ATM_CRYNJ
ID ATM_CRYNJ Reviewed; 2967 AA.
AC P0CP60; Q55QS4; Q5KFE0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Serine/threonine-protein kinase TEL1;
DE EC=2.7.11.1;
DE AltName: Full=ATM homolog;
DE AltName: Full=DNA-damage checkpoint kinase TEL1;
DE AltName: Full=Telomere length regulation protein 1;
GN Name=TEL1; OrderedLocusNames=CNF02070;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- SUBUNIT: Associates with DNA double-strand breaks. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with other DNA
CC repair proteins in response to DNA double strand breaks. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
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DR EMBL; AE017346; AAW44228.1; -; Genomic_DNA.
DR RefSeq; XP_571535.1; XM_571535.1.
DR SMR; P0CP60; -.
DR STRING; 5207.AAW44228; -.
DR PaxDb; P0CP60; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_11_0_1; -.
DR InParanoid; P0CP60; -.
DR OMA; LWLANFD; -.
DR OrthoDB; 80538at2759; -.
DR Proteomes; UP000002149; Chromosome 6.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015519; ATM/Tel1.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR001494; Importin-beta_N.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR11139:SF72; PTHR11139:SF72; 1.
DR Pfam; PF02259; FAT; 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; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 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; Chromatin regulator; Chromosome; DNA damage; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transferase.
FT CHAIN 1..2967
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227700"
FT DOMAIN 1935..2523
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2625..2937
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2931..2967
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 364..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2385..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2631..2637
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2804..2812
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2824..2848
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 2387..2407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2967 AA; 330906 MW; FA723CFFAF25F542 CRC64;
MDSVSGLHAA LSLCASDSAK DRARAHALLP PIFANAQNLR VFQAAAATHG GAPWLALFHC
LFRAVALEKR AVLRGSSNAQ AAARLAHAIR IVRLVAEQAV HLIARKPLIA LVAHMRHQLV
LPPRIFAPAL LDYSKALSTL LAYPPHVESL DRHTWLALMS MCFAAILGDD LVSDDQMDDA
DMLGVAAELE RLDAENVPPH RPPVTLNTSS LVQIIPALLC STVSPIVPPT MKSGDTLTAG
QKVGLGIVLK IRRFFTMYPH VTIYHLHLLT ALNTVLSDME LNCRDLFLLG SVKIFPHLVT
LWAAPERDRD RRIPEQIAIA IHRILPHLAH SAELQGAQDV TENVERLMEM LAKESTMSRG
IEPLDLGTFP STATPSRQST PSKRRKLENP LASLVSAVGM GRPESRLIAL QTLVFVIDRH
WSKLAKDIQS DIRRTLVSLL TDDSETLQSW AYIALSTIIL SSYTAGANEN NNDENNNDGQ
