ID   SPL2_ENCCU              Reviewed;         535 AA.
AC   Q8SS86;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Putative subtilisin-like proteinase 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SPL2; OrderedLocusNames=ECU03_1180;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17169074; DOI=10.1111/j.1550-7408.2006.00179.x;
RA   Roennebaeumer K., Wagener J., Gross U., Bohne W.;
RT   "Identification of novel developmentally regulated genes in Encephalitozoon
RT   cuniculi: an endochitinase, a chitin-synthase, and two subtilisin-like
RT   proteases are induced during meront-to-sporont differentiation.";
RL   J. Eukaryot. Microbiol. 53:S74-S76(2006).
CC   -!- FUNCTION: May be involved in the degradation of proteins for nutrient
CC       acquisition or possess a regulatory function by proteolytic activation
CC       of proproteins.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expression is low in meronts, but becomes induced
CC       in sporonts and spores. {ECO:0000269|PubMed:17169074}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AL590443; CAD26262.1; -; Genomic_DNA.
DR   RefSeq; NP_597627.1; NM_001040991.1.
DR   AlphaFoldDB; Q8SS86; -.
DR   SMR; Q8SS86; -.
DR   STRING; 284813.Q8SS86; -.
DR   GeneID; 858789; -.
DR   KEGG; ecu:ECU03_1180; -.
DR   VEuPathDB; MicrosporidiaDB:ECU03_1180; -.
DR   HOGENOM; CLU_038703_0_0_1; -.
DR   InParanoid; Q8SS86; -.
DR   OrthoDB; 921536at2759; -.
DR   Proteomes; UP000000819; Chromosome III.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 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   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Membrane; Protease; Reference proteome;
KW   Serine protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..535
FT                   /note="Putative subtilisin-like proteinase 2"
FT                   /id="PRO_0000382937"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          221..475
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        255
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        277
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        420
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DISULFID        369..400
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   535 AA;  58673 MW;  DA349C785B44B7D9 CRC64;
     MFFVGVAVLA ALQSVWGNGG LETNEVAGMD RLGVESQKEN PPGILLRKDD GMCEARKPMD
     MSPGEVQTET KTVVKEIVVE IEEPREGIQE VLPVVQYEGQ AKVSAGNDLL KPSCGVSSGF
     TSSAERCYVL TKDAHDGDTS KMISLVESLS GRVKRQYTKN ITGVSFCSSH SDVLRKVDDA
     GMHVEEDKIY TVSMLQNNIP NYMYLMRHYE NTIFNNYFYD NWIFRVLQIK RVMTKFLGSY
     EYYHTGKGVN IFLLDTAISS MDGACNLSGR LEACNAHGNV MAELLVGKTN GFAKDSRLSV
     LDVVDCDGKV ALSEMIHGLE GLRESGGPSI LVFGVSGPYS ASLNSAVDRI SSRGTVVVSP
     AGNSHDQSCN YSPGSSKSVI NVGSVDKHAG ISRFSNHGDC IRMFAPGEDV LQDSSLTGTS
     LSAAIVASSI ALFLETSPRA AFPQIWGYLN QNSFWNSRGS YSVLKIPRLG CKGRIRGSIF
     RLGGLYEDIV PLVFVVLITS ALLYLLLIGI RRFRRRREQE LHDEDVLFDP PVDRF