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Entry: A0A371DBG9_9APHY
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ID   A0A371DBG9_9APHY        Unreviewed;       822 AA.
AC   A0A371DBG9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   RecName: Full=Fungal-type protein kinase domain-containing protein {ECO:0000259|Pfam:PF17667};
GN   ORFNames=OH76DRAFT_1482696 {ECO:0000313|EMBL:RDX49876.1};
OS   Polyporus brumalis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX49876.1, ECO:0000313|Proteomes:UP000256964};
RN   [1] {ECO:0000313|EMBL:RDX49876.1, ECO:0000313|Proteomes:UP000256964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX49876.1,
RC   ECO:0000313|Proteomes:UP000256964};
RX   PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA   Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA   Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA   Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA   Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT   "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT   exposes the biotechnological potential of its oxidative enzymes for
RT   delignifying raw plant biomass.";
RL   Biotechnol. Biofuels 11:201-201(2018).
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DR   EMBL; KZ857402; RDX49876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371DBG9; -.
DR   Proteomes; UP000256964; Unassembled WGS sequence.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR040976; Pkinase_fungal.
DR   PANTHER; PTHR38248:SF2; FUNK1 11; 1.
DR   PANTHER; PTHR38248; FUNK1 6; 1.
DR   Pfam; PF17667; Pkinase_fungal; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT   DOMAIN          201..584
FT                   /note="Fungal-type protein kinase"
FT                   /evidence="ECO:0000259|Pfam:PF17667"
FT   REGION          704..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..787
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..822
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  92450 MW;  BB76EFC9E20C5C4F CRC64;
     MSSVSFSYDV PVALDSPLST TDRLDPSSLR SRNLNNAASL KTRTLGPMPL QEFMDYYLPK
     RYTGDSSRLL SSRHAFKSVP TRAESMPTTC GALVLALNRH TKHKSRCPGF VFEVAATPDG
     AAVDSGDRTP HILCYATDNL DQVRQAGVGS RVEFGYAELF IEVAADPSHD CFADPLASSD
     DDLRATYDLW TRPQAHGDAT SPREAFGQHV AHVAEVFARQ HRISFYSIAI FGSFARIFRW
     ERSGCVVTES FDIHEHPNLL CDFLWRFSQV PHAIRGHDMS VEAARPEEEG TFRDVITAHV
     QFQLDLHPED LDKAVKAHYE PGRVFAVHVI PQHFSSHPEN IRRFIVSRPV VSPSSLIGRG
     TRGYWALDTS TGQVVFLKDT WRFMKSEELE GDTIRRLVDL GVRQIPSLVW HGDIPYHIPN
     IPVPRQIESK EMQQTTVHTL LADRWLCHGS VVQLDIPHRQ HYRLITNVAG YPLETIRGAE
     ELLYAAYDTF TAMRDALAKD ARIHRDISVG NIILVKESDR AVRRGYLIDW EASCRIDDKG
     NARLSGRVGT WAFMSMRMLA VSRLSTCKQT FRDDMESLLY VVLYCALLWQ PHNFPRQELT
     KIVASFFDGS QRVGDVYMGG GAKSANALSR TYTGSMQLGS EALQEWLTTV LNFHWPPQDA
     EEYQGKWTAE HLDTYWAAFL RTHTLERDNR VVHAVDAPIY RPSSTPSIAY IPRSPPSSVE
     LLPTPPSARS RLSSTRPPTP ASRAKRMRAP SSDVVLPTVS EPRTKRTRSK AVIDISSLRR
     SRRLQEKQDQ NPQASASGNT SNGPPRRSGN PKRRRSGAAS RK
//
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