ID A0A167SEY0_CALVF Unreviewed; 3083 AA.
AC A0A167SEY0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=CALVIDRAFT_508488 {ECO:0000313|EMBL:KZP01857.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZP01857.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZP01857.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZP01857.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417266; KZP01857.1; -; Genomic_DNA.
DR STRING; 1330018.A0A167SEY0; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000076738; 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; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365027};
KW Chromatin regulator {ECO:0000256|RuleBase:RU365027};
KW 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:UP000076738};
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 1972..2596
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2704..3016
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3051..3083
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 163..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2994..3023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2995..3013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3083 AA; 347914 MW; FC273C21CDB66578 CRC64;
MAPFGLHTLS HGKVTERHAE LAKVRAYFER IGSNLYTEES DDYLYLYQSL FACIRQDAQV
WEKKPSPAGE RRLEDAGAVL RLVVEKTIHR TERKPFNALR NHVLQSSVYR KELVPPLALN
YAKMLDTALA YNPHLEHLRP DEWVQLVFRC FDVLLGNKIT NETPLDEDFR EPDDADMDAE
DHDARDGLTS PTPGPSTSNK RARVESSSSS PNAKRPRRAQ RLIPMTTVQR EYASVLKRLF
STSRMHLLDK VILKDHRSPD REPEGYEIMK RLQKAVLRSF TSFFSIFPGE TSGTEDVLCA
MNAALFDLEL NAKELVTEFG LDTLPILMDV WGIKSPLTKE QLIITTRLLL PFISHQSVDS
LVSHDLIAKL RRRLEEETDP RGGLEPLTLD SLRLQLADAE ELPAREEEAP FRKVTFRNGH
GLTKEQVVTW AAMEVHADCL SKLHEQSEVS FVGKDGERES KRLRRENPVK LFISAFESPQ
EPEHTRVFRL QFLLFFIDRS WSTLHEELQN LIHNQLTALV SDTHSSVQSW GLLCLAAIAA
CSQPKELRMD WPAVWSLALR RLSTTSTCRS ACHCLHVMLK VPLLEWQRIL SEIADLSREL
AVQGPTFPYD SVCSFLSECL RVASRDSTLY RMQIEDKILA WLEKTWRMVE GTTSGFTTQI
RLEPHTVSDT ISLFSAICQL KTRVSLDTRI LPPDCCMTDR LLGERSSALE RDFLLSARLP
FPDLVKPNDI ASEPQIDKQA EPTDSVDMGS TAGGQSIDEL IFPDLRQRSC STFLQSTLDH
LIQEWSSIKE PQSTTTMEQL RRMADIVTHC LAWEALLTLN GVRFTRKVIQ LAACVLDFLS
SVLAARSKTH VGRPESPALV LSALDPLVNA RSYEGDTSKE IFLRPGAESG IRRAVLMRVT
QTRSTERDSI LRERSRLQGI IWRMADLQDA ALSFLKLLRG YFSQATDDGI DKLGAGHDDG
