK DGERDQKLLN
EAARDLALGM LCGDFVVPST GHQDVIENDD EALQNSALVW KSCNALDLSD EYLAWAGRVV
GRSFAASGEI QPELLEESEL SRYNRLAPGS NNSEQGLLSL LQQLTQSKHT DISGLAESAL
RTIVSEADAQ GDDALLVASQ TTLTEPLFVA SAWGPYRTPP TDFIASQNIP DSQVFFRDHV
ESPDWIQELA VHLAQSVPEY IILAALVPIL KNVKGFAQDS FPFIVHLALY SQLDKQHVIK
RNLSEATKEW LKIQDESART NQKHLINTVL YLRTQQLPKE TSIADRAMWL DVDFTSAAAA
ASRCGMYKTA LLFTEVAASQ ATRSSRRSSA VRDEDSTDVL LSIFENIDDP DAYYGLPQPS
DLSSVLSRLE YEKDGSKLLA FRGAQYDSHI QRGDHASQSD SQSLVRALGT LGLAGLAYSM
QQAQENHDAD EDSLASTFQT ARRLERWNLP APASVDNCSV TIYKAYQNIQ QAADTEHLGA
LAALTELDDV INVSDFSELE GMLEKFEQRG QWMRRGRYED VSHMLSCRET TLSLMSQQSK
LRNTSLSTAE ARQIEIRSKL MSSGIYRFHQ ATQESLNVST SLTSLIVPCE NLGLKVDAAV
KIEAANSLWD HGEMIHSIRM LQGIDNDSSL KKQTIPVSRS DLLSKIGHQV SVARLEKPHH
IQKNYLEPAL KELKGKSEGQ QAGRVYHQFA MFCDEQLQNQ DGLEDLARLQ SLRQGKSDEV
AQLQSLIAST RDSQLKTRYQ SHLNRAKQWL SLDEQELRRV ETTRSEFVRL SLENYLLSLI
ASDEYNNDAL RFTALWLERS DEDATNEAVQ KHLGKVPTRK FATLMNQLSS RLQNESNSFQ
KLLTTLVYNI CVDHPYHGMY QIWSGSKVKP RKEDHVAQLR IRAAEKLAGL LQSKQAVAAI
WQAIDRTSSY YHRLAVDRDN SKFKAGHKIA LKEIHSAQSL VNALIKYHIP PPTMQLEVAA
DKDYSNVPTI ASLDPQMSIA SGVSAPKIIT AIGTDGQKYR QLVKGGNDDL RQDAIMEQVF
AAVSSLLKLH RSTRQRNLGI RTYKVLPLTS ASGLIEFVPN TIPLHEFLMP AHERYFPKDL
KGSQCRKEIS NAQGKSTDMR INTYRKVTER FHPVMKYFFM ENFEDPDEWF VRRLAYTRTT
AAISMLGHVL GLGDRHGHNI LLDHKTGEVV HIDLGVAFEM GRVLPVPELV PFRLTRDIVD
GMGITGTEGV FRRCCEFTLH AMREETYSIM TILDVLRYDP LYSWSISPVR LAKLQGGGQD
DADDDVAGKK QVNEPGEAHR ALEVVRKKLS KTLSVTATVN DLINQATDIS NLAVLYSGWA
AYA
//
