ID A0A0D2B3Z9_9EURO Unreviewed; 831 AA.
AC A0A0D2B3Z9;
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:KIW46946.1};
GN ORFNames=PV06_02565 {ECO:0000313|EMBL:KIW46946.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW46946.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW46946.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW46946.1,
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; KIW46946.1; -; Genomic_DNA.
DR RefSeq; XP_016267162.1; XM_016403265.1.
DR AlphaFoldDB; A0A0D2B3Z9; -.
DR GeneID; 27354639; -.
DR VEuPathDB; FungiDB:PV06_02565; -.
DR HOGENOM; CLU_000288_52_1_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 444..705
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 706..790
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 831 AA; 92412 MW; B6578C3DB05684CC CRC64;
MHSYFGQVGR DPSQDTASRS SRGAASLEKN DEPAHSSLKR REKQEDRRRS SASIGSMVMV
EREQAPVSTP PPDEPQSEST QPVTQADSSR MPPTPISSAA SVVNRDGEVA ENGSSILDGG
LASITQALRN FVLPKSASAV KERRHQSLPV SSVTKSNVSA AHISNPTSST HSSRPESPKP
LSPSSAKPPS SEILEETHEL TSSVADRPRK KSTPPLTPRA LSQEDRRIDT RSPLSSTSTT
ARDSSVDSAE KTIQKEQIPT NAPRGKLSIK IAEGRNLKPS YDPYVVCQFE WNEYVSKGAR
HDKMDVDGDD QKGPVGALQS IIRRTDSDMG KPMAIPMRSR QCSTNGTGDD RGITKVVDPQ
WDHDATFDVV SHQSELDVTV YDRQTEAFLG HVRLCLNLSE QQPDLEGFFR LEARSPEDHD
ITGEIHIRMH FTKVDKKHYG PNDFTILKLI GKGTFGQVYQ VRKKDTGRIY AMKVLSKKVI
IQKKEIQHTI GERNILVRTA TTESPFIVGL KFSFQTPTDL YLVTDFMSGG ELFWHLQKEG
RFKEDRAKFY IAELILALKH LHEHNIVYRD LKPENILLDA NGHIALCDFG LSKANLTQDD
TTNTFCGTTE YLAPEVLLDE QGYTKMVDFW SLGVLVFEMC CGWSPFYAED TQQMYKNIAF
GKVRFPRDAL STEGRNFVKG LLNRNPRHRL GANGDADELM AHPFFGDVNW NALGKKNLIP
PFKPKLSSVA DTSNFDPEFT NALNTSSSLN ARAAALAAGA NPASTPLSPT MQNAFRGFTF
VDESTMEERF GGSREPEDDR IDENELARSR THEHRMSGVQ KTGDDGFFFE E
//
