ID A0A2G7FRH4_9EURO Unreviewed; 261 AA.
AC A0A2G7FRH4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DNA damage checkpoint protein rad24 {ECO:0000313|EMBL:PIG83227.1};
GN ORFNames=AARAC_009932 {ECO:0000313|EMBL:PIG83227.1}, BDV24DRAFT_159144
GN {ECO:0000313|EMBL:KAE8345811.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG83227.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG83227.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG83227.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAE8345811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8345811.1};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR EMBL; ML737118; KAE8345811.1; -; Genomic_DNA.
DR EMBL; NEXV01000461; PIG83227.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7FRH4; -.
DR OrthoDB; 920089at2759; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR Proteomes; UP000325558; Unassembled WGS sequence.
DR CDD; cd11309; 14-3-3_fungi; 1.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF17; 14-3-3 PROTEIN EPSILON; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; 14-3-3 protein; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT DOMAIN 3..244
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 234..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 261 AA; 29134 MW; 522C5496850ABC5E CRC64;
MGHEDAVYLA KLAEQAERYE EMVENMKVVA SADVELTVEE RNLLSVAYKN VIGARRASWR
IVTSIEQKEE SKGNESQVTL IKEYRQKIES ELAKICDDIL EVLDKHLIPS AQSGESKVFY
HKMKGDYHRY LAEFAIGDRR KGAADASLEA YKAATEVAQT DLAPTHPIRL GLALNFSVFY
YEILNSPDQA CHLAKLAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAEPAAE
NASTEKKEEA PAAEGEKPAA E
//