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Database: UniProt
Entry: A0A2A9NZ65_9AGAR
LinkDB: A0A2A9NZ65_9AGAR
Original site: A0A2A9NZ65_9AGAR 
ID   A0A2A9NZ65_9AGAR        Unreviewed;       529 AA.
AC   A0A2A9NZ65;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AMATHDRAFT_55689 {ECO:0000313|EMBL:PFH53192.1};
OS   Amanita thiersii Skay4041.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX   NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH53192.1, ECO:0000313|Proteomes:UP000242287};
RN   [1] {ECO:0000313|EMBL:PFH53192.1, ECO:0000313|Proteomes:UP000242287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKay4041 {ECO:0000313|EMBL:PFH53192.1,
RC   ECO:0000313|Proteomes:UP000242287};
RG   DOE Joint Genome Institute;
RA   Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA   Pringle A.;
RT   "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT   fungi.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ301975; PFH53192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9NZ65; -.
DR   STRING; 703135.A0A2A9NZ65; -.
DR   OrthoDB; 1534388at2759; -.
DR   Proteomes; UP000242287; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd14127; STKc_CK1_fungal; 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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR11909:SF155; GILGAMESH, ISOFORM L; 1.
DR   Pfam; PF00069; Pkinase; 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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000242287}.
FT   DOMAIN          28..312
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   529 AA;  58679 MW;  15031B4E3DE491B9 CRC64;
     MTTPHVIASS SSHPSQSLTA SNVVGGHYRV GKKIGEGSFG VVFEGTKLMS NTPVAIKFEP
     RKSDAPQLRD EFRSYRTLSG TPGVPQVHHF GQEGLHNVLV IDLLGPNLED LFDMCGRKFT
     IKTVCMAAKQ MITRVQAVHD KSLIYRDIKP DNFLIGVPGT KNANMIHIID FGMAKHYRDP
     KTKVHIPYRE RKSLSGTARY MSINTHLGRE QSRRDDLESL GHVFMYFLRG GLPWQGLRAA
     TNKQKYEKIG EKKQSTPINE LCEGFPEEFA IYMNYVRKLG FEETPDYDFL RELFTKVLKT
     QGESEDGVYD WMLLNGGKGW EASTKPHVHS SATPGREHRR ERDAAGHRRA SRQLQDNSAP
     LVLSPTPAHV SKSRRANGER GNSRDISSVQ PLVPASRRPS QQRDPNLLNS SGLTTPHPYA
     TAPSPNGYRN STGGAYGRHS PNAQAHALPN GNALHSNPSE SYIYGQNVAG KTATVSRENT
     TGGTAPRDPA VAVRGMAVYD GEHMQRVGED EEDGHGRRRG FWSILCCRA
//
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