ID Q4X1E3_ASPFU Unreviewed; 2384 AA.
AC Q4X1E3;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=AFUA_2G10270 {ECO:0000313|EMBL:EAL93322.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL93322.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL93322.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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. {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL93322.1}.
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DR EMBL; AAHF01000001; EAL93322.1; -; Genomic_DNA.
DR RefSeq; XP_755360.1; XM_750267.1.
DR STRING; 330879.Q4X1E3; -.
DR EnsemblFungi; EAL93322; EAL93322; AFUA_2G10270.
DR GeneID; 3513753; -.
DR KEGG; afm:AFUA_2G10270; -.
DR VEuPathDB; FungiDB:Afu2g10270; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; Q4X1E3; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; 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:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
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 GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
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; 2.
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; 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:UP000002530};
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 1241..1817
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1991..2310
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2352..2384
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2384 AA; 269583 MW; D62AE34718F5E08D CRC64;
MAQAGPITDI TQRLFSELKS KNEETRVRAS FELYDNVLAI SRDWPPEKFL EFYNAVSQRI
AQLVVTGSDA HERIGGLLAL DRLIDFDGVD AAQKTTRFAS YLRSALRSND NAVLVYAARS
LGRLAKPGGA LTAELVESEI QSALEWLQSE RQESRRFAAV LVIRELAKGS PTLLYGFVPQ
IFDLIWVALR DPKVLIRETA AEAVSECFEI IAARDAQVRQ LWFARIYEEA LLGLRSSNVD
SVHGSLLVLK ELLLKGAMFM NEHYRNACEI VLRLKDHRDH KIRAQVVQTI PILASYAPVD
FTETYLHRFM IYLQAQLKRD KERDAAFIAI GKIANAVGAA IAQYLDGIII YIREGLALKA
RNRAAVNEAP MFECISMLSL AVEQSLSKYM ESLLDPIFAC GLSESLTQAL VDMAHYIPPI
KPTIQEKLLD MLSLILHGTP FRPLGCPESR LPPMPSFAKD FAPQELHSDA EIALALHTLG
SFDFSGHILN EFVRDVAINY VENDNPEIRK AAALTCCQLF VHDPIINQTS SHSIQVVSEV
IDKLLTVGIG DPDPEIRRTV LWSLDRKFDR HLARPENIRC LFLAVNDEVF AVREAAICII
GRLSSVNPAY VFPPLRKLLV NLLTGLGFAS TARQKEESAQ LISLFVSNAT KLIRSYVDPM
VTTLLPKATD ANPGVASTTL KAVGELASVG GAEMRNYLPR LMPIILDSLQ DLSSHSKRES
ALRTLGQLAS NSGYVIDPFL EYPHLLAVLI NIIKTEQTGS LRKETIKLLG ILGALDPYKY
QQISEIEPDV HHINEIQTVS DVALIMQGLT PSNEEYYPTV VIHTLMQNIL RENSLAQYHS
AVIDAIVTIF KTLGLKCVPF LGQIIPGFIS VIRGSPPSRL ESYFNQMAIL VNIVRQHIRA
FLPEIIEVIQ EFWDSSYQVQ ATILSLVEAI AKSLEGEFKK YLAAMIPSML DTLEKDNTPR
RQPSERILHA FLIFGASGEE YMHLIIPSMV RLFERAQNPQ SIRKSAIDSL TKLSRQVNVS
DFASLMIHSL ARVVAGNDRT LRQAAMDCIC ALIFQLGQDF CHYINLLNKV LAHHQINHVN
YQILVSKLQK GDPLPQDLNP DETTGTLADE SSYSDIGQKK MVVNQQHLKN AWDASQKSTR
EDWQEWIRRF SVELLKESPS PALRACASLA GIYQPLARDL FNAAFVSCWT ELYDQYQEEL
VRSIEKALTS PNIPPEILQI LLNLAEFMEH DDKALPIDIR TLGKYAAKCH AFAKALHYKE
LEFEQDQNSG AVEALITINN QLQQSDAAIG ILRKAQAYRD VELKETWFEK LQRWEEALAA
YKRREKIDPD SFGVTMGKMR CLHALGEWKV LSDLAQEKWN QASLEHRRAI APLAAAAAWG
RGQWELMDSY LGVMKEQSPD RSFFGAILAI HRNQFDEATM YIEKARNGLD TELSALLGES
YNRAYNVVVR VQMLAELEEI ITYKQNIGDP EKQESMRQTW NKRLLGCQQN VEVWQRMLKV
RALVTSPREN LDMWIKFANL CRKSNRMGLA ERSLASLETV VTDNNGTRTI APPEVTYARL
KFNWATGRQR EALQMLKEFT ANLTDDLNRF NALMASQSDH NGVDGVNGIT EANHADMMGL
RERIGDVAKF RKLLSKSYLR QGEWQTTLQR GDWKPEHVRE VLGAYSAATK YNRDSYKAWH
SWALANFEVV TTIASQTSRD GGIKPVVPGH IVTEHVIPAI GGFLRSIALS STSSLQDTLR
LLTLWFTYGG DQEVNNVVTE GFNAVNIDTW LAVTPQLIAR INQPNLKVRT AVHRLLAEVG
KAHPQALVYP LTVAMKSHIT RRSQSASTIM DSMRQHSATL VEQADLVSHE LIRVAVLWHE
LWHEGLEEAS RLYFGDHDVE GMFATLAPLH DMLDKGAETL REVSFAQAFG RDLAEAKHYC
MLYRETEEIG DLNQAWDLYY TVFRKISRQL PQLSTLDLKY VSPRLKDCHD LALAVPGTYQ
SGRPIIRIIS FDPILHVLQT KKRPRRMTLK GSNGSSYMYA LKGHEDIRQD ERVMQLFGLV
NTLLDNDGET FKRHLSVQRF PAIPLSQNSG LIGWVCNSDT LHALIKEYRE SRRILLNIEH
RIMLQMAPDY DNLTLMQKVE VFGYAMDNTT GKDLYRVLWL KSKSSEAWLE RRTNYTRSLG
VMSMVGYILG LGDRHPSNLL LERATGRVVH IDFGDCFEVA MHREKYPERV PFRLTRMLTF
AMEVSNIEGS YRITCEAVMR VIRDNKDSLM AVLEAFIHDP LINWRLNIRE SPERPPFSTE
RRQSITSVMN LEHGVQPSNF SRHRRPSILD GGILDVQEGI PPEAREAQNA RAVQVLARVK
EKLTGRDFKP TEELNVSDQV DKLLAQATSV ENICQHWIGW CSFW
//
