ID C5FQW6_ARTOC Unreviewed; 2889 AA.
AC C5FQW6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=MCYG_05088 {ECO:0000313|EMBL:EEQ32269.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ32269.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 ---------------------------------------------------------------------------
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; DS995705; EEQ32269.1; -; Genomic_DNA.
DR RefSeq; XP_002845219.1; XM_002845173.1.
DR STRING; 554155.C5FQW6; -.
DR GeneID; 9230975; -.
DR VEuPathDB; FungiDB:MCYG_05088; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OMA; HACSVIR; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002035; 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; 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; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 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 Reference proteome {ECO:0000313|Proteomes:UP000002035};
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 1839..2420
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2523..2835
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2843..2884
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 177..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2889 AA; 325414 MW; 7E54CF4E1B0B6225 CRC64;
MGEVNIDQAI NLISSGRLKD RTDGLEDLKH ILLQNRRSPR LASLNDKVYH SIFETLFRFI
AIEKSSLSKA SRVVSKTQAA NRLAKCAGVI RTAAEVSLRQ LRTKTVIALV NHVIDSLTVP
GEGLWESLST DYIKTLRVIL QYPPHVEHLS KDIWCDLLDF CLQGIGLVKD GNPLQMSIRS
GRSVPPEELS QSNRSSPNPT TTSSHPPMKH DSRGSSEDFE ICIQLLVSCS GMPILGAAPK
LFHNLTKYLS SLNPVGSVPH AAFNALNTAL SIVIIENVTL AQDILCDLIP TIRRYWATKS
VMLKEEMLAT LVIGKEVLCR RGQVLRPELD IEIFQNILDR LHLEYIRLPE REILQTDDLN
FSLHPVSSQA GIQFISPNLR APKAIQNWTI LSLIATFSRF VDEYHSREKR KLEAEVILNK
KQHLLSRTDD IFRDASRAAG MSRICALQLI PFIVSEAEPE LGTISILLEQ LIKNILDDNI
VVASWSIVAI ASITSCENAK SDKLKGRWLQ AWELNVRHIS SPAISRVVCH FMSVSMHSKL
LHYSDIAHTL DSLVSSADLN GPASLNDSAL CLWVNVLELW SQVNATQSQG LTKQACGWLR
NKWVLVPTDR TQTSHMAAFA RPLPLLNLLM SCSGISVPTL DLPFIGPMNR ISRIWVSLQQ
NSKIINYLLL TESNKSSLLD IRETVSVYAA PRHHPSETLI LDLLQNKLDA FYQVWTALCT
DKGHHVTMEI IQILTSICVV SNILTEFIQS RTLRCQNIQE SVGKLWEGLC DKFCRDEEHL
NACLEVLAPL ALSLKAPFDP NNVILRGLVK MAGLLVPILE RYRLSDEMNS QASDVMDLDT
