ID A0A0D1YB19_9EURO Unreviewed; 798 AA.
AC A0A0D1YB19;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PV11_09755 {ECO:0000313|EMBL:KIV77984.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77984.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77984.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77984.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846954; KIV77984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YB19; -.
DR STRING; 1016849.A0A0D1YB19; -.
DR HOGENOM; CLU_010392_1_2_1; -.
DR OrthoDB; 1508at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR12984:SF3; N-TERMINAL KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR12984; SCY1-RELATED S/T PROTEIN KINASE-LIKE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 6..312
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 548..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 85679 MW; 2F2D976181A999D9 CRC64;
MDFLKSAVAS AIAKSSSFPV IIGDRVDAGE SIFALHNGTK KDDNTACSLF TFDVNANKSR
LPLAKNAARK LRTLRHPGVI RVIDVIENET HIYIVTERLT PLSWHIKRKS LSEETIKWGL
YGISSTLKFI NNEASSVHGA VRVPSIFTSD SGEWKLGGFE VLSSMNEDDA IIYTYGSLLP
DSNRYAPPEV VNGGWSAIKK NPLGAPDAYG LGTLIFEAFN GSFSGNDQLS QPGRIPGNMV
QSYRRLINAN AKLRLTAGHF VDQGKKTNGF FETPLIHITE GADNLGLKSE DERDQFLAEL
DELTDDFPED FFKMKILPEL LKSVEFGGGG PSVFGAIMKI GLKMSDDEFE TRLSPVILRL
FASPDRAMRV CLLDNLPIMV DRIPQKDING KVWPAMTTGF TDAAPIVREQ TVKGVLSVIS
KLSDRIINGE LLRHLAKTAN DEQPGIRTNT TICLGKIARN LGVGSRSKVL IAAFTRALRD
PFVHGRNAAL MALTATIDVF NDDDCATKIL PMICISLIDK EKLVREQANK AVDAYLGRVR
KYATTLPDTV LPPESAPSTA GPAAAAAPAR MGNQNDTSWA GWAISSFTNK MAGASGEMSA
STATNGANLT QTQSLPASGR ATPSVNVISE KPVAVSRPPI SDTARSSTSQ PPEPEDIFED
DNAGAWGTMD DDGDNFFDAS SNQHTKTSTA APAAAFDDGG EPDFAGWLAA QSKTKSQKPL
PKGLGKPGSA GSGLSVRPTA PARSISAGPG AGVNNVKRPT IPAARTIATT SLKKEIKTEL
PKPKQPEPTD DDWGADWD
//