ID A0A166C6A9_9AGAM Unreviewed; 384 AA.
AC A0A166C6A9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE SubName: Full=DUF159-domain-containing protein {ECO:0000313|EMBL:KZT37123.1};
GN ORFNames=SISSUDRAFT_1034314 {ECO:0000313|EMBL:KZT37123.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT37123.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT37123.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT37123.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000256|ARBA:ARBA00008136}.
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DR EMBL; KV428090; KZT37123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166C6A9; -.
DR STRING; 1314776.A0A166C6A9; -.
DR Proteomes; UP000076798; 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:UP000076798}.
FT REGION 267..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43196 MW; C572A5FB92CCD0C8 CRC64;
MCGRFALHLA RQEAREPRVN ARVQVNGWVN EERYIPRYNI APRTHSVVML PNTMGESIES
SSSAPLNVTL HTMKWGLVPH WSKHEDLSKS TMNARSDVLI EGGGMWQSIK GRNRCAVVVQ
GYYEWLTKGK EKIPHFFKHD DGKLMLFAGL YDSVLLEARR ALLNKTRKLG QQERLWTFTI
VTTDAAGPYE WLHCRQPVIL QDDEQLRSWL DTSKGWHPGL FPILQPYSGP QLAVYQVPKE
MGKVGTESPA FIEPVSERKD GIESMFKKQI ARSPSKNTKS PPSSPTKREE KMKSEVIEID
DIEDVKDVKD EGSPSTEPAS QAEDKSPNAS QEKGTLKVPS TPTTKRTHPT DFPSSPSPSK
KARKGKNLDP DGTSSKITSF FAKK
//
