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Database: UniProt
Entry: A0A0D2DN95_9EURO
LinkDB: A0A0D2DN95_9EURO
Original site: A0A0D2DN95_9EURO 
ID   A0A0D2DN95_9EURO        Unreviewed;       956 AA.
AC   A0A0D2DN95;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=PV04_08745 {ECO:0000313|EMBL:KIW63767.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW63767.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW63767.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW63767.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KN846961; KIW63767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2DN95; -.
DR   STRING; 5601.A0A0D2DN95; -.
DR   HOGENOM; CLU_006016_3_1_1; -.
DR   OrthoDB; 1783441at2759; -.
DR   Proteomes; UP000054266; 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; cd07491; Peptidases_S8_7; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          645..887
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        653
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        693
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        851
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   956 AA;  108037 MW;  B2A5D524BCA9FCFC CRC64;
     MAPMQRKPGE KDGKEIGGMD HSLKTNRMDR VKRRAKVSES SNQYDPRTLL QEAEKVDFRI
     KEQADNFKRK YNDYLLGRTD MGDSRKNILH VLADHENRWT DDQIQTFLDW LLKEYHGLLE
     KKDDLGYAPL FRALQYDKHA FVNAVLSYPN LKNLGAVLKL TCDKGNILHV AIYNESPYIK
     TMVKKCRSYP AIFTQGNDAN ARHTPLHYAV LIDEGEKDLE EVLRKHGVVA KHDSPNKATT
     ESALSIRRVG TTSLNQQNPK QHSLSPSEPA PADWTVVDGD PRYATKGVQP LELVELLVEA
     CPAALSYKNA AEETPYQARD SLLQDSTTVQ SAINKILEAT ENTNEKGPTD EMRERAFRKI
     FVDDPIASYI REYCMCNLAR DETMKCLYRP GQELHIEFDL AGIPNPNIPQ AYLEQLANHL
     RFESILKYVA LPRLSIDVPN RLASRVKKDT RLSRRGLTDM KLIFDWLRSK GVKKIVKVMV
     IDDGNPSHSD AAIEDALRGL EVELWDWKKL DLCTDVIATS SKKVKEVSLY SSGNNAVLMG
     WASSEGLTNI AKFPKLKRVN LFIREGQENS ERLHRYIDDF KARVGSAEKP NNQDLEIISV
     LDNNDVSYAS EFQTSEGSLQ PENPWIKCVK DFATFLRGVD KGTKHHVKIA VIDDGVDASW
     DSLTGKIAAG KSFCPYPNST DLMSAYFAPT GKHGTCMADL ISQLCPNVRL YVARLEEHRK
     MDGDGRRQIT TRSAAEAIQW AVNCQVDIIS MSWTIETQIT ETEDMQNFRS AIFEAEAKKI
     LMFCSASDQG GNSTDGCYPG QWGNCIKIGG ATSTGEILTW VKEDKIDFLL PGKKIPFTNP
     DGSKFTESGS SVATASASGL AGLLIFCDRL LEQDSDSYFR NRLNMTAAFK KLSMNERKFP
     HVEYFFEEKF KSLLLADVPE KERPNRSIAI EEEVWNEKSR YALQELIKLI KEKNPY
//
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