ID A0A2G8K8K1_STIJA Unreviewed; 256 AA.
AC A0A2G8K8K1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Serine proteinase {ECO:0000313|EMBL:PIK44289.1};
GN ORFNames=BSL78_18879 {ECO:0000313|EMBL:PIK44289.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK44289.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK44289.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK44289.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK44289.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK44289.1}.
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DR EMBL; MRZV01000786; PIK44289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8K8K1; -.
DR STRING; 307972.A0A2G8K8K1; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-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; 1.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 99..144
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 183..236
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 256 AA; 28008 MW; B7DDD3A962881394 CRC64;
MLQPKTCAPT LDLCSNLRPV IQPKTCAPTQ DLCSNPKHVL LPMFSQMQDL IAFNAIALSN
VGLLKPCNGI LHQLKLSNMK WFIDYVYFDH SKTVVKDSFL GVVSTASTAV ALNGFAATLA
PKALELVRRF NFVKYVEEDQ IMRIDAVASW VLTELTNKTY LLITVSLQEP LTRNCNPWIA
NDGEGVNVYV IDTGINPTHV DFGGRAYTEA SMDFVSINRG GVDCNGHGSH CAGTVAVLLM
VSPTKPISLE SEYLAV
//
