ID A0A1X7R775_9SACH Unreviewed; 2796 AA.
AC A0A1X7R775;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=KASA_0L03641G {ECO:0000313|EMBL:SMN21300.1};
OS Kazachstania saulgeensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN21300.1, ECO:0000313|Proteomes:UP000196158};
RN [1] {ECO:0000313|EMBL:SMN21300.1, ECO:0000313|Proteomes:UP000196158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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|RuleBase:RU365027}.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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 -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574, 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; FXLY01000007; SMN21300.1; -; Genomic_DNA.
DR STRING; 1789683.A0A1X7R775; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000196158; 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:SF6; -; 1.
DR PANTHER; PTHR37079; 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; 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|RuleBase:RU365027};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, 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:UP000196158};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1733..2328
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2437..2747
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2764..2796
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2718..2750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2718..2743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2796 AA; 323046 MW; 314361653A620F74 CRC64;
MNNTDIITIL SSFSSSKLKE RNAALEDLTT VLKEDPSRIP SKALHGTSES LIELLDLEHR
KYYDLLDDRS KSNTSKLSLS ENRLSTVAYV LRLFIEKVGY RFKLKTLNLH LAILPELMVK
DRDQTLVEPA SVHLTFALLN IIESCPFQLK FTSHQWFSLM EKVCLCLNKQ ISISVSNRTV
SNLISIVASL LKLDTIALYD GALSVHGTIL RLLKTVEYLS TDTRTIIQIV NLLLAKTFMS
HINVCFSIIQ ETWKYAINFN DSTVEPLQDE LMYHYLLSTD LICHKLPNMV GVSLPTFDDN
SFLDLFKQTL STRLNTYNPK SLDPQSIIFN KTININDLDW LNFCDIKLNT EENPKSWINT
LVSVKLLQAY FYLKQNLSNS IPLFKRNKTE NEFNTALNNC VNIESLLLEC LSSTSSTKVQ
LTSLQLFTFL ASMSNIRESS LNEFKSTLLQ RFENPDLITW CTISLVPLLT QSSLQLREED
IVKITKLCLP LIKEHNNCRP ACSVISKIIR YSDKIVADPT LRNQIFDLYD LSDVNGPSLV
CNESFEFWQY LQHYASEYRS REGKLSEYRV RIWLMNSWDQ IFSSSENQKE IDLFLLWLAG
IDIDDRPNII ETMAIENAEQ YLSWGHRIII EKESRPHRKF LIQPPQTEKQ IKYGQRTIQM
IRNISNNKTV NDILFKALDI LEKHDTYSID VILKWTFTLL RIGKYIKSNT DYEDFIYALK
NTLYLSKYSV EFKSYKTYLQ YFKEVIRGDF DWALVDEIFD HSHIFNLFTD KFLVINTNKD
NNDRDFEKTS PEKTIKRTGT PLPQEYAIIY DSFELRLSFE ALTHIILDSN SENRFSILLD
YLNKLTPQLI ISCLRLFFKL SQNNKKSTLD IGNSELEKLT SLVGQKLLSN QYNTSNATIE
CLCDYLFIVD EHWLSDPSSH IYSDCNDILN WLIMRFEDQT FSGTYALRHL ILLFLNILTY
PKLSQNTDKG TKQRIFEVLI QCLQRLDTNS IMCVENSIIE YMKIITYKNQ NIFLKEIIKV
FSVPQQSIEI AACYTLTLIH MTSISYTILV QCLLDMLSYQ QYYHVEYFIH HAFDLITKSW
KMETALELFD MCKLELLSNW IKGISKSDST SIYQWDITAF GFSDIDHVYI KYSREIGAIY
MSSGSNCKDV LDRLLKNGSK DEADILTRSL FLAIPLAFVE DNIGSLIFDV GFQLLGKNMQ
VYEKKDSLLT FKIFLRLLDL GRPDDVNSAL QRYYPNIIKW NEIIKNEKST IRYQFPFHID
LISGMKFMNA YFNHSEFVRS EICERLLWVE LTELENSDEV IGKLRCLREI KVIFFHFGKN
LFKCVGYHAI IRKIAQYIMD KNLLFDIIPL LQIIFTNEQR TIIDSKKSIS TVFLQFIRLK
LHINLNFGSE ITSLLNEISI STDQNGFPLW SMCIEYINGN EIELDYNIVS EVLNGLLYCD
EDLLIISVLL SDNTKVHLNK SQFELSERSL FRLLTTDVDS PFSSKRFTLL KALFIKYKVD
KNISIPSSAE AASIIPKCSN IFKSSNPLLI FYQDFLNFNK HLDSKNDSNK TFLLSRTISD
FLLCNIGSGS IIDTTRINLR EFPDKLNNTQ ELIYDIISPH WEPHVDINEF ALDSKKYEKF
SSDLWRTSFM SALLQAMSFT VPIITIFNPL IVESYQYRQK TFNSLFILSL FYDPKGFIEW
YPTLIITVMN SSNVTDYEAK LRIVLSTVSI IRYGCKLQNK CCMKAFQKLN LSQLCFLAID
AKMPTLGLML YEEIYMEKNT ENDQILLSKV YDSLGDRDFQ SGLPPAHSLM EAFNSTIKLD
YNPWKSFVFS NASFDANYKS RTSDDLTLLK MTSEKNGFYG ITKSIESGNP SQESNENFDW
NFQLGNWDLP IPEKVDSISK GLYSTLKLVN NEHSSVNLAL EESLIRIMGA QNNFKNSEDW
FGLVTEIGKL IDIVDNLNIP MKLGDVLNKI AKYSNSTPNP ADLDNQRMFL QSRHHFLSAI
FANVKLSAHY NPITLDLART IVLKDQMKFS IKNHKLQDSL RNAFILTSLN KVSQSPPIED
SISHASSRLI SFLSAITLWE SDDYKTPIMM MNDLLRTSEP EIEADISEFK PLVNLLSVEN
GIVLGYLVKW CSESRMESPN EIYKKYIGGK TIQVEESDLR ARTFRIFGDF LNNQIKKLQA
SGEIGKFQER SKISRQNLET LTLISQNQTV SEKERKVAKR HIYKAQLQYD RDQGRLNELE
LLRDEFTYES LNFYMKTLIS TNIYDSDVMD KFCALWFENA DNSTLNQKLM ESISSIPSWK
FIPWVNQISS KLNNDDSAFQ KPLQLTMKRL LYKLPYESIY SAISIKLYQI YTIGSNANIV
GKIAAVKNIF ESLQSFDSGN YYSKYILPIE EFCQKSVELA SFRIKEASKV INLKGLKIGD
YWLNKLPMNK IPLPTDHITI HSSEDGKKNR PYIVSVTEDI HVTSTGISLP KIVKFKMSNG
VTKQVLMKGS NDDLRQDAIM EQVFTQVNNI LMQNEELSKS KLRIRTYKVI PLGPRAGIIE
FVNNSVSLHQ VLKEYHKDDK LKFDDARREM KAVQTKPNPE RLKIYNKIVS IIEPQLRMFF
FENFIDYNAW FEAKKCYTRG MATTSIVGYI LGLGDRHLNN ILLDSSTGEP IHIDLGIAFD
QGKLLPIPEL VPFRLTRDII DGFGITGVDG LFKRSCERVY TALRKDSEKV MCVLNVLKWD
PLYSWVISPV TKHKHLLEDD TELDDNPNLE QRTNNKDGKQ VVDNNDNQES NRALKGVEEK
LNGDGLRVEA TIEGLIQDAT NPENLSIIYM GWSPFY
//
