ID   W9HBV2_FUSOX            Unreviewed;       603 AA.
AC   W9HBV2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=FOYG_16834 {ECO:0000313|EMBL:EWY80038.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY80038.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY80038.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; JH717851; EWY80038.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9HBV2; -.
DR   OrthoDB; 2734230at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR48182:SF4; DUF676 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 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:UP000030753};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          311..542
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        318
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        358
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        515
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   603 AA;  68198 MW;  A86ABE648F7375FA CRC64;
     MNGHWRSSWT HRVTQTMWLE SLLPFEIPRS RVMSYGFPHT AFKFSPKKSS LVSSYEIAKR
     LLDLLSSVRR EEQSRRPIIF LCHSTGGILL KRVLVMSFLQ FEDIFLSVRC IAFFGTPHRG
     ATPGIVSMGQ TVTTIARLAQ LFFGQLHEND ALNPLSKNYT ANLEELNDEF VSVMKISNKI
     SVLSFYETMT TNLGTLNTKV VDKYSAILGF HQLETVYAID SNHASLVKYR DADDPNYRLV
     LEQIKRITET LSNYSTLESR IGSYYPFERD DHRPLSELEE MKGLRADKWF ENLKILVHDI
     VADRADERDD RIRVAVLDTG IDFDHPLIAE SQSRIKQRKS FLPEHVTGPA DTSDMNGHGT
     HVTHILMKTA PNADIYVGRI FFEGKEFEME ENADKIAEAI RHATTKWDVD IISMSWGGPN
     DISPIKDAIR EAFYHGVTLF AAASNDGRMS NVAFPARMRQ VICVNSLDGY GRPSNFNPPA
     KPDTNIAALG EFIDAAWPWP IRGKGGQTIR KAGTSMATPV AAAIGALILE YANQDDMEGN
     KVEAPEQLSH CDEIRRILIE MSREMDGFLC LMPGDLFYKK YRDRTMHGLI CARINETVNG
     LSR
//