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Database: UniProt
Entry: A0A395GUN1_9EURO
LinkDB: A0A395GUN1_9EURO
Original site: A0A395GUN1_9EURO 
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
//
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