ID A0A074WU31_9PEZI Unreviewed; 2384 AA.
AC A0A074WU31;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=M437DRAFT_40781 {ECO:0000313|EMBL:KEQ65931.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65931.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ65931.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65931.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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 -!- 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:RU364109};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; KL584826; KEQ65931.1; -; Genomic_DNA.
DR STRING; 1043003.A0A074WU31; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 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:RU364109};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1242..1827
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2001..2319
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2352..2384
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2279..2327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2384 AA; 270113 MW; 180A47B028CA95EC CRC64;
MAQAYRDALE RTVQELKSRR DEKRLHAAES LLHEVEAAHR ELSAAQFTPY YVEVNKRIAE
LIQNGADTHE RIGGLYALSQ LIDFKGDDAA QKTTRFHTVL RKVMSGNDTA AMVVAAKTLG
HLVSPGGTLT AELVDAEVKV ALEWLQIERN ENRRFSAVLN LYELAKSSPT LLHVWIPDIF
EVIWVALRDP KVMIRESAAN TISQCFEILM ARDPQQRQKW LTRTYEEIDK GFQHNTVEAI
HGSLLALKEL LQKGGMFMHG PRYKEACERI LSYREHRDPL IRREVVYIIP ILARYAPKEF
CNGYIHRSMS HLQGLLKSPK DRNLSFIAIG NVANAVGSQI APYLDNILLH IREALSVKAR
IKNTDEAPIF KCISMISIAV GQTLSKYMEA LLDPIFACGL SDALTQALVD MAHYIPPVKP
IIQEKLLDLL SMTLCGKPFV LPGHPSHSTP LPRIFTREVR DQNDPQHVEH KEQQIALALY
TLGSFDFSGH VLNEFVRDVA IRYVEDDDAE IRKAAALTCC QLFVRDPIVY QTSHYSIQVV
SDVIEKLLTV GVADPEAEIR RTVLASLDAR FDRHLAKAEN VRTLFLALND EIFGIREAAM
TIIGRLTAVN PAYIFPSLRK VLIQLLTEIE YSNNVRNKEE SARLISHLVG SSSKLIKPYV
DPMITVLLPK AQDPNPDVAP ATLKAIGDLA TVGGDEMVKY VPELMKVIIE SLQDLSSAGK
RRAALRTLGQ LASNSGYVID PYVEHPELLS ILVQIVKNEP PGELRKETIR LMGILGALDP
YRHQVMEQSS VNHLVTDSQT VTDVGLIMQG TTPSNEEYYP TVVINTLLDL LKEPTLAQHH
AAVVEAVMSI YRTMRLKCVN FLGLVVPGIL LVIRTSPAGN IEKYFNNLSE LVEIVRQHIR
PYLPEILATV QDFWADNSPY QATMLALIES IAQSLEGEFK IYLANVLPLM LGVLDHDVTP
RRLPSERVLH AFLVFGSSAE EYMHLIIPVI VRMFEKPGQP AHIRKLAIET IGKLSRHVNI
SEFAAKIIHP LSRVLAGQET GLKQTALDTL CALIFQLGPD YIHFIPTINK ILVAHKVPHT
NYALIVSKLQ KGEPLPQDLS PDERYKTSAS EEVQRGVDNR KLAVNQQHLK IAWAANAKST
KEDWQEWMRR FSLELLKESP QNALRSCSQL ASSYPPLARQ LFNSAFVSCW TELYDHYQES
LVRSIETALT SPHIPPEILQ VLLNLAEFME HDDKALPIDV RTLGMYAGKC HAFAKALHYK
ELEFNAEQNA SNVEALISIN NQLQQTDAAF GILRKAQGYV DVQMKETWFE KLQRWEEALT
AYQRRERDEP DSFEVIMGKM RCLHALGEWE VLSSLAQEKW MHASSENRKS IAALAAAAAW
GMGQWELMDG YLSVMKLHSP DRSFFGAILS IHRNQFDDAQ LHINKSREGL DTELSALLGE
SYTRAYSVIV RVQMLAELEE IIAYKQSSSD PHKQERMRLT WTKRLKGCQK NVEVWQRMLK
VRALVISPPE NAEMYIKFAS ICRKAQRNGL AEKSLNSLLG WQGSLMTPEG QERTLHAPYP
VQYAVYKYMW SNGYSSGALT GLRDFTERLR MDYEQRSLAV TNPGTNGMNG MNGTNGVNGT
QFPAAGVSPQ VSEKDMAQLA DWQKLLARCY LKQGDWLSLQ MRGEWDAHRV HEIRSSYKAA
THYNQDWYKA WHAWALANFE VVTALTANKD RGEADGMQRR YIHDYVVPAI QGFFKSIALS
SSSSLQDTLR LLTLWFNHGE HQEVTSAVTQ GVTTVSIDTW LEVIPQLIAR INQPNRLVKE
SIHHLLCEVG RAHPQALVYP LTVSIKSEDR DRSRAAKDIM AAMEQHSPNL CRQAAVVSHE
LIRIAVLWHE QWHEGLEEAS RLYFGDHDID GMLRTLEPLH RMLDEGPETL REISFIQSFG
RDLAEARDWC NNFKRTNEVG DLNQAWDLYY GVFKRIARQL PQLANLELQY VSPKLKNVHD
LELALPGTYK SGKEIIRILS FDPSSTVIQS KQRPRKLTVT GSDGGTYQYL LKGHEDIRQD
ERVMQLFGLV NTLLSHDPES LKRHLNIQRY AAIPLSTQSG LLGWVPNSDT LHVLIRDYRE
SRKILLNIEH RIMLQMAPDY DNLTLMQKVE VFGYALDNTT GQDLYRVLWL KSKSSEAWLE
RRTNYTRSLA VMSMVGYILG LGDRHPSNLM LDRNTGKIIH IDFGDCFEVA MHREKYPERV
PFRLTRMLTF AMEVSNIEGS FRTTCEHTMR VLRENKESLI AVLEAFIHDP LLTWRLGNKN
SPPEPSFPSE RRTSIIGDLD AAPRSTPGGR KRAPPGGENV PGEGKEVQNA RALQVLARVK
EKLTGRDFKK DVELAVEEQV EKLLSEATNL ENLCQHYGGW CSFW
//
