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Database: UniProt
Entry: A0A094AIH0_9PEZI
LinkDB: A0A094AIH0_9PEZI
Original site: A0A094AIH0_9PEZI 
ID   A0A094AIH0_9PEZI        Unreviewed;       695 AA.
AC   A0A094AIH0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=V491_01047 {ECO:0000313|EMBL:KFY27088.1};
OS   Pseudogymnoascus sp. VKM F-3775.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY27088.1, ECO:0000313|Proteomes:UP000029338};
RN   [1] {ECO:0000313|EMBL:KFY27088.1, ECO:0000313|Proteomes:UP000029338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY27088.1,
RC   ECO:0000313|Proteomes:UP000029338};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:KFY27088.1}.
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DR   EMBL; JPJT01000533; KFY27088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AIH0; -.
DR   HOGENOM; CLU_396447_0_0_1; -.
DR   Proteomes; UP000029338; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 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.
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:UP000029338};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          400..625
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          349..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        444
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        608
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   695 AA;  78530 MW;  351578C5C7F6CEFD CRC64;
     MDPLFGPQLL QELNRQRRLI LPNDSGSLRR PTDVLFTLSK QDDDYRLMLL KLEETLSSRL
     KLSLDAQFAE SIRPLDIPIW QVLAFTEPSW FIDPERLKQR SKALISSQRN RRVVTVQKRG
     DFWNNSQITD WASKDQSSLI LLQGSYITRN LIESTAVELI EYLQEQDQHV IWLLHALPND
     PNKEIAPWDG CSVLKQIAIQ ILRENTSFNS LNDLASMVRL FQAASSVEDW FQILAATLEA
     IPQIYIVINL GVLCSRISDT QTWPQHFVRL FEALEKSSGA ILKVALLNHC PFSKSTLTPK
     TPLVQVTTIP MPPGQTLSSG HNFSGIRGGH RVHLPIFKRT RELKIGDNKL EASGPQTSPV
     IGGVAGKSKR QSPGDWFTEI KSFEKCIDAS RKDPDELHRR VRIAVLDTGV DTKHPDISRE
     LQENRIKVHD FVKDSTDIED LSGHGTHCVS VLAEFAPNAE IYVGRVFQTS QASNSSPETL
     KKAIRHAVNV WKVDIISLSL GFTEDNEELE DEIRMACANR VLIFAAAANN TMNEKTPIRF
     PARMKEVICV FSSDAYGRPS NFNPAPRFDR PNFMFPGEHI KGAWPAYLDT DDAFEHKGST
     YRYQDGTSCA TPVAAALAAG VLEFAWQERD YNIRNVKRLK HFSGMSDIFL KRMVDGYKVG
     NNSYHYVKAW KLISTNKSKA EIPILISDIM DDVLC
//
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