ID   A0A0G4ES84_VITBC        Unreviewed;       970 AA.
AC   A0A0G4ES84;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=Vbra_12800 {ECO:0000313|EMBL:CEM00531.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM00531.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM00531.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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DR   EMBL; CDMY01000295; CEM00531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4ES84; -.
DR   STRING; 1169540.A0A0G4ES84; -.
DR   VEuPathDB; CryptoDB:Vbra_12800; -.
DR   InParanoid; A0A0G4ES84; -.
DR   OMA; FEWLSAE; -.
DR   OrthoDB; 668390at2759; -.
DR   PhylomeDB; A0A0G4ES84; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF118; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254}.
FT   DOMAIN          327..680
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          717..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   970 AA;  106573 MW;  985F7270112285E9 CRC64;
     MKYGEPWQWS SPTPTAASAG VVAQLKTALE SSVDSARGAL SSLGDSWNAL VSSAVPKMTG
     ASGGGAVDLI KAEEALKQKI AASMDLDPST VQIDPSSPFI TVREQLVDLL SNIPPELNID
     TSGFRETTLA TLDFYNWLWS VYPIPNKAEI KNALVFLAQA DAAAVALDLV LGGIFVYSLT
     KGFGKGKLSA DDGPPPRYNI TDYERFFAQR RDVVTDRVTE LLWRGGGLAW KIWRDTKGRD
     YETNEPKRAQ ELRELITDLG PAFIKIGQGV SVRPDLLSET YLRELQKLQD RVPPFGADEA
     KQVLLKELQA AGGSPDQTLE DYFEDVSVFD EPVAAASLGQ VYKAKWKRTG KTVAVKIQRP
     DLLAKCSLDL FVIRKALSLG AAASFLPKRT RDSCRSFGKV IDNAGARFIE ELDYMKEAAN
     QRRFKEEVEA NALLDGSIVV PGVVKASQFV LVTEWIDGQK LTDLSIKEDD TPATKADKEV
     VLEKVVKSLL NCYLVQLLET GWLHADPHPG NFLRTADGRL CVLDFGLMTE IKPDQRVALV
     EYVAHLSARD YDKALNDLIT LGFIPPEIGA DPEKRAIVVP LLSNVLGQLA NGGGASGINV
     ESVGRDVEEL SKQYPISIPS YFGLIVRAFG TLEGLGLGLD KQFSILSECL PYLAKRLLTD
     DSPRVREALR SFLYGKQNYL DPERVNQILQ GYTSFTLDVT DPSTFLGAGL SEEQQEQVLT
     ATGQRARPPP GSPQARASET LANRLAAFQV DETTKELLEI LLAPEGNFVQ DLVLDEAVRL
     TDAVTRTTAG GAARAVRSAT DSIQQQFTNL SPAALFLLPI LPQATVANAI SRSVEELNQP
     TEEDAKTIQT AQQVLRAIAP NALTTSLRRQ LAPTALRNFQ PAEDDDRRRA DGRNRRPTFV
     QTLERARERR RERRRLALAQ LNALQEVSRV LNDLSPGITT VVDKFARKLT RRVLQRLAND
     LLAGKEEGKR
//