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Database: UniProt
Entry: T1K684_TETUR
LinkDB: T1K684_TETUR
Original site: T1K684_TETUR 
ID   T1K684_TETUR            Unreviewed;      1042 AA.
AC   T1K684;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN   Name=107360633 {ECO:0000313|EnsemblMetazoa:tetur05g08980.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur05g08980.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur05g08980.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804}.
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DR   EMBL; CAEY01001593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015782813.1; XM_015927327.1.
DR   AlphaFoldDB; T1K684; -.
DR   STRING; 32264.T1K684; -.
DR   EnsemblMetazoa; tetur05g08980.1; tetur05g08980.1; tetur05g08980.
DR   GeneID; 107360633; -.
DR   KEGG; tut:107360633; -.
DR   eggNOG; KOG0603; Eukaryota.
DR   HOGENOM; CLU_000288_58_0_1; -.
DR   OMA; HQAHKEG; -.
DR   OrthoDB; 5489497at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 3.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 3.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000606-
KW   51}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000606-51};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          279..349
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          616..934
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          373..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          945..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..457
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        732
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         14..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         622..630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1042 AA;  116566 MW;  996A24E94F53A526 CRC64;
     MPVDIDDFEI LKVLGTGAYG KVFLVRKLCG PDINHLYAMK TLKKSSLVNK PKTLEHTLIE
     RKVLEIVRSG PFLATLHYAF QTSDRLHLVM DYISGGEMFT HLYQRDRFTE DAVRIYIAEI
     VLAIEHLHKH NIVYRDIKLE NVLLDKDGHI VLTDFGLSKM FKENSENNRT HSFCGTIEYM
     APEVVRHGSG GHEFAVDWWS VGVLTYELLT GASPFTLEGC PNVQAEITAR IIHDRPPIPE
     YMSNVAVDFI LKLLAKDPRR RLGAGRYGAS EIKRHPFFGN LNWTHLAEKR VRAPFVPKIN
     GDTDTSNFSD EFTSMSLVET PDISPPEEVP ENSFNGYEYI SPDLIAANRF YYGEAAVPIE
     EVQNQEVIEY VNSEQSEDEE EIQEEDEESV QNSYASSEEE GETVDESSEE EQESEDNNDD
     NSDDSEEDED EEEEEEEEED EEDDEEEEDE EENVSTIDED SISTIGEESS VTEEVEENTL
     DNLAHRLNQP LLDASTIPVP EESFESSTSS TQRDINEIFG SSMSSNGSII GSINSHHNLS
     PKRSVSGSSF DIDVQLHHSN YIMTSTPANP KRKFTRKTDN QHHPISPPSP ISPSPKNVLY
     TLRITANSVF HQKYSLTLNS VLGDGTYSIC TKCVDRKTGE EFAVKIVHKQ SDITSEVESL
     NMCQGHPNIV NLVEVLTDDY YTYIVQELLR GGELLAKVGS NGAFSEVEAS RLFRGLVSAL
     NYMHTNQVVH RDIKPENLIF TDDSPDAELK IIDFGFACKI SRNEVLKSPC CTFVYAAPEV
     LKIAKKLSAN ESRTYPTSSF TSSSDRYSSS SPPSTPPALS QSIQEQLANI PFVVNRSPDS
     DRSYHREDGY TESCDLWSLG AVLFTMLGGN PPFAHVHDLS ASDVLEGIKN GAFDMNGPNW
     AKVSTAAKSL ISGLLDVNPA ARLKLSYLTC HPWVQGHFNE SSMNISYRRT PSTPPGTYLR
     QGSPGSTPVP TVGSLRLADV SEAILAKRRA CKRLFIDNNG NDCSPHIESS HKRIKTVLTR
     EYNSLNNNLF LFKAHPLLST KN
//
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