ID A0A165J6D7_EXIGL Unreviewed; 611 AA.
AC A0A165J6D7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinase-like protein {ECO:0000313|EMBL:KZV94395.1};
GN ORFNames=EXIGLDRAFT_708818 {ECO:0000313|EMBL:KZV94395.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV94395.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV94395.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV94395.1,
RC ECO:0000313|Proteomes:UP000077266};
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; KV425973; KZV94395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165J6D7; -.
DR STRING; 1314781.A0A165J6D7; -.
DR InParanoid; A0A165J6D7; -.
DR OrthoDB; 1615835at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04515; Alpha_kinase; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR45992:SF2; EUKARYOTIC ELONGATION FACTOR 2 KINASE; 1.
DR PANTHER; PTHR45992; EUKARYOTIC ELONGATION FACTOR 2 KINASE-RELATED; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZV94395.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 363..606
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 311..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 67184 MW; C434A3FA33B50711 CRC64;
MSFCELCSRP VNPQSLDPKR CFDCSRNAPL PAQACTVCGV QYPRLQGDTC FACSEGTSRA
EVEYQNGLNA TLRYHMEQPA SAVQLGQNRH RRPKGNGINA AAYAGSDPAY RARAEAMVSG
LTQGYGAALL QNEASGNPQR PVQRPKVFQS PVPIPAMKSM RISVQIERMK CGKTVLDALA
FEKQFYGSDR WGDVENKMKA MAIESVREFG VNAVSTDLRF GVGSRGKLLL DGEHSLPDMS
LQQVFNWHQA NGSSYITKNQ VTRTLFALTA NFNLPPPPKN FNADVRAPLL WSRYPLTSEL
KGTSRAYTTV TTTAATRSAA TKRQRSDDNN NDSERFLETR PRKRAYATIA PPQREHVTVT
ESRLALTTGS ENRQITQLPD ETGIAVSIDK EPSCRGASKE VYKLYRGQSG EVWAAKRFFA
IGPANAFGIV NATSSEDELR TEMMRQVIVQ DLLLDFLAAA GSAVKLPIPE IRVAVPTVMR
VESAAMGGSV YLVDRWLAGD FTKFSTNVEA GDSGLNDNIS FHSLCDALPH WTMDSAGLVV
VDIQGIFTLE LGRQGMQKKV LTLFDLMIHS EEEAYGLGDE GQKGIDRFKS QHRCNRVCRL
LGLDDGSSVD N
//
