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Database: UniProt
Entry: A0A0C2CMS9_9BILA
LinkDB: A0A0C2CMS9_9BILA
Original site: A0A0C2CMS9_9BILA 
ID   A0A0C2CMS9_9BILA        Unreviewed;       311 AA.
AC   A0A0C2CMS9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=ANCDUO_18849 {ECO:0000313|EMBL:KIH51067.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH51067.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH51067.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH51067.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364109};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|RuleBase:RU364109}.
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DR   EMBL; KN747750; KIH51067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2CMS9; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR040122; Importin_beta.
DR   InterPro; IPR024585; mTOR_dom.
DR   PANTHER; PTHR10527; IMPORTIN BETA; 1.
DR   PANTHER; PTHR10527:SF5; IMPORTIN-5 ISOFORM X1; 1.
DR   Pfam; PF11865; DUF3385; 1.
DR   SMART; SM01346; DUF3385; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364109};
KW   Kinase {ECO:0000256|RuleBase:RU364109};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW   Transferase {ECO:0000256|RuleBase:RU364109}.
FT   DOMAIN          66..237
FT                   /note="Serine/threonine-protein kinase mTOR"
FT                   /evidence="ECO:0000259|SMART:SM01346"
SQ   SEQUENCE   311 AA;  35103 MW;  893C7B12D931834D CRC64;
     MKHVDVTVHV LHAISELCVV GGAEIVRNID PLFQKLTQLI NDSSSLQRRE AALRTIGRIA
     RSTAYVVDPY KDYPNLLDDL LRLLKTEMSS KMRRQAISTL GILGALDPYT HKVFTGAVQS
     ATSISTALSL PMARDAADPR QDIIQWYNYE KCTLEEFYPA ITIANLMVMV QDEAFTQYYK
     EIAQALLTIF RSLGDSFPQY VQQVVPRLIE VTRACRGRPS HREFFLRQLA SLVAIIKVHA
     KPYMKQIFSL IADAWSEDQS VKVTVVSVLE QIGTALGQEF APHIAELIPY LLYVVQTDKS
     EDRKLTAQVR S
//
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