ID B6Q603_TALMQ Unreviewed; 2902 AA.
AC B6Q603;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=PMAA_033490 {ECO:0000313|EMBL:EEA28542.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28542.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995899; EEA28542.1; -; Genomic_DNA.
DR RefSeq; XP_002145057.1; XM_002145021.1.
DR STRING; 441960.B6Q603; -.
DR VEuPathDB; FungiDB:PMAA_033490; -.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OrthoDB; 8448at2759; -.
DR PhylomeDB; B6Q603; -.
DR Proteomes; UP000001294; 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:UP000001294};
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 1842..2439
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2543..2855
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2870..2902
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2832..2858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2271..2305
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2902 AA; 326939 MW; 6C8782B8EB09CC2F CRC64;
MADPSLSETV ARLSSDKQKD RTDALNDLRR ILNKKRQNLS ETLNDKAYHR IYEALFRCVA
IEKSAYSRLN KSSARNASAP RLPLCASAFR ATVEVSVAVL RTKTVHAIID HIVQTLTQPG
DGLWNLLGID YIKGLRLLLE YPAHVEHLTE SDWVDVTSFC LSCLSSNGDE ATQLSIRTSY
RSLSQGLVDE EGGQRTPSRT TSGRDALSSS SQVNRSIADE AVICIQLLTA TPAAPLQERV
RPLMSELLVY LSSAMPANAN QALKAINNLL ERVICDQCAL VKDFIPDIIP IIRRVWLTKS
SAVKDEALVT MLLCMDLLRS NPQSLFSQAS LQPLEDLLET LENEYTKRPE KEQIQIDDLV
FYQNDISFQH LYLFGPRLGS SRSEHNWTLI WTISSLIGIL DKASDHMSNS AENELGPNKR
PRLSSRTDDV SRECVTSTGP RKGYCLQLLS FLVGRMSVED KASRLSRLAA GIVDDNPSTS
NWTLLAICNI AVSDSSKSPL LKPYWRQIWD LAFRASAFQV NTRAACALME IILRLELVES
TDLTDNIRSM LSSMDLNGPS ALCDTSLRLL TTLFDKRLHT AAGLGVDSVK SICNWLRSSW
TFGAGVDKLQ MAQVALFASP ANFLGLLLTL TNRPAPLRHA EYQGTTATIS STWFRHREKS
SLKEYLFSFD SEIPQDLWCV EETFPSVESS IRNDPNDHVV LELLQTKVDT FSQAWKIMSE
EKSQHITADV FKIMVSACIV VALFIESLPQ PDNNRAADLR RTNLGFWTDI CDYIASRDDL
TQGCLSILSP VVASAPCIPN NAIPISRALF GLASPLVVNL KSRESTQNGD FLNDPDAMDF
DGIPSPPQGE LARDMILRNN RHNVNAFPEI NTFQRCLSTR LYIFLSGNEA SGADPSTQSS
LVNSLKALDD VDVLSTRNFL PHLFQQSDRF SRNDILDIVE HFGEICLQRY QLERCESAQC
FSISMMKCFV DSWTSNEDDD LSVSAADLYG WFIQVFLNKK KGSSGVLIAL SRLLEQIINL
NPTFSVDGSG PSPRTSLFSI LRDGDTVVKF AIASCITNIF SRFLLKDHEK IFDDVVESLP
TDPDWNEGIA LRLYILGQLA SRWPTLLRRS IYHIFETPAQ VPESTRYAEK CLLEVSCSLR
LQEPKDIFRL FMPQILYTWT ETQSIISMPF SIFRYSSLQA MLQDAQDELV GQIMMRASDQ
DANEIATYLG KPFNELLRES FYKAEAYTVA RDISLPPSQD SQPKGVESRV KKTLGTDQFA
QSIENKFPEV VSALFRSLSQ EEQIERAFAK RPKFRYASKI LNRITEKSSS TTILPGNQQP
SFRARYLLDQ LEYLCKRAGY DLETMWTPAL VSFVCRTLLD SMDPALGSLH ACAVLRKIRI
LVCISGSVIC QDYPLEQLLY ALRPYLTEFH CSEDALGLFW YLLEEGKSYL THQPGFFAGI
AVSTLVSLRN FLQSSPESTT QESQFNAVIS KSQEFRQWFG EFLEDYCPSD LDQSAKDSFH
RMVTSSKQIN NTGNSEKGTH ESELLLQLLQ DRISRNSILS KSVSDLILSL LCVDFQISSD
IFNDILGDDD ASSKHNVAVW QSIHSGVTDK GYRLWAARVL GRAFAATGQV SEELLREQNL
ETIPSQSQDL KHTEPFLVSK AAILQVLCEA LSNSDRANVG LVEQTLQLIM SKIARFPNLE
QCENIIPRPL MKALIWEPYY CPEIRARIPE TKIDNIWPTL NPESPITSTQ WARDLALALA
TSAEGDPVIG PLKDVLYVIP DLSVRLLQFV LHDVLILESE KDQACREMVS KIFNDILRST
TEATVAHAQI ALNAILYLRQ QQRPQESTIV ERDEWLDIDY GLAASAAVIC RMYKTALLFI
EIQASRSIST SRRSSIKYLP PTDLLHDIYR RVGDPDLFYG IQQDATLNSV LEKLDYESVG
FKNLIFQSAQ YDSDLRLGGK GNTHGLFKAL NATNLHGVAN AMLSVPNNSE GASIDSEHLL
STAISLQQWD IPALPSQGSA MTVLFKAFQN LNTVDTMKDV LKFNDNCFLD ILDQSQDKNR
SVTALRDSMR ALGLLTEIDD VLRSTTSAQV EDLWSRITSR TSWFQAENFE DIAQILFSRG
SFFSSINKKP YLKSALKLTS RASQLLEVKA LRESFKISRE LEGSQEALTS AISLSKLVQP
CTALGLSIEN AAKYDMANVL WDQGEMTTSI RMLQQLNERG DLQKQALVVS RAEVLASLGH
HVAEARLEKP DAIVQEYLVP AVKELRGNVE SEEAGGVFHR FALFCDQQLL NQDSLEDFQR
IEQLRDRKEQ EVLALKQMMS AAEGKEKNQL TMHYTKAKGW FDLDDREYQR LNNSREAFLQ
QCLENYLLSL KACDNYKNDA LRFCALWLDK SDDPNANESV GRYLSQVPSR KFAPLINQLS
SRLLDESGSF QPLLSALVFR ICVDHPFHGM YQIFAHSKTR GNRDQAALSR FQAATKVVDK
LMIDKHASST WMSLHNNNIC YVRFATEKLD DKIKSGAKVP LRKSPTGLKL EQDVSNQKLP
PHSMRIELRV DCNYSDVPKV VKFQPEFTVA SGISAPKIVT VIASNGLRYK MLVKGGNDDL
RQDAIMEQVF EQVSNVLRDH RSTRQRNLHI RTYKVLPLTS NAGIIEFVQN TIPLHDYLMP
AHQKYYPKDM KPSACRKHIS DVQTRTLDQR VRIYRQVTDH FHPVMRFFFM EKFDNPDDWF
SKRLAYTRST AAISILGHVL GLGDRHGHNI LLDEKTGEVV HIDLGVAFEQ GRVLPVPEVV
PFRLTRDLVD GMGITKTEGV FRRCCEFTLE ALRRESYSIM TILDVLRYDP LYMWTVSPLR
MRRMQDEQDV EEPPAVLASG AERTKVNNRN PKEPSEADRA LTVVAKKLSK TLSVTATVNE
LIQQATDERN LAVLYCGWAA YA
//
