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Database: UniProt
Entry: A0A068S5D5_9FUNG
LinkDB: A0A068S5D5_9FUNG
Original site: A0A068S5D5_9FUNG 
ID   A0A068S5D5_9FUNG        Unreviewed;       315 AA.
AC   A0A068S5D5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Duf159 domain protein {ECO:0000313|EMBL:CDH57205.1};
GN   ORFNames=LCOR_08176.1 {ECO:0000313|EMBL:CDH57205.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57205.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH57205.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) 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:CDH57205.1}.
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DR   EMBL; CBTN010000044; CDH57205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068S5D5; -.
DR   STRING; 1263082.A0A068S5D5; -.
DR   VEuPathDB; FungiDB:LCOR_08176.1; -.
DR   OrthoDB; 204678at2759; -.
DR   Proteomes; UP000027586; 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:UP000027586}.
FT   REGION          242..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  35737 MW;  9AF7D4819E27A130 CRC64;
     MCGRFACSLC PYELRTTLRS SDVAVSDKWN DEDYFHPSYN VAPRKWIPVV RYADNNDLIL
     QTMKWGFIPS WAKHTPDNQP INARDETLSV GHSMFDHAKN KGRCIVVAEG FFEWKKLTEK
     KKIPYYTKRK DGKLMLFAGL YDHSNIDGQS LYTCTIVTTS PSKFFSFLHD RMPVILENGS
     PEVEKWLSSE PWGKDISKIM KPYEGELDCY QVTDAVGPTT NNSSDFVVPV DQLKGSISNF
     FSKSSTTPAT KKPHPSASTT KSKEQEKPIT PSKRSADKDT QEDPIKKKLK STQAATTTTD
     KSKNKKKITS FFTKQ
//
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