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
//