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Database: UniProt
Entry: B0F9T8_TRISP
LinkDB: B0F9T8_TRISP
Original site: B0F9T8_TRISP 
ID   B0F9T8_TRISP            Unreviewed;       370 AA.
AC   B0F9T8;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   SubName: Full=Putative serine protease {ECO:0000313|EMBL:ABY60761.1};
DE   Flags: Fragment;
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:ABY60761.1};
RN   [1] {ECO:0000313|EMBL:ABY60761.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISS534 {ECO:0000313|EMBL:ABY60761.1};
RA   Liu M., Fu B., Wu X., Yu S., Deng H., Liu X., Guo H., Sun L., Chen Q.,
RA   Boireau P., Li L.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABY60761.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISS534 {ECO:0000313|EMBL:ABY60761.1};
RX   PubMed=19091476; DOI=10.1016/j.vetpar.2008.10.035;
RA   Wu X.P., Fu B.Q., Wang X.L., Yu L., Yu S.Y., Deng H.K., Liu X.Y.,
RA   Boireau P., Wang F., Liu M.Y.;
RT   "Identification of antigenic genes in Trichinella spiralis by
RT   immunoscreening of cDNA libraries.";
RL   Vet. Parasitol. 159:272-275(2009).
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DR   EMBL; EU263331; ABY60761.1; -; mRNA.
DR   AlphaFoldDB; B0F9T8; -.
DR   HOGENOM; CLU_610222_0_0_1; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264:SF54; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ABY60761.1};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN          1..223
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          236..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABY60761.1"
SQ   SEQUENCE   370 AA;  41047 MW;  4C4D1474560E95DC CRC64;
     NSARVKLCGG SLVELKPGNG SQWVLTAAHC AYYAEYGRRF TPDEVQVILG AHRPNEEEKT
     QLKVDTKRII SHPRYDDVTV VYDLSLVMLK EYLIYNNEIR SACLPKPDEP VPLDVPCFAS
     GWGLTYHGGR GSDVLRIAEM KPLPKDECRI KPEEHAIVFC AYGVDRSATC QGDSGGPVVC
     LKNNKATLYG IVSYGPPTCG DARHSVKFAK VPAMMQWIQD TARSIDSTVP VVSRFEPKPS
     EQKVDQKDTQ PSPSVSPGRV DVGKKDIMKD LPEIPTRENV KDTPGDYKGS DVFNFIYRDG
     FPSHSKFPDL EQIMSDFMSP GSGGMSGGSF FNSPRVFIET KTINRLPSVS RSRSDVGRFG
     FNDPSFTFFR
//
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