ID A0A1I8F0N6_WUCBA Unreviewed; 2462 AA.
AC A0A1I8F0N6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-2.8-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-2.8-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-2.8-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 STRING; 6293.A0A1I8F0N6; -.
DR WBParaSite; maker-PairedContig_926-snap-gene-2.8-mRNA-1; maker-PairedContig_926-snap-gene-2.8-mRNA-1; maker-PairedContig_926-snap-gene-2.8.
DR GO; GO:0031931; C:TORC1 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:0048856; P:anatomical structure development; 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:0051247; P:positive regulation of protein metabolic process; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; 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; 3.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic 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; 2.
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; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1281..1940
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2114..2426
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2430..2462
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2462 AA; 279882 MW; 1E1115A57FC0B705 CRC64;
MDSCIRETSA RAIAADFLMR LRKKGGDENR LKVARQLYDY INGELRDSSD QFATEFFATF
DAKVDQSAIH TLMTSLDNDE RKAGIILIAC LVENAGDETK RVPRFAKYLL KALVQGDEAG
MKLVARAIAY LIQTSKTFAA ELVEKSINQV CEWLEESERH ESRRLAAVFL ARQLALYTST
SFFLRASNFF SNIFKVIRDP KATVRIAATK ALHAALTVTS QRETHQKSEW YWRCYDEAMN
SLKFDGLNRD ERQHPMLLIL NELLRIGNAP AERQRILALG CQPQQNVRTV IGSNAIDWLT
ERTYSVTVDS RTANQLIAEK FSDIYRVCNL ACTSRYVCCQ TTLLEIFPRL SSFGKTQMVT
SNELNIFDVD VASMFNHALN LTAKHSPAFF TLGLLVLDRP IELLLKLPRL FAVIQIQLQT
ATYKHKSVDE YVFLCLTLVI RALKEKIEFE IKTLLPILLS TGLTDVAYEI MQSIPGLKTE
AQDGLLKELC QLLMNRKLPS KLDPPTEPPI PAGPVNVTNV ALTNLALATL GRFEFQRHAL
QMFINYIAHG YLSSDCAEVR LAAVDCCAKM LTPFVRVFES FECANKKQRF DVLNLIQSVL
RQLVTCFKDG DPLLLSHLAQ ADMLDSIFMT LHDEKLEMQE HAVALLGKLG SLNPAYVLPS
LRNVLLETLT QLTNSGVPRL EEHSARVIAQ VAKQSPKFAK PYMNPILTAL VPKLSSEISH
VDVTVQVLNA ISELAVAGGA DLAALRTMGQ LCQNTAYVVD PYKEHPELLD VLLRLLRTEM
SVSMRRMTMR VLGIIGALDP YTHKVFTGKV SSQKSNSLAL SLPATSPSLD MRNDTIQWFH
YEKCTLAELY PAFSIASLMQ MLKDDALSHL HRDITQALLT IFGSLGPSCT LYVSKVIPRL
IEVIQTATRP DLKQFYLQQL ANFIAIVGSS MKPFMSKLFN LIRESWSEDV SMRLTIVNVM
QQIGAAFGAS FAPYIPELCP YLLSIVHSDR TKDRAITCAV FTCVQSISMC LTPHIHLVLP
PILFVLDDRS VKVEVRRIAL DTVYQMAETI CIRDHAPRIM QVWLRVISVH ALQQKLLLLL
VVIVRQMWRQ FLVFRKSVDC ALARHGLHCD EYLKLTVQLD EGSAASPSHS PSVRVSSSQV
KQFSTSVRHE KGQRINFDVL KRTWTTAQLV SKEDWDQWLV LLRIQFIRQS PSAALRACAP
LADVHISLAK DLFNAAFMSV WTDLDEMQQR DLETNLKYAL DSSNHTDIIQ TILNLAEFMD
HSEKKDSEKS FQGPLPVGSE RLCKCAEQTR AYAKALRYTE LNIREKFNRD PDPEHCRSLI
TYANKLNLQE EAAGIVAFAR QHNMEIGRQG RWYEKLNEWE KALEIYNNET FITDELYEHQ
MRCLEALGQW AELNDLGKKA FAEVGAAASA TRRQNMAITA ARGSWAIENW ETMDYYVKQI
NENNQDGSFL RAVLAIRNEQ YHDALAYIEK VRDMCDTELT AMASESYERA YGAMILVQQL
TELEEAIEYK MWPDRRIRIA VVWSRRLQGC RPNIEQWQRL LLVKSLVLSR NEMRPLWIKF
SSLCRQYGKL SMSRRILADL LGLKRNEELH EISDLPMDKP SLVLAVCKQY WAENLNELAC
NTLEKLINQF EIEKREIKKN SEICRLMAKC CLKLGDWYDT LPQPTKDIQT MNINVQQSLQ
PISIPQQSPT NSSIMINVPP LLLPSSYVQI SPPPIIPPSS HVVQSLQPSL SPPLTQTMKF
YTNATVYDPT WYKAWHKLAS AYFNAAMYQT QNSFSPAPPP PPFIGAMPSS PSYSPFGSII
DRDILSDILI PELYPQPPPS DAVIVNPPSP APNQAMIFFA KQAVSSFINA VTLAEGSRLE
DTLRFLTLWF KHGDQVEVFE TIKESLKLLP VEMWLEVIPQ LMARLDSKQN VAQLIKEVVI
DLSKVHPQSL VYALTVAAKS ANLRRSAVAT EILTIMSDSQ STLVEQAKLV SDELIRCAIL
WHEQWHEALD DASRLYFQDK NVKAMFDLLK PLHDLIDRGA TTLKEQSFKQ TYENELKEAW
NACRCYLRSQ NAKELNQAWD LYYIVFRKIS SQLRQLTSLD LNYVSPRLVK ARDLELAVPG
TYDPSAALVT ISSISNTLQV INSKQRPRKV VMKGSDGKDY IFLLKGHEDP RQDERVMQLF
GLVNTLLLHQ GDTSRRNLTI QRYSIIALSQ NSGLIGWVPN CDTLHSLIRD YREKKGILLS
MEHKIMQNFA HDLDQMTLLQ KVFHHALEMT SGNDLQQILW LKSPNSEIWF DRRTNYTRSM
ACMSMVGYIL GLGDRHPSNL MLDRISGKIV HIDFGDCFEV AMTREKFPEK IPFRLTRMLI
QAMEATGIEG NYRITCERVL RVLRSNKESL LAVLEAFVYD PLINWRLMEA GGRRPPPETL
QKDGQTDSKA ESSLKRIKQK LAGRDFNPNV EFSIPEQVSL LIEQAVLAEN LCQCYIGWCP
FW
//
