ID U5HB66_USTV1 Unreviewed; 2373 AA.
AC U5HB66;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=MVLG_04424 {ECO:0000313|EMBL:KDE05182.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE05182.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE05182.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE05182.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE05182.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC Lamole {ECO:0000313|EMBL:KDE05182.1};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_04424T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; AEIJ01000434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541691; KDE05182.1; -; Genomic_DNA.
DR STRING; 683840.U5HB66; -.
DR EnsemblFungi; MVLG_04424T0; MVLG_04424T0; MVLG_04424.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; U5HB66; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000017200; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
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; 5.
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 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:UP000017200};
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 1276..1828
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2002..2313
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2341..2373
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 453..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2373 AA; 266568 MW; 4C00FD0B10FB896A CRC64;
MSSSLFVAAK ASKAERPLDA ILGDLRSKHD EIRFKAAQEL YNYILASSRS LSAEAFNKTY
SEIHARCFAL VNSSDLQDKL AGVTAIDKIV DVLGNDMSRA IRLAASVQRA FPCSDSLVMT
NAAKVFARLA AQGGILMSGH VDTQVKSCIE WLQGDRIENR RYAAVLILRE LTRQAPGLIY
EHLTELLDNL WTAMWDPKVA IREAAADALA GCLLIATQRD GQLRVDAYNM VFGQAQIGFK
TGYPETIHGS LLGYKELFLE GKLFMADRYG EVCDQILFYK DHRDPLVRRA VIELIPTIAS
YNANEFAAHY LSRTMAFLLD QLKKDRGDRA TAFQAIGRVA LQVKSMMTPY LDPILNSIKD
GLLSRGRKNQ PAGLENSIFQ CIGMLAQSVG PALTKHMHEL LDLMFAYGLS PALHTALQQL
GRDIPPLLPD IQERILNLIS MTLADEPFVQ AGAPHKGSKH PDLTVSGVNG HAHHHHPEKQ
SPERIMLALE VLGTFNFKGV FQPPKHLTPG MMPEPVVEQS LGEFVRDHVI HYVEDDNPDI
RRAAALSCCQ VLSNDPIVTQ ASNHAIKLMN EVLEKLLTLA IADPDPSIRQ ATISHLDPNF
DRHLAQADCV RSLFIALNDE VYAIRESAIR IIGRLATLNP AHVMPSLRKT LIQLLTELEY
STASRNKEEA STLLGLLVGA SQRLTKPYVT PMLNVLLPKS RDASPSVAAS IVTTLGELTK
VGGEDVLPSL DELMSLILDT LHDQASTQKR DAALRTLGQL ASYAGYVIDP YLQHPTLLGI
LISLLKTEPA PHTRREVIRV MGALGALDPY RHSVVEGISN DAYVESFNPT DPTHPSNIGP
SHEEYYPTVA FNALLGVFSD PSLSDHHTAI VDAIIYIFRS LRLKVVTFLP QVLPVYLNVM
RTCPVGLQEF YFQNLSQLIQ MVKQHVRNHL APILAIVREF WNSTTNPGLQ VIIIDVIQSI
ALALDAEFKA YLPNLLPLML KAFDHDFIEL RRQSSLIKVL HAFAVFGTSL EEYLHLIIPA
IVSTFERPDI PAVLRRHAMQ TLSQLCRKIN FADHASRIIH PLARVLANPA SPLELRVPAM
DAMCSLLLQM GPDFVLFVPM IHKILVRQRI SYPPYQTLVD KLLAEEPLPQ DLTFGDPIIM
PNTEAIVAAD AGMSKLPVNQ VHLKSAWEIV DRPKADDWRE WIKRISVQML KSSPSLSLRA
CANLAEVYHP LARDLFNAGF VSVWGELYDN YQEDLVRAIQ NAFSSPTLPP EITQQLLNLA
EFMEHDDKVL PIPISTLGQY ALKCRAYAKA LHYKELEVLS DPSLHTIEEL IRINNSLQQP
DVSVGILVHA HQRHGLVLKE EWYIELERWE DALAALQRKA QEQPDSFDVT LGRMRCLHAL
GEWESLAHLA QENWARASHD MKRKIAPMAA AASWGLAQWE SMDTFIGVLK HDSADRAWFR
SILSIHRGQF NKAQSHINKA RDLLDTELTT LVGESYNRAY DAVVRIQMLS ELEEIISYKE
ATASGNLERR NLIQRTWMKR LLGCKRDVDV WQRILKVRAL VVSPHENIEM WVKFANLCRK
SGRLGLADKT LNSLMPDDIG PGGATGMTGP PEIIYAHLKY MWATGAREET LGFLRTFTSQ
RSNEVGLTSN MLLPESGSSS GNVSKDVRLL ARLYYKLGEW QSAMQDNWGS DAITDILQSY
LLATKLDPTW YKAWHAWALA NSEVVSHYAK SLNEQDQMAP QVFIDHLVPA VEAFFHSIAL
SPGNSLQDTL RLLTLWFKYG GDEKVYEAIM KGMKTVSVDT WLDVIPQLIA RIHAPSANVR
SLIDSVLTDV GKQHPQALVY PLTVASKYPS APRRSAAVAI IDKMKVHSEA LVAQALLVSQ
ELIRVAILWN ELWHEGLEEA SRLFYGDHNI DAMFATLAPL HDMLERGPET LREIAFAQTF
GRDLADAREA CNRYRQFGEI QDLNHAWDLY YQVFRKINKN LPTLTLLELQ YVSPKLLAVK
NLDLAIPGTY QTGKKIVRIA SFGPTSEVFT SKQRPRKLRI VGSDGVDYNF LLKGHEDLRQ
DERVMQLFGL VNTLLQKDSE TFKRHLTIVK YPVIPLSPNS GLLGWVNSTD TLHVLIKNYR
DSHKILLNIE HRLILQMAPD FDHLCLMQKL EVFEYSLDNT TGQDFYRVMW LKSRNSEAWL
DRRSNYCRTL AVMSMVGHIL GLGDRHPSNL LMDRVSGRIV HVDFGDCFEV AMQREKHPEK
VPFRLTRMLM SAMEVSGIEG TFKITCQHTM RVLRENKESI IAVLEAFVHD PLINWRLVQG
GRQIEGKVAA DNGGVGGARR PRGDETNIYD EDAVDQINTR AVQVVERVQQ KLTGRDFKAT
VELSVNDQVD KLIAQATSLE NLSQCFIGWC PFW
//
