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Database: UniProt
Entry: G3VY68_SARHA
LinkDB: G3VY68_SARHA
Original site: G3VY68_SARHA 
ID   G3VY68_SARHA            Unreviewed;       705 AA.
AC   G3VY68;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=TANK binding kinase 1 {ECO:0000313|Ensembl:ENSSHAP00000008123.2};
GN   Name=TBK1 {ECO:0000313|Ensembl:ENSSHAP00000008123.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000008123.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000008123.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000008123.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3VY68; -.
DR   Ensembl; ENSSHAT00000008190.2; ENSSHAP00000008123.2; ENSSHAG00000007043.2.
DR   GeneTree; ENSGT00950000182937; -.
DR   HOGENOM; CLU_004414_1_0_1; -.
DR   InParanoid; G3VY68; -.
DR   OrthoDB; 2546268at2759; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:Ensembl.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR   GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0044565; P:dendritic cell proliferation; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   CDD; cd13988; STKc_TBK1; 1.
DR   CDD; cd17127; Ubl_TBK1; 1.
DR   Gene3D; 1.20.1270.420; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR041309; TBK1_CCD1.
DR   InterPro; IPR041087; TBK1_ULD.
DR   PANTHER; PTHR22969; IKB KINASE; 1.
DR   PANTHER; PTHR22969:SF14; SERINE_THREONINE-PROTEIN KINASE TBK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18394; TBK1_CCD1; 1.
DR   Pfam; PF18396; TBK1_ULD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..310
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          616..643
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   705 AA;  80547 MW;  55F422A7458CA0C5 CRC64;
     MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLFAVKVF NSISFLRPVD VQMREFEVLK
     KLNHKNIVKL FAIEEETTTR HKVLVMEFCP CGSLYTVLEE PSNAYGLPES EFLIVLRDVV
     GGMNHLRENG IVHRDIKPGN IMRVIGEDGQ SVYKLTDFGA ARVLEDDEQF VSLYGTEEYL
     HPDMYERAVL RKDHQKKYGA TVDLWSIGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG
     KPSGAISGVQ KAENGPIDWS ADMPVSCSLS RGLQVLLTPV LANILEADQE KCWGFDQFFA
     ETSDILHRMI VHVFSLQQMT AHKIYIHSCN TATVFHDLVY KQTKIVSSNQ ELIYEGRRLV
     LEPGRLAQHF PKTTEENPII VISREPMSIV GLMYEKISLP KVHPRYDLDG DASMAKVITG
     VVCYACRVAS TLLLYQELMR KGIRWLIELI KEDYNETIHK KTEVVIALDF CIRNIEKTVK
     IYEKLMQIDL EAAELGEISD IHTKLLRLSS SQGTIETSLQ DIKSKLSPGG LLADTWANQE
     GTHPKDRNVE KLQVLLNCIT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YFYATKAMSH
     FTDECVEKYE TFLDKAEEWM RKMLHLRKQL SSLTNQCFDM EEEVSKYQDY TNELQETLPQ
     KLFAASSGIK HTMAPIYPSS NTLVEMTLGF GALTMDGGLR NVDCL
//
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