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Database: UniProt
Entry: A0A1V9XR74_9ACAR
LinkDB: A0A1V9XR74_9ACAR
Original site: A0A1V9XR74_9ACAR 
ID   A0A1V9XR74_9ACAR        Unreviewed;       358 AA.
AC   A0A1V9XR74;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQR75892.1};
GN   ORFNames=BIW11_08131 {ECO:0000313|EMBL:OQR75892.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR75892.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR75892.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR75892.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
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=2.7.11.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQR75892.1}.
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DR   EMBL; MNPL01005627; OQR75892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9XR74; -.
DR   STRING; 418985.A0A1V9XR74; -.
DR   InParanoid; A0A1V9XR74; -.
DR   OrthoDB; 2723903at2759; -.
DR   Proteomes; UP000192247; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF238; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          32..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          290..358
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   358 AA;  41755 MW;  AA80E84A04C65CF8 CRC64;
     MLERSATDEI PRLKGSEQQP IIRFRKYSLL DFNLLKVLGK GSFGKVFLVE LRDVPVYFAM
     KCLKKDVVLE DDDVECTLVE RQILSLGSHN PFVCKLFCTF QTESHLFFVM EFLRGGDLMF
     HVQNEGSFTE ERARFYGAEI VCALKFLHRR GIVYRDLKLD NVCLDGDGHI RLIDFGMCVL
     RVYRYEPTAF CGTPEYMAPE IIEGKQYNYA VDWWSFGVVM YEMLRGRSPY TGCDEDELFW
     NVMNTEVEYP KYFSREAKDL IQNLLQRDPD YRLGMPECGR GDIRDHPFFD GISWSQVEKK
     QLTPHFKPFI HGASDVSNFD EDFTREPAIL TPVEDNVLAT MDQEVFKDFN YTNPNMTT
//
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