ID A0A165CVY3_9BASI Unreviewed; 572 AA.
AC A0A165CVY3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=AGC/Akt protein kinase {ECO:0000313|EMBL:KZT51499.1};
GN ORFNames=CALCODRAFT_460352 {ECO:0000313|EMBL:KZT51499.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51499.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT51499.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51499.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV424104; KZT51499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CVY3; -.
DR STRING; 1353952.A0A165CVY3; -.
DR InParanoid; A0A165CVY3; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZT51499.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 239..494
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 496..567
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 572 AA; 63235 MW; CB2978377910C420 CRC64;
MSWKIGKKIK DATLSSKSSN PSLTASADIS RSTTPTPGNL NGSGNQGLSR SGLLTISVSQ
ARGLSLPAGV PLPPAVDKAL RSQEAQVASS VSAASVSKQQ QQARSSKNRE SLQRKQVWWL
PYVIVEFDKN EILLDALGGD ISAPVWMYRT HFDVSRSGEV SLQLYLRSGA GDAVNDAGVD
SMGKSDLYLG GVKFMPDFEA ASTRVINEWI PLTGGSGEVN LQIMYKPISH AAPLTIHSFE
LLQVVGKGSF GKVMQVRKRD TGRIYALKTI RKAHIVSRSE VTHTLAERTV LAQVNNPFIV
PLKFSFQSPE KLYLVLAFVN GGELFHHLQR EQRFSEERSR FYAAELLLAL EHLHDFNVVY
RDLKPENILL DYTGHIALCD FGLCKLNMTD NETTNTFCGT PEYLAPELLL NQGYTKTVDW
WTLGVLLYEM MTGLPPFYDE NTNEMYKKIL YDPLVFPDDM GSEARSILTG LLNRDPSRRL
GVNGAQDIKA HPFFSRHIDW RKLGAKKIQP PFKPSVASAI DTSNFDQVFT SEEPLDSVVA
DSQLSSTVQA QFAGFSYDGR GDELAQSVQS GI
//