WDMGQHSVAL QGQPLPSATL RTLPQRACAE ISVAYLARVP GYQSQKESVD LDQPARDLIL
LGIANRTFLI SRSFFRSIQS RELRFTIEDA KAILKALNEA SFEYSNVRSE AFWLCVAEHL
RCTLKLWLRQ STHSADAFFE FAGTAIRACQ TYNFRWVPPF ITEWLHVYLS SDPEESQWVL
EDETARSVLE DYATHGDYRV RFHLGPYLGA LFVQNQKEGQ PLDYYNTLFD KLPAHADRFE
EMCTRSMIMG NIMLPSSEVR KAPYWALIST CLQFDLYKEH VQNVLVLVSA LLGMGSLADL
FRPYAGQFAF TASQMTLQTD NMDVYDLTKL PKMFGYPDRK SLASDCFLLM GPVFLALSND
VDANGGSCFR ALCTARGIQP TAGMQECLPR TLGLRIAFFM NNITLDDPSA APNLEDIAFL
NDGITRHAQL CGIEEPEPAH LVSTHIVDIV LSILTLLVDT DFGSPGASVL RLLQSASQLA
AKFPGSRGSK IDSPSAISTF RAFVIDIDQD YPMHRPILPA VSSLTILRCL LWLNSHYGGA
FLHETAYHVV TELFALATRA SMVNEQVRAL RSVMMYISLC TSCFTQLSVL RVLLRGASAL
IDQMDVARTS RNFLNWGLQL FLRIDKPDEI LTEILLRIGR AMDGYGLRAS DPASIYFNQE
LEAWIVQRME ELYESKVLRE MVRTAVILWP STDVDLFPFC EVSLDSVHAV LLKEQTAGDK
FPLVRYVSAA AQGGIGDLSS LSAAGFWQLK AALHTSTKTD IEHSHQISNL LFSYSCRLEA
VEMDTRPVPM ALTRYLREVA AHRRRFRELS SAFYLVAHLS QLLTDVQAGR RAAAYATLRR
VMPLIPEEVR GLSQVTQAEV SLIRTYPLEL YPWRERSIQE LLDPAPTQLA ATYSDWIHFF
TTFLVELHAP YDPIWAQAIP ILQMDVSFAE LLLPPLVHAV LKREVLVDGI EHRSIRTLIS
AYFQRLLEQQ GITSTACTLA IIDVIIYLRN FEVDEKVDPL SHDKWLDLDF GLLSKCAAAS
GAYKTALMLH EMMADSPDKH AQNVSDEEVL YAVYSHIEEP DGFYAIKARD ARTSVVRSVE
HEGRWDLALG FHGSGSRTGF SKPGTGSEDS ALGIVRSLKS LGFDYLAVSF LNSLDKRIAL
PDLEYDLAWR TDSWDLPNIR HESTNTNAAL YMALQAVHRE RRPEQANAVM NDAFVQTVQH
LKVIPDDDMV GLLKACTTLV CLREVLHWLE PCFQIALKSE EVPAADVEEL LKIPTDMDFS
VTESTVATRV SLLRAVQTAD ATEQIGNLRT SFSQRLRAIE RDCLLGLSEA ARKSGKVQVA
LNAVTQAQQL QTTQISNIAT STEFANVLWA QGEKKSAIDA LSALLQDQLD SYPDFQQMSD
SDKAKIAALE AHLGWWISEA GLDEGRNIND QYFQPAIELL GKTSGPISSD HASVFYRYAL
FADEQYQTIG TRDLSRYELY IRRKEQELAW FEAQGYDAAV RRVQEARIAK IKPRPNDTNL
IHKYRTHRDR ANTLLQRDQA RYAELVLAGK LFLRKAIEMF SKVLSFSDIH DENAAVRLLA
RWFSQFKDDD LNNVIGPDLE RVPSHKFVFL VHQLSARMDR TPSLPGGQRN LQSLMLRICK
EHPFHSLYQV YALGGLKRSR MAAAQADEGS QQGRIDAAAF IYHALSVDAS SGGRIKHVFE
ACEAYLEWAN YPMKAQKPDQ GKNHAMPARL RILQLVNYDI PVATVHTSVD KTMMYRDIVT
IQQYDKVFKV AGGNNCPKIS TCIGSDGRRY HQLFKGEGGD DLRQDAVMEQ VFELVNNLLR
HDLHTTKRRL QVRTYRVIPL ASQAGMLEFV ENTSPLGTWL QAAHLRYNKG EPPTNKIRER
LPAPEAQIPP DRKYKFFDEI CKRVRPVMRH YFTEKRKIPA AWFAMRLRYA RSVAVTSIVG
HILGLGDRHL SNILIDNQTG EVVHIDLGIA FEQGTLLPIP ETVPFRLTRD IVDGLGTCGT
DGVFQRCAEN TLRVLREESD HIKTILEVFR YDPLHSWTAS PFQIAKAQAI EVTPPSTGMP
PSTAGSEFAP SVSLASKPSE GDVTEELNME SDMAQENADR ALKSVADKLD KSLSVEYTVN
RLINEARDMW NLSQIYSGWL PWY
//
