ATM_CRYNB
ID ATM_CRYNB Reviewed; 2968 AA.
AC P0CP61; Q55QS4; Q5KFE0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=CNBF2640;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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; AAEY01000031; EAL20188.1; -; Genomic_DNA.
DR RefSeq; XP_774835.1; XM_769742.1.
DR SMR; P0CP61; -.
DR EnsemblFungi; EAL20188; EAL20188; CNBF2640.
DR GeneID; 4936816; -.
DR KEGG; cnb:CNBF2640; -.
DR VEuPathDB; FungiDB:CNBF2640; -.
DR HOGENOM; CLU_000178_11_0_1; -.
DR Proteomes; UP000001435; Chromosome 6.
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: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; IEA:InterPro.
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: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; IEA:InterPro.
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; Serine/threonine-protein kinase; Telomere;
KW Transferase.
FT CHAIN 1..2968
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000410188"
FT DOMAIN 1936..2524
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2626..2938
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2932..2968
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 364..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2386..2408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2632..2638
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2805..2813
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2825..2849
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 916..930
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2968 AA; 331155 MW; DC20E77C12EC606D CRC64;
MDSVSGLHAA LSLCASDSAK DRARAHALLP PIFANAQNLR VFQAAAATHG GAPWLALFHC
LFRAVALEKR AVLRGSSNAQ AAARLAHAIR IVRLVAEQAV HLIARKPLIA LVAHMRHQLV
LPPRIFAPAL LDYSKALSTL LVYPPHVESL DRHTWLALMS MCFAAILGDD HVSDDQMDDA
DMLGVAAELE RLDAENVPPH RPPVTLNTSS LVQIIPALLC STVSPIVPPT MKSGDTLTAG
QKVGLGIVLK IRRFFTMYPH VTIYHLHLLT ALNTVLSDME LNCRDLFLLG SVKIFPHLVT
LWAAPERDRD RRIPEQIAIA IHRILPHLAH SAELQRAQDV TENVERLMEM LAKESTMSRG
IEPLDLGTFP STATPSRQST PSKRRKLENP LASLISAVGM GRPESRLIAL QTLVFVIDRH
WSKLAKDIQS DIRRTLVSLL TDDNETLQSW AYIALSTIIL SSYTAGANEN NDDDQSHNGQ
SQDDWKQVWS FALRKCHLPG SSRSASHAAA 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
ADVPLVKEEE EEEEEEDWPI LVKPDVQSGI RQDLLPPTMY DTPPQEEEAE SSDPPKRFTQ
YPPTFPSTLL PTPTAITPSS LSTFQSQSNS ASLVHAIWRL PDVSAALQGL FSVCLQVITR
SSSSTSSGQP TQLSHDDDDD GEDDDDDFAV ASGETTSAPL PEKAAELRAS TSLLRSAVAF
RLQGVMLVSA GAAGGAQSKA YKDTQLVNSF LQADGLRAVE IGWAICEAMQ KGWLRLGIDA
VDLVVASLGN MLNSYGYARD ERLLQLCLEF LKCSAPVWMG NDHSNDDDLK DEAMRLVCYI
ATKITAGSIT SWRVRLAMLR FIEAFLHYDS ASKLWADCMV QEEAEEEEQD VSMEDENHLF
HYIAQSLSDP DMRVRARAAT TAASALYRPS IHPSEHPIIY DQVSNSQAGD PTFAEHYLSY
VLWKLNCCIA SAKQRQTVIF DLYEAAIGGT EYSDHLQAGL NAVARRLGLP SITALYLPYA
PTTTISHDTS RSSAIAFVLN TTHRLFGLSN RSAFFTACLE HAGAYMLYCG KIGLFTSACD
AAGVLPEDLA LQLSVAAAAM AMVLPLSNDK ATNVSMNKCK AEALALLSSF PGISGPDAAE
KFLHSYANGV AAHLWELMDL ESSVDEIVAW FDKTEKESAA GIAFAQMMAH DNAKTGRVKA
INPAASFQSI HNVCRFLEKN YSSISLHAFT FAAILRLTSL INNAFLVSEQ RRYLRALAML
LSVHQGTLQR PLIWEAFLTE TITLLLQPDI CRTVLSMVMW AFDWLESLSS TPSKLVNIFC
QLGEIRIELG GSGTPGSQPN QMGDALEDWI VKMSPKWFKS QISQEAFERA VALWPDSLRS
RLSVHASPLS LRDLDDLSQN DAVHNAGQLC KHFLHLADAD HGQDVVSVFV DSTFWSLKDK
ISSVWDKEGI NAFQDLLYLC NGEVRAPSLN FYGQDTFSKA LNATTGEHKK TEAMNALYHA
MCKTMVQLLH DRRPQIRSAA YRCLQRMKPI LTGKDLKELP ADVSDVVPIL VPIPIGSVRQ
SQAMKLDGVI NNATWNKKAE HFATWSLELS RLLCKTASQH DKFFLSFEPL LSTPLLPLHH
FLGHFVHAAL VCSRSMSSER SKAISEHFET VLQNPFASIE AVRSIVNIVL QLRRYEHPFT
SGMLGYNAWL SVNFVDLSKA AVKCGLYVSA LLFLELANDQ GESLDLAEPR VRQIMYDIYS
NVEDPDGFYG IHNKDIRDSL RRRLEHEGLS WQALGWAGAV YNVDGNDSRS AIPVLHHLHD
IGLSRLASVV ATETRTSGSV PLDDPFFADL SWRTGDWNLP IGRESSATSS GLLYSALSAV
HRSKSYESAS KIVDKAVRAE MTRLGGLQKE MLTSIQSTVT NLLCLRELNR WLDPQLQQGM
QEAIDRGTLR DLQDINDKFE FASAERIIAT RLSVFDSVKQ RESQDMIGDA LTPKMELVTK
AESTCHIKLS RLALKSNNLQ AAINSLTALQ KLQTDVGVID EAQDVFCEVL WKQGEHTLAI
QLLEDLLLRE KEKKSKGQRI PALEGRLAHW ASEARLKAAN EIFGMFSNVT KSIKRSTADV
SEHAEIFYQF ACFADKQYVS QSSSADVKQL KEYSKLRASQ ALRLSARQSR ARESDQKDSA
VREAERDEEK LKKFEMQQKQ YLNAALQFYA EAVSMSDNFN DCITRLVTLW LENDENEESN
VTFSRAAHKV PSYKFIFLGP QLAARLHRPE SPTIFNSTLN GLMFRMSQDH PYHTLYHVIP
LLWEHKQPQS TNSSMLGRKS AADDIMRRLA SSASNRLAVG AAKSMKRFVA IAMEWTSFFE
KDKRLEYKLP SDSPLRKAPR DIPVATSTPS IDVTCQYKDI ATFDHFSEWY TRAGGLSRPK
VMTCFDSNGQ KYTQLFKKDD GFRQDAVMEQ IFVLVNDLLN RNRQTRSRKL RYRTYGVLAL
PEATGVIEFV VGTKPLIKYL PPAHEKYHPK DITSHDFLKA MQEVQSVKNN DEKIIQVWTK
LKKRFRPVMR HLFTEKYRDP MAWFSMRLTY ARSLAVTSIV GWVLEIGDRH CSNILMDECT
GELVHIDFGI AFGAGRILPI PELVPFRLTD DLVDALGVTG VNGTFRQCSQ LVLQTLIDSS
DVILTILEVF KQDPLHTWMV DDKMKKAQDG NHKMYPERGQ EKADRIMRET RENLSKELSV
QYRVNQLIQE ARDVNNLATI FRGWHSWL
