ID A0A1I8JC24_9PLAT Unreviewed; 509 AA.
AC A0A1I8JC24;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase S1 domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0046652-snap-gene-0.9-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0046652-snap-gene-0.9-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0046652-snap-gene-0.9-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR AlphaFoldDB; A0A1I8JC24; -.
DR WBParaSite; maker-uti_cns_0046652-snap-gene-0.9-mRNA-1; maker-uti_cns_0046652-snap-gene-0.9-mRNA-1; maker-uti_cns_0046652-snap-gene-0.9.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..509
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009321632"
FT DOMAIN 28..144
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 278..508
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 234..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175..190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 216..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 509 AA; 54462 MW; 9350290196CE65EF CRC64;
MRLPKLLPLL LIGGLATLNV AIADELNCGV NLLYETDQTV IASHRLYGRK SYQPNSVCRY
IIRAWSPDYR IEITSVSFDL EYTSECTGDS LTVYSGGNDS SPVLGRFCGS LDWSVLTQSS
FVALVFSSDA YLEKGGFQLR YRFVSKDEYQ KRIACPNGYL ACNSGNGCYP SKWKCDGIKD
CKDGSDEQFC TSTLTCPSGQ VACKDNSKCI FSGWWCDGFR DCGDGSDETS CSGGGNTGGN
TGGGTGGSTG GSTGGSTGGG TAPSGCGTPA IPPDETRIVG GKEAVKNSWP WMVSLRLFGG
HFCGGSIYNA NWIITAAHCV ENYMSPSMWG VDAGRHCRDC TEATLQRRKV TQVVRYPNYD
SSRTNQDLAM MRVDRPFQFN SQVSPVCLPS SPVSNMASCF ATGWGSTQGT GDNTRLLQVM
VPIVPNSICG DASHYGGAIT SYMVCAGYEQ GGKDACQGDS GGPLVCKSGG VWYLQGITSW
GEGCAKPQRP GVYTRVQMYT SWIQQTASG
//
