ID A0A0D2CAQ4_9EURO Unreviewed; 688 AA.
AC A0A0D2CAQ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW46947.1};
GN ORFNames=PV06_02565 {ECO:0000313|EMBL:KIW46947.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW46947.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW46947.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW46947.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847333; KIW46947.1; -; Genomic_DNA.
DR RefSeq; XP_016267163.1; XM_016403266.1.
DR AlphaFoldDB; A0A0D2CAQ4; -.
DR GeneID; 27354639; -.
DR VEuPathDB; FungiDB:PV06_02565; -.
DR HOGENOM; CLU_000288_52_3_1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000053342; 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; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 301..562
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 563..647
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 688 AA; 77147 MW; 99C869424DD189E4 CRC64;
MAQTGLNPQD PADLLRQAMA QNSARHQLRD DIGDGIGSGS PTPSGVATPR PDLHDKRLPG
IMHSYFGQST PPLTPRALSQ EDRRIDTRSP LSSTSTTARD SSVDSAEKTI QKEQIPTNAP
RGKLSIKIAE GRNLKPSYDP YVVCQFEWNE YVSKGARHDK MDVDGDDQKG PVGALQSIIR
RTDSDMGKPM AIPMRSRQCS TNGTGDDRGI TKVVDPQWDH DATFDVVSHQ SELDVTVYDR
QTEAFLGHVR LCLNLSEQQP DLEGFFRLEA RSPEDHDITG EIHIRMHFTK VDKKHYGPND
FTILKLIGKG TFGQVYQVRK KDTGRIYAMK VLSKKVIIQK KEIQHTIGER NILVRTATTE
SPFIVGLKFS FQTPTDLYLV TDFMSGGELF WHLQKEGRFK EDRAKFYIAE LILALKHLHE
HNIVYRDLKP ENILLDANGH IALCDFGLSK ANLTQDDTTN TFCGTTEYLA PEVLLDEQGY
TKMVDFWSLG VLVFEMCCGW SPFYAEDTQQ MYKNIAFGKV RFPRDALSTE GRNFVKGLLN
RNPRHRLGAN GDADELMAHP FFGDVNWNAL GKKNLIPPFK PKLSSVADTS NFDPEFTNAL
NTSSSLNARA AALAAGANPA STPLSPTMQN AFRGFTFVDE STMEERFGGS REPEDDRIDE
NELARSRTHE HRMSGVQKTG DDGFFFEE
//
