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Database: UniProt
Entry: L2GXQ9_VAVCU
LinkDB: L2GXQ9_VAVCU
Original site: L2GXQ9_VAVCU 
ID   L2GXQ9_VAVCU            Unreviewed;       642 AA.
AC   L2GXQ9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VCUG_00590 {ECO:0000313|EMBL:ELA47870.1};
OS   Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC   Vavraia.
OX   NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA47870.1, ECO:0000313|Proteomes:UP000011081};
RN   [1] {ECO:0000313|Proteomes:UP000011081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Vavraia culicis strain floridensis.";
RL   Submitted (MAR-2011) 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}.
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DR   EMBL; GL877410; ELA47870.1; -; Genomic_DNA.
DR   RefSeq; XP_008073613.1; XM_008075422.1.
DR   AlphaFoldDB; L2GXQ9; -.
DR   STRING; 948595.L2GXQ9; -.
DR   GeneID; 19878475; -.
DR   VEuPathDB; MicrosporidiaDB:VCUG_00590; -.
DR   HOGENOM; CLU_438175_0_0_1; -.
DR   InParanoid; L2GXQ9; -.
DR   OMA; IMGIDYV; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000011081; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
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   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 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:UP000011081};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          61..96
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          253..342
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          468..607
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          116..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        262
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        294
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        574
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   642 AA;  70954 MW;  4C244E82C628C9E2 CRC64;
     MVSHYALSSA TLPTHMLILL IRYICAARYI VMLKDNPKRY NYNILSNSVF NALGMGDTVV
     NTLSNGFIGD LKEESANKLR NDEKVAYVER DMKVQIKEFI VKGEFVLGAD ASSAQHDSWD
     DELSDRLSVD RGDEGERRNK KHKSDRSDGS YGKTNNTREA LIGANRMLKN RDHRFSQVQN
     ASKYKNHKLD DLRKNNVIGN ADKGSGSTSR IRTQSHAHAV LEYQNDAPWG ISRISSGTKV
     NTMHTFRYPY SSGKNTQVYV IDTGVELSHP ELQGRAFFGA NFTTSSSDAD LNGHGTHVSG
     VIAGKTVGIA RKAEIVAVKV LDKMGSGMLS SVIMGIDYVI RKHSEKMERY EENKRNEYYK
     RVLDGRYDSG QDMNDNSWSD WREKGIPHRR IGGSIMSTSA FNPLWHVSSI INTVRSFLSV
     VNHDLGTEND PLGQLKLTGL TDPFRISSFN PLLSITGNSS YATNSLGTAS SDHKPKSIVN
     MSVGGLKSKV LDYAVKYATD IGIHFSAAAG NDHEDACEFS PSSSKLAMTA GASTASDTVA
     FFSNYGQCVD LYAPGVDIKS SWINGEYKVV SGTSMAAPHV TGAMALYLGE KDYTPAELIN
     MLKNDAYKVV HEPGKNTDDN YPLISIRKLI REIYDNSKKM DK
//
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