ID A0A165XR22_9AGAM Unreviewed; 821 AA.
AC A0A165XR22;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=SISSUDRAFT_1055505 {ECO:0000313|EMBL:KZT32454.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT32454.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT32454.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT32454.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV428331; KZT32454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165XR22; -.
DR STRING; 1314776.A0A165XR22; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
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.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT DOMAIN 316..667
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 92897 MW; C2BC1B11B82B6FAE CRC64;
MEDSTGHSLT PSLQRRIADI IEDTPRSAPT TGGVPSATER NESIEPVLRT ELADGLSLDA
DDFFDKILHC DRYTKQQVKR CFTALVMQNL YDDVKKQFDI PSSGLEKDMY PPLIKVINAI
TKSAKEGGVP DVDETIWREV HRGIQGKDPN HQSIFPDIAG AKRTQGPANP LLEAAIKAAS
DEILSWQLIG NICEVKTHAN KDTDTELHLQ LAKYARKVLM YQRGRRRFVL GWTLCGDVVR
AWLFDRAGGL SSRSFNYHAD PDLFIRMIIS LSSMSSEELG YDPTITQNPD GKLILDFTYR
DSDGKFQTEK YVITESIVPR PSLRGRGTVV WRAYKLSDEG VPEAERQYYA IKDSWRDLHR
DRNEGYFFEQ IEGLGPKDGV VKFIQFAAVE IGNKTAAKRP DTIETTVRQG VQGSRGSEFD
HRGHVRLLME EVGVTLDGFA SLRELIGVLM DAIQGHRNLM NKNILHRDVS FGNILMTEET
DEELGRRRGY LIDLDFAKDL TPKANDQEDR EDAESAKKGK KGKKARVTGT LPFIAIDVLC
TDENHRDVHD LESFFWVLLW MCLKYLGPHF NPIKPRPESE DVQPYRALRR LLVCCDLREG
GHNKLSILRE CQNQNDIADM INPYFHDLIP CIQSLAVIIS RGQTRDIDVR IGIPPVTNDE
RTYDKFLEIL KETYDGLPEF EALHVDVETN NLIERFKQAR LDSKLDAEEE EQLFTDREQS
LGSFEQYQRS RSYSRPATPT RGKSRTTRAP PAPRAKAKHT PQQEPIFATG LSATQPAEPI
QRMTRSRSRA AAQVPQGANA TDQPVEGGSK PKTTKSTTKK R
//