DFSLQRPSTA ETCVISNTYR GDNGIPLFPD TSSVRIATSI QLAIIHKIRL DEEPCLLLDD
IVTGYITTLT ETDILVGWRY IIGILKGKPD ISRINACRII EHFGEKCLES YELEGCEAAI
CACISLVGCF VDLWTANERD DLFESASELY TWFTGVLLGE GLGSSKILIR LADLSAAILR
VNPSYLKDTR QVSPRMTFFR ILHDGDLVVK FHISNLIPDI FSRFVLKEHD AILDDVIDRL
PQDSTWTEGI ALRLYLFAQL ASRWHTLLRQ GIYRIFETSG NVPASIPHAK ACLQDVSKAL
GLNGPKEVFQ LFTPQILYTW MDKESVTDIP FAVFGYPTLR ELLLDIQDEV IGQTAMRVKE
DDKNAIASCL EKSFEDLLCE SFYKAEAYSV ARDISLPPSQ EVGAKGAERG MINLLGKEKF
FQLSEKFFPQ TVATLFGSID QTEQIQRAFE KRPSFNHALK TWQNIHERSH STSVLPLSQQ
PCFRARYLLD EIEFLCKRSG FDIDTMWTPS LVCFVARTLL DSTHPALGSL HTCAVIRKLK
ILICVAGQIL LYDYPLEMLL HGLRPFLTDF HCAEDAIGLV WYLIEHGKAY LTDNPSFTAG
LAVSTLASLR EFLSAPQEST TRRAQFKATL SKAHEFHVWF SEFLDTYNPS TEYSALDELS
TKSLRTIIHA SQNIQLLGNG IKGTYESELI LELLRDKISG RNLLTTHTSN LVLSQLCHNF
QRPDTFRDDI LGEDDVAASH AMTLWTSVEN QTQGKGFRLW VARALGRAYA STGVVSPSFR
KEQRSEFLNY SRDGFLAGSK ISILRILCDS LSNSSGPVGL AERTLQVILN NLAGEPRSDE
CIQIIPPTLL KALIWEPYQC PKLTFSASTT ASFLTLPHWD VATTASDFAQ HLALFLCHQV
TKDAVIGALS KIVFTAPSFA VQLLPYILHD VLLSEIDGNQ KTRNEVSTLF KGVLQSKDDF
ILPHVRLIIT CILYLRHQPL PRETTMSERD GWLDIDFMLA ATAATRCRMY KTSLLFLEIY
HSQIAKASRR SSAAMMTEPT DLLHCIFSNI DDPDSFYGIQ QNQSLDSVLK KLEHESSGLK
NLFFQSANFD TDLRLGRGID DRGGIEMIKA LNYTNLQGLS SAMFRSSMPT RSGNEAFDYM
LSTNIYLQQW DIPVPTTTSP TGTLFKSLQA LNSLEDKTQI IESLDDCFLE IIDRLNQENQ
SLSSLKTSMT TLGILTEIDE IVASNDASHI REAWHRLIRR NTWLKSESRQ PHLKKMTNLN
SKDARLLEAK CIRESLKISR EHEISQASLQ CAMSLSKLVQ PSAELGVRID AAAAFDLANV
LWDQGEMKTS IQILQGLSSQ KDLHSQAIPV SVAEILASLG HHIAEARLEQ PDAIIQSYLA
PSIKELKGEY HGAEAGLVFH QFAAFCDQQL QNPDMLEDFV RLEHLRSRKL KEVTDLEDMM
KTSEGKAKDQ LRVYRTKAKQ WFDLDDREYQ RLKKSREVFL YQCLENYLLS LTACDNFGND
VLRFCALWLD NSDNQLANDA VSKHLPDVPS RKFATLMNQL SSRLLDDSDA FQPLLSALVL
QICVDHPYHG MYHLFVCSRS KKDNDPKAIS RYNAAGKIVD RLKKSKRSAE WLAIHNTSYH
YLNFAAEPVE GKVKSGTKLV LKKTIYGTRL QSAILNTKIP PPTMTIPLRT DCDYTNVPHL
VNFQPTFTIA SGVSAPKIVT AVASDGARYK QLFKSGNDDL RQDAIMEQTF EQVSDLLQDH
RDTQQRKLGI RTYKVLPLAS NSGIIEFVQN TMPLNDYLLP AHQRHFPKDF KPNQCRKFIN
DAQSKSRDQR IKAYRHVTDH FHPVMKYFFM EKFPNPDDWF NKRLAYTRST AAISMLGHVL
GLGDRHGHNI LLDTETGEAV HIDLGVAFEQ GRVLPIPECV PFRLTRDLVD GMGITKTEGV
FRRCCEFTLE ALRQESYSIM TILDVLRYDP LYSWTLSPLR RKKMQDAQDA ENSTVNEGGR
KATINEPNEA DRALTVVRKK LGKSLSVAAT VNELIQQATD DRNLAVLYCV ALNMLYRVGR
SYYLVEDYQ
//
