SPL1_ENCCU
ID SPL1_ENCCU Reviewed; 465 AA.
AC Q8SQJ3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative subtilisin-like proteinase 1;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SPL1; OrderedLocusNames=ECU01_1130;
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=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
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 [3]
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: Secreted, extracellular space {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; AL391737; CAD24986.1; -; Genomic_DNA.
DR RefSeq; XP_965951.1; XM_960858.1.
DR AlphaFoldDB; Q8SQJ3; -.
DR SMR; Q8SQJ3; -.
DR STRING; 284813.Q8SQJ3; -.
DR MEROPS; S08.032; -.
DR GeneID; 860292; -.
DR KEGG; ecu:ECU01_1130; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1130; -.
DR HOGENOM; CLU_011263_1_6_1; -.
DR InParanoid; Q8SQJ3; -.
DR OMA; TWIANET; -.
DR OrthoDB; 921536at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 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 Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Sporulation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..465
FT /note="Putative subtilisin-like proteinase 1"
FT /id="PRO_0000382936"
FT DOMAIN 19..90
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 115..447
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 386
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DISULFID 329..360
FT /evidence="ECO:0000255"
SQ SEQUENCE 465 AA; 50778 MW; 3109F99457119F45 CRC64;
MILAIISLSV VICREVSDYI VMFDQDPSMD RASMKVLYNM NIHEAQNILR PDESIGIKMT
NGFVARMSES TAERMKRHPS VKMVVKDSPV GISGLKFDVP GSDDRSGIVM QRHAPWGLAR
VGGSVSLVHG NYCYPINSGK GVDVYVLDTG VEIEHPEFGG RARWGANFVP KSPDRDEHGH
GTHCAGVIGG KNFGVTKESS IIAVKVLDKY GSGMTSRLLQ GVDFVIKEHE KKKDELYNAA
ADEYLSSGGS SDIEIEMDGS ESFSFVQPET PSIQRLVDAI SRKALQPKTV VNLSVGGFRN
AALNFAIEYA SRLGIHFSTA AGNEHEDACD FSPGSSRAAI TTGASTYRDT VAFFSNFGKC
VNVFAPGVDI LSSWIGGTQK IVSGTSMAAP HTSGAIAAYL TYYDYDPHML KSRIIGDARL
IEDVSEDDYD GTTIWPLPSL FNANKKKLPI LSMERLLRRV RNKMR
