ID A0A0B1TAT9_OESDE Unreviewed; 386 AA.
AC A0A0B1TAT9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:KHJ92485.1};
GN ORFNames=OESDEN_07622 {ECO:0000313|EMBL:KHJ92485.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ92485.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ92485.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ92485.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; KN551321; KHJ92485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1TAT9; -.
DR Proteomes; UP000053660; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 42..137
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 156..384
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 10..28
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 22..37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 386 AA; 42789 MW; 4C0A66D2BC636450 CRC64;
MCSTCTEAVC SDGSCLPRQK LCDGIKDCYD GSDEDDCNDL TFRLVDVNEL SGSVQVSFKG
MWQPVCSQGI GQNPANFICN SMNMGTPANV LAPRLLRNFG WQLQCDGQCF LRGFVFCQYG
ARIRCHSSKP SLSLSCGTRR VPAIARDPLV TRFARVVGGF ETAAGAFPWT AAVRNKAKIS
KDEESKTRAK FYVFRDDRRP TSYTVVVGDW DNTISEDHEQ RFNISRFYFY PLYEDLFAHD
LAIIEVPAPG IRFDDWTQPI CLPPRNFTYQ TGRKCVVSGW GSIGLTYPRR LQAAVLPIID
REECMNSSRI YSSMSRSAFC AGYLHGGVDS CQGDSGGPLA CQNDNGPFVL AGVISWGDGC
AQKGQPGIYT MVAPYLTWIQ GILKQR
//
