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Database: UniProt
Entry: A0A137Q692_9AGAR
LinkDB: A0A137Q692_9AGAR
Original site: A0A137Q692_9AGAR 
ID   A0A137Q692_9AGAR        Unreviewed;       825 AA.
AC   A0A137Q692;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-type protein kinase domain-containing protein {ECO:0000259|PROSITE:PS51158};
GN   ORFNames=AN958_02229 {ECO:0000313|EMBL:KXN82716.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN82716.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN82716.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN82716.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ962926; KXN82716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137Q692; -.
DR   STRING; 1714833.A0A137Q692; -.
DR   OrthoDB; 1663818at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR   InterPro; IPR004166; a-kinase_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF02816; Alpha_kinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51158; ALPHA_KINASE; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          574..812
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
FT   REGION          338..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  90888 MW;  A1D2C3798BDC6D2C CRC64;
     MLPHAKFTTK VVENKNGFLC GRCGISVPPG IVPGIIASNV PTEEARVTCP SCTKHYIAKG
     IAMKELTIDV EQVFQTASQA NHYTQMQQNF TPSRSTRETE HSFRAPAPQQ IQNNGMMKTV
     YSSSGQSIPY NASAIQNSVN ASQCTGVDYA GPSGRITPIG SVQVSSTSCP NVHDPRHFRE
     FDRRFIPEAM SGYTKEHLAL ELQHQVHSLV LTHLELLISG LQLDVSQMPV YKSLTSIPVL
     ENPNDTSASY FRNRFFVATS KGLDVFKPKK TEFYVEISND EWTILLKYNN LIRSMSPEDA
     ELETMLSLTR QTIRTPITIR LRNINILCFQ AALEASSEAG DTETSSPAKS PRKKSSKRGH
     KVQQDSSLGS PQAPAPKCSC PASTQAARPP KPSIPISTLP PESVYSDPSI PANTWPTVSA
     YSGEEPVLYT QQRTVSSMED SEKETQSPPS FGSSGEINAP TQPPQASVTA SVGDTTVERD
     IETSDEGGEE FEGWTEDDVQ VAMLSGGRLG NLNLDVIIGG HITDNVAIYP IKRLPFASII
     QISLAGELPF SLKPGDAQFG LLEYDRTDAV GQGAFKVTFA CWFSLQTLLP VSQDKSARML
     ALKRVFKPAR KKPAIVTLPG STHTPTTPSP PAPIPLKDLK FWPKRDELMR ICAEATTLGW
     ATSLVLMAYD FIENVIKQKG VQPPWPIPQL WMVKGYVCAY LLEEFIQGDE LLFLKYILNS
     QAVLLLPPTH KQYKIAEFLC FMQHVQWVKT NGIAFMSDFQ GGKTLLTDPQ IMTHLEKLSG
     TFCEGNLKVA FHQFPCQHEC NKYCEWFGLE RLIVSGIDKG AGVAG
//
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