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Database: UniProt
Entry: A0A2A9NQH3_9AGAR
LinkDB: A0A2A9NQH3_9AGAR
Original site: A0A2A9NQH3_9AGAR 
ID   A0A2A9NQH3_9AGAR        Unreviewed;       337 AA.
AC   A0A2A9NQH3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=DUF159-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMATHDRAFT_146348 {ECO:0000313|EMBL:PFH50006.1};
OS   Amanita thiersii Skay4041.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX   NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH50006.1, ECO:0000313|Proteomes:UP000242287};
RN   [1] {ECO:0000313|EMBL:PFH50006.1, ECO:0000313|Proteomes:UP000242287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKay4041 {ECO:0000313|EMBL:PFH50006.1,
RC   ECO:0000313|Proteomes:UP000242287};
RG   DOE Joint Genome Institute;
RA   Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA   Pringle A.;
RT   "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT   fungi.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC       {ECO:0000256|ARBA:ARBA00008136}.
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DR   EMBL; KZ302014; PFH50006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9NQH3; -.
DR   STRING; 703135.A0A2A9NQH3; -.
DR   OrthoDB; 204678at2759; -.
DR   Proteomes; UP000242287; Unassembled WGS sequence.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1680.10; SOS response associated peptidase-like; 1.
DR   InterPro; IPR003738; SRAP.
DR   InterPro; IPR036590; SRAP-like.
DR   PANTHER; PTHR13604:SF0; ABASIC SITE PROCESSING PROTEIN HMCES; 1.
DR   PANTHER; PTHR13604; DC12-RELATED; 1.
DR   Pfam; PF02586; SRAP; 1.
DR   SUPFAM; SSF143081; BB1717-like; 1.
PE   3: Inferred from homology;
KW   Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242287}.
FT   REGION          250..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  37905 MW;  A9C11E2CD9885D6B CRC64;
     MCGRFALRLD RHQIRNAIPD ADEWLDEDAF MPRYNIAPRT YSPVIRRPAP ALAPIEDRLV
     LHTMKWGLVP HWSKVEDKTL STTNARAENL VNGGGMWSNI KGKNRCAVVC QGYYEWLTKG
     KVKLPHFTKM KDGNLMLLAG LYDHAVINGQ SLWTFSIVTT DANPDFAWLH DRQPVILSTP
     ESLNAWLDTS TPGWTPTLTK LVQPYKDTGH PLECYQVPKE VGKVGTESPS FIEPIKDRKD
     GIQAMFQKQL QSTSGSGGGT KRKHDSSPTE ESKDDSKKEI KPEPAEEKKV KLRPTITPPS
     TPRKPKSSPT RRSTSPRKSA LPPTPEKARI TAFFRKK
//
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