ID A0A319EVB7_ASPSB Unreviewed; 400 AA.
AC A0A319EVB7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE SubName: Full=DUF159-domain-containing protein {ECO:0000313|EMBL:PYI12305.1};
DE Flags: Fragment;
GN ORFNames=BO78DRAFT_330749 {ECO:0000313|EMBL:PYI12305.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI12305.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI12305.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI12305.1,
RC ECO:0000313|Proteomes:UP000248423};
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 (FEB-2018) 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; KZ826315; PYI12305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319EVB7; -.
DR STRING; 1448318.A0A319EVB7; -.
DR Proteomes; UP000248423; 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:UP000248423}.
FT REGION 44..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:PYI12305.1"
SQ SEQUENCE 400 AA; 45616 MW; DFBB71EFB8969DE1 CRC64;
MCGRYVLGVR MNFIRNRLQD QGMPVDEAPD DDEVRETYNF APGNNGAVYR ADTPTEYHPD
DLHVQPSPTD KAASERNATK SHYKLQSMKW GLVPSWTKRK PDYGSLMRTI NCRDDSLFED
RGMWTSMKRK KRCVVVCQGF YEWLKKGPGG KEKIPHFVRR KDGDLMFFAG LYDCVSYEDS
SEQLYTYTVI TTSSNPYLKF LHDRMPVILD PNSKEMKIWL DSGRTIWSKE LQSVLKPYEG
ELECYQVPKE VGKVGNNSPD FIVPVSSKEN KSNIANFFAN AMKGGIVKEE LDQKVVKEEP
PQEILKDERA TKDAEWSEDN APKPVPGVKR ERSSEVEAEE TKKQKTEPSV ASSLGYTSPS
KPVTHPGKNM RSATHNKPVK KTPEKKPTAG TQRITNFFHK
//
