ID A0A395GUN1_9EURO Unreviewed; 626 AA.
AC A0A395GUN1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Serine/threonine-protein kinase gad8 {ECO:0000313|EMBL:RAK99122.1};
GN ORFNames=BO80DRAFT_139164 {ECO:0000313|EMBL:RAK99122.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK99122.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK99122.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK99122.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824448; RAK99122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GUN1; -.
DR STRING; 1448316.A0A395GUN1; -.
DR VEuPathDB; FungiDB:BO80DRAFT_139164; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000249402; 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:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 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:RAK99122.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 283..540
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 541..612
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 22..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 626 AA; 70023 MW; D9C96A9E94BF5139 CRC64;
MSWKLTRKLK ETHLAPLTQT FTRSSSTSTI KGDSGEETPV VSQTPSISTT NSNGINASES
LVSPPVAPVK PGILIVTLHE GRSFSLSPHY QQIFNSHFQN NNSYGMRPSS SSSHSAHGQA
ASFVQSGRPQ STSGGINAAP TIHGRYSTKY LPYALLDFEK NQVFVDAVSG SPENPLWAGD
NTAYKFDVSR KTELNIQLYL RNPAARPGAG RSEDIFLGAV KVHPRFEEAQ PHAEDPKSKK
APQERQLGQL GAEWLDLQFG TGSIKIGVSF VENKQRSMKL EDFDLLKVVG KGSFGKVMQV
MKKDTGRIYA LKTIRKAHII SRSEVTHTLA ERSVLSQINN PFIVPLKFSF QSPEKLYLVL
AFVNGGELFH HLQREQRFDI NRARFYTAEL LCALECLHGF KVIYRDLKPE NILLDYTGHI
ALCDFGLCKL DMKDEDRTNT FCGTPEYLAP ELLLGNGYTK TVDWWTLGVL LYEMLTGLPP
FYDENTNDMY RKILQEPLTF PSTDIVPPAA RDLLTRLLDR DPQRRLGANG AAEIKSHHFF
ANIDWRKLLQ RKYEPSFRPN VMGARDITNF DREFTSEAPQ DSYVDGPVLS QTMQQQFEGW
SYNRPVAGLG DAGGSVKDPS FGSITE
//