SQDDWKQVWS FALRKCHLPG PSRSASHAAA VLLQFDKVDS PSTIRGIQTM LTTIAVQGPP
TAHDSVCALY SIALEAARSD IQLYSLNLEE QVLSWLEKTF AREKFERDKM DQRLDQATPG
DILRLFSAVS RIQYHVPLAE PVTKEFLPDS AVVSYALERA KTQPIRDFLL YHTCPTPPPP
PPPLDDSHTT PLLAASENHS TFLGGRPRRL SELLLSILNA TTAQWETKPV ISSGERPRRC
VDLVALGLAF QGLLQLDGYI PHAACINAAI RLLHLLKPSL TSSDLSIPSL DLVWRGLRCL
ADVPLAKEEE EEEEEDWPIL VKPDVQSGIR QDLLPPTMYD TPPQEEEAES SDPPKRFTQY
PPTFPSTLLP TPTPITPSSL STFQSQSNSA SLVHAIWRLP DVSAALQGLF SVCLQVITRS
SSSTSSGQPT QLSHHEDDDG EDDDDDFAVA SGETTSAPLP EKAAELRAST SLLRSAVAFR
LQGVMLVSAG AGGGAQSKAY KDTQLVNSFL QADGLRAVEI GWAICEAMQK GWLRLGIDAV
DLVVASLGNM LNSYGYARDE RLLQLCLEFL KCSAPVWMGN DHSNDDDLKD EAMRLVCYIA
TKITAGSITS WRVRLAMLRF IEAFLHYDSA SKLWADCMVQ EEAEEEEDDV SMEDENHLFH
YIAQSLSDPD MRVRARAATT AASALYRPSI HPSEHPIIYD QVSNSQAGDP TFAEHYLSYV
LWKLNCCIAS AKQRQTVIFD LYEAAIGGTE YSDHLQAGLN AVARRLGLPS ITALYLPYAP
TTTISHDTSR SSAITFVLNT THRLFGLSNR SAFFTACLEH AGAYMLYCGK IGLFTSACDA
AGVLPEDLAL QLSVAAAAMA MALPLSNDKA TNVSMNKCKA EALALLSSFP GISGPDAAEE
FLHSYANGVA AHLWELMDLE SSVDEIVAWF DKTEKESAAG IAFAQMMAHD NAKTGRVKAI
NPAASFQSIH NVCRFLEKNY SSISLHAFTF AAILRLTSLI NNAFLVSEQR RYLRALAMLL
SVHQGTLQRP LIWEAFLTET ITLLLQPDIC RTVLSMVMWA FDWLESLSST PSKLVNIFCQ
LGEIRIELGG SGTPGSQPNQ MGDALEDWIV KMSPKWFKSQ ISQEAFERAV ALWPDSLRSR
LSVHASPLSL RDLDDLSQND AVHNAGQLCK HFLHLADADH GQDVVSVFVD STFWSLKDKI
SSVWDKEGIN AFQDLLYLCN GEVRAPSLNF YGQDTFSKAL NATTGEHKKT EAMNALYHAM
CKTMVQLLHD RRPQIRSAAY RCLQRMKPIL TGKDLKELPA DVSDVVPILV PIPIGSVRQS
QAMKLDGVIN NATWNKKAEH FATWSLELSR LLCKTASQHD KFFLSFEPLL STPLLPLHHF
LGHFVHAALV CSRSMSSERS KAISEHFETV LQNPFASIEA VRSIVNIVLQ LRRYEHPFTS
GMLGYNAWLS VNFVDLSKAA VKCGLYVSAL LFLELANDQG ESLDLAEPRV RQIMYDIYSN
VEDPDGFYGI HNKDIRDSLR RRLEHEGLSW QALGWAGAVY NVDGNDSRSA IPVLHHLHDI
GLSRLASVVA TETRTSGSVP LDDPFFADLS WRTGDWNLPI GRESSATSSG LLYSALSAVH
RSKSYESASK IVDKAVRAEM TRLGGLQKEM LTSIQSTVTN LLCLRELNRW LDPQLQQGMQ
EVIDKGTLRD LQDINDKFEF ASAERIIATR LSVFDSVKQR ESQDMIGDAL TPKMELVTKA
ESTCHIKLSR LALKSNNLQA AINSLTALQK LQTYVGVIDE AQDVFCEVLW KQGEHTLAIQ
LLEDLLLREK EKKSKGQRIP ALEGRLAHWA SEARLKAANE IFGMFSNVTK SIKRSTADVS
EHAEIFYQFA CFADKQYVSQ SSSADVKQLK EYSKLRASQA LRLSARQSRA RESDQKDSAV
REAERDEEKL KKFEMQQKQY LNAALQFYAE AVSMSDNFND CITRLVTLWL ENDENEESNV
TFSRAAHKVP SYKFIFLGPQ LAARLHRPES PTIFNSTLNG LMFRMSQDHP YHTLYHVIPL
LWEHKQPQST NSSMLGRKSA ADDIMRRLAS SASNRLAVGA AKSMKRFVAI AMEWTSFFEK
DKRLEYKLPS DSPLRKAPRD IPVATSTPSI DVTCQYKDIA TFDHFSEWYT RAGGLSRPKV
MTCFDSNGQK YTQLFKKDDG FRQDAVMEQI FVLVNDLLNR NRQTRSRKLR YRTYGVLALP
EATGVIEFVV GTKPLIKYLP PAHEKYHPKD ITSHDFLKAM QEVQSVKNND EKIIQVWTKL
KKRFRPVMRH LFTEKYRDPM AWFSMRLTYA RSLAVTSIVG WVLEIGDRHC SNILMDECTG
ELVHIDFGIA FGAGRILPIP ELVPFRLTDD LVDALGVTGV NGTFRQCSQL VLQTLIDSSD
VILTILEVFK QDPLHTWMVD DKMKKAQDGN HKMYPERGQE KADRIMRETR ENLSKELSVQ
YRVNQLIQEA RDVNNLATIF RGWHSWL
