ID A0A2B7XKG4_9EURO Unreviewed; 437 AA.
AC A0A2B7XKG4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE RecName: Full=DUF159 domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GX51_00862 {ECO:0000313|EMBL:PGH09108.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH09108.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH09108.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH09108.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000256|ARBA:ARBA00008136}.
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:PGH09108.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDNC01000006; PGH09108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XKG4; -.
DR STRING; 2060905.A0A2B7XKG4; -.
DR OrthoDB; 204678at2759; -.
DR Proteomes; UP000224080; 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:UP000224080}.
FT REGION 51..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 48413 MW; 559517665453831B CRC64;
MCGRYAMGIR LAFIRNQLQQ RGQPVDEAAD DDDVRQTYNF APGSYGAVYR ADSSDHGGAV
GSQDDDIGSN EQVEDQGAHD EPTKTTERRT HYKLQSMKWG LIPFWTKRSP DYGSMLKTIN
CRDDSLIEDR GMWTSMKKKK RCVVICQGFY EWLKKGPGGK EKVPHYVRRK DGDLMCFAGL
WDCVQYEGSD EKLYTYTIIT TDSNPYLNFL HDRMPVILDQ GSPEMATWLD PNRVTWSKEL
QSILKPYEGE LECYPVSKEV GKVGNNSPDF IIPVNSKENK SNIANFFASA GSKGKSGQKA
QGQGISKSSS GKPGAKDVST LAQESTVKQE EEGHKDEVNL TSFKSDSDAQ SASQTSTVKR
KWESPKGAED TSVTTKLPKI TQSDSAQLPS EKGVSHSPTK AGGRKMWSAT SNGSAPKQGG
AKRTTRGTQQ ITNFFKK
//
