ID   R9ABN8_WALI9            Unreviewed;       940 AA.
AC   R9ABN8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Minor extracellular protease vpr {ECO:0000313|EMBL:EOQ99628.1};
GN   ORFNames=J056_001713 {ECO:0000313|EMBL:EOQ99628.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99628.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KE007240; EOQ99628.1; -; Genomic_DNA.
DR   RefSeq; XP_009269616.1; XM_009271341.1.
DR   AlphaFoldDB; R9ABN8; -.
DR   STRING; 1299270.R9ABN8; -.
DR   GeneID; 20374665; -.
DR   KEGG; wic:J056_001713; -.
DR   eggNOG; KOG4266; Eukaryota.
DR   HOGENOM; CLU_003559_3_1_1; -.
DR   OMA; DCADFFA; -.
DR   OrthoDB; 662485at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR   InterPro; IPR010435; Fn3_5.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF06280; fn3_5; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..940
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004470394"
FT   DOMAIN          167..569
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          621..722
FT                   /note="Fn3-like"
FT                   /evidence="ECO:0000259|Pfam:PF06280"
FT   ACT_SITE        176
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        525
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   940 AA;  100167 MW;  C31CE6321FA1ADCC CRC64;
     MPRLFIILSF CLVACTLAVS SWSDSRAIPK TTQYALELAD GHAPHDSLFQ QLQSRDIPYT
     LTQSFNSPDL FVGAAIHLQN SDHSYHLPSL ESVKHVYPIN SFDSPNAFTE VVNTEQRNLA
     ESSFTPSLYP LVSGTQAQPS FYAVQTLSQS VLDMSGLAYA HAQNLTGSGI FIAFVDDGVD
     YSHPALGGCF GAGCPISRGW DLVGDAYNTT NNILNPGPLP ITTCKSHGTS TLGFAASQLR
     ELPGGAPNAT YGMYRIFGCH GSSGDDVLAM GLIRAYEDGA DIINVSAGGP DGWTTSLPSV
     VASRIVQRGR HVVTSAGNYG QQGLLYSNSP AGGIGVTPVA ALDLPYVPVL NASLTVAELP
     GERFPYIPEE VFGAGNETRR SYVVDDACGG VSAAEMGSLD DLALIIDSST DECDLSTKLA
     NLKTANASLV LITDTHSNLT QAPHVGGLDT ALLRTSVASA IPHNGTLTLH YTPQLTHIPR
     GGLVAQYSSM GPSADGYGKP AVSAIGSNIP TPAPNNSYMI QSGTSFSAPV YASLLALLLE
     KHAIDDVHLS PEQARAIMLN SAQSVRLAVD ADDGDAFTVL QGNGRTSIAR ALAASAYATP
     DIVNLNDTWG ADSTGAGAGE KSAQVQLVNL SQKRTTYTLA HHPALTGYVL EEGTIQPSTY
     LPPYSNDTAT VKMAHSVSVE PLSSVDVDIV FTPPQCSDHR LPIYSGFIEF TDAQDVNNTL
     HISYNGIAGN LSQMTILDNT DDFFQQGFPV PFTYRSSDRT MLNDTNTLTF SLEDDDRPAL
     VYRLAGPSPY LRIDLVGADT ERNRTTSSIT IPAQESNNNS RRTSRSLADG VMGWMADLLG
     GTNINTNTNT HVDSDVKNNS STLTINTLGI LYEELGVSRN GFKGSGQGSS FYRYDMNTFA
     DGAPIPTGEY KFLLRALKVH GDEHDSADYE SWLSDAFKVI
//