ID   A0A2I2G563_9EURO        Unreviewed;       458 AA.
AC   A0A2I2G563;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=DNA repair protein rad9 {ECO:0000256|PIRNR:PIRNR009303};
GN   ORFNames=P170DRAFT_497038 {ECO:0000313|EMBL:PLB48018.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB48018.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB48018.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB48018.1,
RC   ECO:0000313|Proteomes:UP000234275};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts in DNA repair and mutagenesis. Involved in promoting
CC       resistance to ionizing radiation and UV light, as well as regulating
CC       cell cycle progression after irradiation.
CC       {ECO:0000256|PIRNR:PIRNR009303}.
CC   -!- SIMILARITY: Belongs to the rad9 family.
CC       {ECO:0000256|PIRNR:PIRNR009303}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLB48018.1}.
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DR   EMBL; MSFO01000005; PLB48018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2G563; -.
DR   STRING; 1392250.A0A2I2G563; -.
DR   VEuPathDB; FungiDB:P170DRAFT_497038; -.
DR   OrthoDB; 1111055at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0030896; C:checkpoint clamp complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.70.10.10; -; 1.
DR   InterPro; IPR026584; Rad9.
DR   InterPro; IPR007268; Rad9/Ddc1.
DR   PANTHER; PTHR15237:SF0; CELL CYCLE CHECKPOINT CONTROL PROTEIN; 1.
DR   PANTHER; PTHR15237; DNA REPAIR PROTEIN RAD9; 1.
DR   Pfam; PF04139; Rad9; 1.
DR   PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|PIRNR:PIRNR009303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT   REGION          283..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..406
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  51104 MW;  5229E42441E3E36F CRC64;
     MTTLSFALAP QALIQLHDAL ICLSKFDETV VMEAEYDLLR LSVLNSTKTS YSAFALDANR
     FFQDYSFGVL RDANSARNRQ PNKFCCQVYL KALLSVFKGR MGGRNKDTAV ERCEVDLYED
     YDTAECRLII KMICGLGVIK SYKLTYEPTT AQHAVFDRSK TTNEWSIEPR FLREITDHFS
     PSAEQLDIYS EAGKVIFTSF TTKIAEGKEV LKQPVHTSVA IDKKDFSHFL AQDGIHLAIS
     LKDFKAVIAH AETAGAIITA RYTRPSRPMQ LAYDLEGHRS EFTLMTTGDP GADDGPDSSR
     PQELSARQTP APIQSNTSRP SQPRPSSRAT DVRQMPPPTS RSRSIRPLTG TSARNTQTQP
     QTQSETQPPP ASINFESLFV PADDDGQWDV PNDEEEETED VLGWDAMGDQ DIDGLGQRLR
     DTQPSMQRGD QATTNEEEEM GIPPTQRMSQ LHGLGLFD
//