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Database: UniProt
Entry: A0A0M9VRQ1_9HYPO
LinkDB: A0A0M9VRQ1_9HYPO
Original site: A0A0M9VRQ1_9HYPO 
ID   A0A0M9VRQ1_9HYPO        Unreviewed;       541 AA.
AC   A0A0M9VRQ1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   10-APR-2019, entry version 16.
DE   SubName: Full=Subtilisin-like proteinase Spm1 {ECO:0000313|EMBL:KOS16862.1};
GN   ORFNames=ESCO_004905 {ECO:0000313|EMBL:KOS16862.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS16862.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS16862.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease
RT   agent of ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|SAAS:SAAS01077246}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOS16862.1}.
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DR   EMBL; LGSR01000029; KOS16862.1; -; Genomic_DNA.
DR   EnsemblFungi; KOS16862; KOS16862; ESCO_004905.
DR   OrthoDB; 921536at2759; -.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053831};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|SAAS:SAAS01099369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   Serine protease {ECO:0000256|SAAS:SAAS01099373}.
FT   DOMAIN       43    134       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      191    434       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   COILED      510    541       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   541 AA;  57715 MW;  A1458679867787C9 CRC64;
     MRTVLALSVA AVAQASSFKI GTIHDNSAPI LSSIDANAIP DAYIIKFKDH VDDSAATDHH
     SWVQDIHGEG EQQRLELRKR NIGNVEAFSG LKHTFKIGKS FRGYAGHFHE DIIEKVRNHP
     DVEYIERDSI VHTMLPLDHK NHIAEDKCAG DTEKGAPWGL ARISHRERLN FGTFNQYLYS
     ADGGEGVDAY VIDTGTNVGH VDFEGRAKWG KTIPSGDEDE DGNGHGTHCS GTVAGKKYGV
     AKKAHVYAVK VLRSNGSGSM SDVMKGVEWA ALAHIEQVKL AKNGKRKGFR GSVANMSLGG
     GKTTALDAAV NAAVKAGLHM AVAAGNDNAD ACNSSPAAAE LPVTVGASAI GDDRAYFSNY
     GKCTDIFAPG LSILSTWIGS NHAVNTISGT SMASPHVCGL LAYYLSLQPS TDSEYSVAPI
     TPKTLKENII SIATKGALSD IPDDTPNLLI WNGGGCSDYS QIVKAGGYTV KKNNNSSSSK
     TVGKPLSISE LEEAIEGDFE VLSGKVVSGA KKFTSKAEKF AEKLKELVNE EIEEFIHEVS
     E
//
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