ID A0A0L8HK54_OCTBM Unreviewed; 2497 AA.
AC A0A0L8HK54;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=OCBIM_22013564mg {ECO:0000313|EMBL:KOF89145.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89145.1};
RN [1] {ECO:0000313|EMBL:KOF89145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF89145.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF89145.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ418038; KOF89145.1; -; Genomic_DNA.
DR RefSeq; XP_014771975.1; XM_014916489.1.
DR STRING; 37653.A0A0L8HK54; -.
DR EnsemblMetazoa; Ocbimv22013564m; Ocbimv22013564m.p; Ocbimv22013564m.g.
DR EnsemblMetazoa; XM_014916489.1; XP_014771975.1; LOC106870424.
DR GeneID; 106870424; -.
DR KEGG; obi:106870424; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
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: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; 4.
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; 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; 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 1349..1920
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2094..2409
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2465..2497
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1198..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2497 AA; 283898 MW; 4423E19FB72F14CA CRC64;
MTSKHITPFI TGLRSRNDES RLATAYELYR YVNTDVPEMP LDDQNAFIDE INHNVFEMVS
SSEVHEKKGG ILAIATLVGV DIGNAATKIS RFANYLRNLV PSSDVGLMEM TAKGMGILAL
SAGNHAAEYV DFETKRSLEL LAGERHEGQR YSAVLILKEL ATFTPTFFFQ QVPQFFENIF
NAVRDPKPAV REAAVAALRA TLAVTSQRET KRDHSEDWYK TCLEEALRPY SDALAKEKRL
NKDDWLHGSL LIINELLRCS NMEGERLRVE MEDLAIQQNT FEKAVKEFSP RRRSPANTSG
FQQLHQKSPL IVFDASHASA PQKRGLFESR VCKELMTKNY DKVANLVHQL YQGNRSSYVQ
QVMLKAIPRL AAFDPELFSR TYLRDTIVYL LNALRRDKER AAAFQAVGLL AVAVKDNIFS
FCNRIMEFVR SALPPKDLPQ KKQKAISVEP SVFTCISMLG RALETSIARD MKDILDSMLF
TGLSPALTAA LRDLATYIPQ MKKDIQDGLL RMLSLILIGR PLQHPGAPKN LPIGSSAGSD
SQDDTSITLA LSTLGSFDFE GHSLTQFVLH CAENYLCSRS KKIRSEAIRT CARLLIPLLT
ALEGQQKHSM KTMNTVADVL KKLLIVGITD PEPEIRYCVL SVLDERFDPH LAQAENLNAL
FVVLNDEVFE IRELAICIIG RLSNRNPAYI MPTLRKTLIQ ILTELEHSGV GRSKEQAARV
LGHLASNASR LIRPYAEPIL KVLIPKLKEP DPHPGVTISV LAAIGEQAEV SGLEMRKWVD
ELLPIILNTL QDLTSVEKRE VSLWTLGQLI ESTGYVVEPY QKYPALLGIL LNFMKTEQTH
SVRREVVRVL GILGALDPHK NKLNVSRMKE ESGLTLSGAS IDSFVINKSS SDSQTSIPLA
DYSTNELLVM MGAPTSLEDF YPAVVVSALM RIMRKACFSS DHSLLIQSIS FIFKSLGSRN
VPYFDQIVNA YVTVTRKAEV NVKEFMFQQL GFLVTFAKQH VRNFLGDIFQ LIKENWTMKS
QDQNIYLSLL EQLVHAVGSE VKPHLPQIVP QILRILMYDT SKQREYTLQL LEVLQLFGSS
LDDCLHVLLP YIIKLFDSND VPLNVRKMAL ETVDVFTEDL DMTDFASRLV HSFVRTIDST
PELIPTTMDT MCSMMLQLGQ KFLLFVPMVN KTVVRHKIVH QRFEIILTKI TKGGLGDEAP
EGLLTRRRQR KRKDSNAENT SELPMSKKLH VFFTNLQKVL TPARRVSKED WNEWLRQLNI
ELLKESPVPS LRSCWALAQV HNQLARDLLN PAFVSCWTNL NESQQDELVQ CLENALNSQE
IPEVTQTLLN LAEFVEHCDK GPLPLELKVL SQRAMRCRAY AKALHYKEDE FHRAHTRETL
EALISINNKL QQHEAAAGVL EYARKNRLAD LIEETWYEKL HEWEKALKAY EKKQETHPDD
KNCILGRMRC LEALAEWGSL NQLASDTWCI ANDELRTKMA QLATAAAWGL GDWNSMEDYL
TFIPRNTYEN FFYRAVFSVH NENYSQAFQF IDKARDILDT ELTAMAGESY ARAYGPMVNA
QMLSELEEVI QYKLIPERRD VIKQMWWDRL QGCQRVVEDW QKIIQVRSLV ISPLEGVKTW
LKYASLCRKS GRLALSQKTL EMLMGVDLSK QSNNNLPTDM PMVTFAYIKH MWLCNQKQDS
FAALQQFIHQ TQRQSEVLLS TGDAAAVTEL RKLLARCYLK QGDWLLELNG IDDSSIAKAL
DSFKMAQDRN KNWYKAWHAL ALTYYEAVLY YKKKEMSAAN LSASSASQTE GAVATGKEAP
PDIGMKAQSH NTPNILLHCV PAVRALFKAI SLSNQNSLQD TLRLLTLWFD YGHYSEVHES
LIEGIKTMQI ENWLQVIPQL IARIDTPRHS VGRLISQLLI DIGKAHPQAL IYPLTVASKS
SVLARQAAAN KVLKSMCEHS NTLVKQAVLV SEELIRVAIL WHELWHEGLE EASRLYFGEK
NIKGMFETLE PLHRMMDRGP QTMKEISFSQ AYGRDLLEAQ EWCKIYQRSA LLKDLTQAWD
LYYQVFRRIT KQLPQLTSLE LQYMSPNLLR CQDLELAVPG TYDPNQPVVC IHHVQTTLQV
ITSKQRPRKL SIYGSDGKDY VFLLKGHEDL RQDERVMQLF VLVNSLLANN PKTFRRNLSI
TRYAVIPLST NSGLIGWVPH CDTLHSLIRD YREKKKILLN IEHRLMLRMA PDYDHLTLME
KVEVFEHALE HTQGDDLAKI LWYKSPSSEV WFDRRTNYTR SLAVMSMVGY ILGLGDRHPS
NLMLDRMSGK IIHIDFGDCF EVAMTREKFP EKIPFRLTRM LINAMEVTGI DGIYRHTCES
VMSVLREYKD SLMAVLEAFV YDPLLNWRLM DANDKPKGKA ETSDSMPSSQ ERGEHLMEAG
DMQTTHKKTT GQNTTVAAAT AAAAAPEMIH SLSDTVQPEA LNKKAISIIN HVKEKLTGRD
FSKEEAVEVS RQVDLLICQA TSHENLCQCY IGWCPFW
//
