ID A0A139IGW2_9PEZI Unreviewed; 2949 AA.
AC A0A139IGW2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=AC579_10022 {ECO:0000313|EMBL:KXT14037.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT14037.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT14037.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT14037.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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-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 -!- 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:KXT14037.1}.
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; LFZO01000096; KXT14037.1; -; Genomic_DNA.
DR STRING; 113226.A0A139IGW2; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
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; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000073492};
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 1877..2483
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2590..2906
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2917..2949
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 418..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2320..2347
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 424..439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2949 AA; 328178 MW; A470057270E04AEF CRC64;
MAASVSLRDA LEGIQSATVK ARSDGIRDLK HILDYNRNSS RISELRDGEY NTILETLYRC
ADKEKQNAIN GKTQTARTSA SNKLADISNA VRHTVEASVQ LLKPKTVAAL LSHIEHTILL
RNTEFCMPVA LDYVKSMRAV FECQPHVVSL QEDGSGEDCR WDALALFCMH CIGKIEQEQP
SDAEPLSTPG TGTMNAFTIR SERSVIKESA GSQARRPSLR PIAEEMVACI RFLTAVPTVP
LKRKAEPLLC TIIEALQKST VSHKSWAHAF AAINNIVCWS RTEDTNCTKK FVSHIVKLIR
HLWRSNVTKD ATCQMLVTVL LLEPYILLCM QQSAGLTLRP ELVGLLHVLQ TDYNKRKERE
QLRLDDLRLE INLTNVPDGK VASLFLTLRC SGLQAESNWL VAHIMAFLHR AILPPSPTSE
ELEQASEREE EEEEEEEEVD ISQRPRKRQR TEDDFTKLVS AITFGTQQER TCALQTVAFL
APRMRFSFIQ LRRLLDSAAV SCSDENGVIS SWAFIACAYC ASQKSAADRQ LSARFDSIWQ
LALRAISNPS SSRAASFSLF VLFRLRRVSS QHVTELLQIN ESMDLNGPSQ MSDGAIWLLN
VVLEASQELS PAAGTRAADA AAAWLARCFT PSRLEDKHYT GACNSYDSSD VLSLIKSCLG
STAHQSPATG MPVWDVGARG WLLCQGGDEL MRYLLLTDEE GSALDDKRLS SGVDASRTLK
QLTRPSVETL LMSHLFSEVS RTVDTFTGLV RSRQVTMDSF NTLCKSCVTF MCASTCVTFK
DSRKLEQFHQ STKKLLGHVQ DFVATPSTDQ DKVDIFLSVF TSTFPCLRGV GQQSNRSERP
GCQMMACAAI KEAITRRQSA DVVNGDDDFM DLDEAFDSQD SRPAQNSSPQ EIPYSDLDAA
YSLSTLRSSS MLYATAAIAV QTYHASTPTA GLASTSITDF ILELPVDAML SCRDVISSLP
SLGLVLGASD TARLMTLYLD LLAKSTYKAS EVAIGSLLDV MLSLVDVWTD PHHRDAHNLG
LDAYEWLITV AVPKELVSPN VVKRLMNLLI QLFKIDAEYG LNTDANTPRL VLFELLKTAP
VTAQFELTGR LPEIFALYVL SQHETIFDDL LHDLMQNQDW FEGTVIRLRF FAKLGSTWPS
LLRRCVWLLF DSAGNIKDAS AHAKVCINQL ASALPLRQPR ALFTLFAPQL LWSWTSGHLR
LEDLPFAAFE YDSVHDLLRA NESEALAQIT LQGNEKAMDV VTRAVKMMSR DAVKRSYAKC
LAYCMAYDVS SPKEPGAKSN PSEERLREAI GGKVEHQKLL IRHFPCIVGH FCLLMKTDDV
GDTWLAKRDS YADMAKALKE MKVYSHSERS LPETQDPCVS DRYLLDELER LYKRTQLQIT
DLWSPSSFSL TARMLVNEID ESLGSLHTCL IVRRLRIFIA MSGELATDGF GLEMLIHSLR
PFVSDSECAD DTLGVLYYLF NRGRSYLRSC LPFATGAIIS LVLQMRQHAQ TAHDRTTQES
QHTATIDKMV NFQNWLVDCL TALTREEPST GYKQLLASLR GIQLPGNGRS DSPESNLLLF
LLEQWQSSKP LCSRHDILEA LTLLAENFVC PDSLSEDCLG LDKSTVHYVQ PLWEVLNISA
LSDNFVAWAG EAIGRAYGCT GTRPEESKGQ GPSILKELPS DMVGTLTASN STIVKHICQT
MYSRKRSEAG LAEFTLRKIQ ESFASAGDSD EAVEFSQLLP DAICAAICDG TFGWNPMPSQ
LEPDAADAES LRQALQAPTN GSIDQWTSRL AKVISAWSAN NAIVSSLAPL VQNLKGLARQ
LLPSMIHICL HNEFNAVPSL RQILSEVIGV CMPDGSEAQR PKQKFFLEIL LYLRSQELPG
EATKADRLNW LDVDFVVAAG AASRCRMPAC ALLFAESAAP VAVPQSGRRS TSRASTSHMQ
PAPIPEELQI AIYQQMDEPD SFYGVPQPAT IDSVLHRLDH EQDGFRSLMF RSAQMDSHMR
HLHRLPERDA VGMIQSLSAL NFNSLAFAMV TQGLGDLASC AAPMLNAAQT LQQWDISVPD
SPSEASLTFS VHQELSRADD LELIRDKVRN AVLQHVTNRP QAGDSPTHAW CSALASLTEI
GEVISSSSEA EMASRWSVMQ SRQAWMQMAR FQEVKPFLSN RQTLFGVIRQ NAFLQKGLHL
TERRCRALEV EALLASSGLA REHSQLQDAL TATATLSDMI EHCGAVHLKV AGAVKLEAAT
VLSEAGETTI SVRMLRDILG MSDLDSQDLQ VGRAGLLAQL GHQMAQARLE KPEDILERYL
TPAVNELYEQ PDQRQAGKVY HELATFCDKE LQNPGNIENL NRITKLRQAK EEEIEAYNQA
IQAAKRNGGD RNQLGRSLGQ AKTWLAIDRS EEQRLQGIKQ QLVSLSLQNY LRALANSDSY
DLSVLRFFAM WLENTGDVEA DNAVARYLPR VPSWKFVRLM NQLMTKLEDG VSSFQRALGA
LMLRIFKEHP YHSINHLFAA CQKPKGTNID SASQARHSIA MQIQKDLQSP QNGKLGELVR
NIFRANLRYK NLADRAPDQS QQGLKLPVSK VPEAGGIVNS GTIRKLPPIT LTIPLRRSGD
YDDVPKVERF GGDVSIMGGL SAPKMLKLWD STGQEHKQLF KSGKDDLRQD AIMEQVFEEV
SNMLRNHKAT RQRDLKVRTY KVITLAKTSG VIEFVPNSIP LNDFLRPAHK KYHPADMNDG
QARAQISNAW AQGEGSQGDR IKAFQKVCSK MHPVMRHFFF ERFTDPDEWF QKRTAYTRTT
ASVSILGHII GLGDRHCSNI LLDEKTGEVV HIDLGVAFEA GRVLTIPELI PFRLTRDIVD
GMGVTKTEGV FRRCCEFTLD AVREDKESIM TLLNVLRYDP LVEWSVSPLR AKRMQEESNR
INNGMIGGDA ENSSKKREHS AGEADRALAI VEKKLAKTMS TTATVNELIQ QASDEKNLAL
LFQGWAAFF
//
