ID A0A0V1NSZ7_9BILA Unreviewed; 1322 AA.
AC A0A0V1NSZ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Papilin {ECO:0000313|EMBL:KRZ87085.1};
DE Flags: Fragment;
GN Name=Ppn {ECO:0000313|EMBL:KRZ87085.1};
GN ORFNames=T08_13148 {ECO:0000313|EMBL:KRZ87085.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ87085.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ87085.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ87085.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ87085.1}.
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DR EMBL; JYDM01000106; KRZ87085.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 7.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 8.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR028150; Lustrin_cystein.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 8.
DR Pfam; PF14625; Lustrin_cystein; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 8.
DR SMART; SM00289; WR1; 2.
DR SUPFAM; SSF57362; BPTI-like; 8.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 6.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 8.
PE 4: Predicted;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 189..239
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 323..373
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 478..528
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 532..582
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 646..696
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 705..755
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 770..820
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1014..1064
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ87085.1"
FT NON_TER 1322
FT /evidence="ECO:0000313|EMBL:KRZ87085.1"
SQ SEQUENCE 1322 AA; 148661 MW; F8B351BF3F68C8C3 CRC64;
LNVLHFKNFA STKFNSFLYY CIFYRMAQVQ NVVLFSVQVL LIYLSFVNAE ENACFRQQFQ
SACSDGSKLR IALRYYVKDG RCVAYPASLC EGANEQKLDL FKSAAECERR CLNSNLADDS
QQTPAPSKAS SSLSSPPSSL EVSKEIPKMT KHVDIIRIRK IGRPTVPTVA TVQPQLTSAP
ISNKFSSQCS VAYDAGHCKN ETQRWYFDFQ LSKCQTFTYS GCGGNGNNYR TEEECEISCK
EHRQPVCPKR TSPLVDTNGN LFDCFLQSCP SDFKCIYTSE KAYCCPDILN NGTKIALFRN
IVTFISCFIT EVASNLKTRP ALCEQKKERG FCDLFELRFY YDVQLEECNY FFYGGCGGNQ
NNFKRLSDCK QTCGGRKDST TRWNQKQIAE KLIQLETTQG GEEQQQQQQQ KSSEKKPELK
PSRVVQDKDP DLIVVNTVSS VTVKPAQHTV QTSFSDRIEY GTGKPSAENS EDNKFQRCSQ
PAAKGHCSRR LRRWFWDAKK NQCVQFIYSG CGGNGNNFLT EKHCTDVCAD PCMLPKKVGV
CRGAFQRWYY DHSANKCRKF IYGGCDGNEN NFVGKEECIS ACVRGDSNSD TIEVDDTDDN
DYETTDYTDE ESKDTELVQR LKAAVSFPVT KVNNNEDLFQ PIPIGCLQPV ETGNCDGVDV
RWHYNKGNHK CEAFVYTGCN GNDNNFASQL ECVNVCIERL PLNVCHHPVD KGTCKESYNR
WYYDRPKGAC KQFSYSGCGG NGNNFANEKE CLKMCNAQSE IDYPASDDIC YRPLDVGFCN
DEFIRWYYDP SIGDCKLFIF TGCGGNANSF SSSQECRRRC VRGQKTETLT VTNVLQQVVH
KSDQFKETTV KSDDLSTTES ISELEENWNT TRSANEQETP DEHDSKGDTH AVVHAVIDKI
TKELKENQTA STVGDLEETL VDLVAEGNTS VDLNTRDGRT IRLDKDSLTK ICKQLARRIK
VDMNDEILQA SREHSIPLVP VYTGENGHHS EGQMSGSAIV FAMINDEQDP LAKCLDELHP
GRCSNYVERW YYDRGTKKCR SFQYGGCGGN RNHFYSKENC IFHCERIADE VEKEYEERKQ
AREDDDSEPE DTTSPTSMPG YIPPEEKLTD SLSKDKDSPK APGFEPKNVF SGYKITPESD
VQQGPTISPP QPPPLLHVMA PPTFPEQEIR YIPGELMQQE QQLYNNNGYF PPPTISASEF
ESSPPYVTPP ISVMHSPPPP YATAQVPYLQ SVAPTSPAPS LPVEPYGVAS GRQHYSSRLP
PPCASGEVPV KNHDGSFLHC LPGQMTCPPD TSCYYNGLDY YCCSQAPDQS IKQYMPSTAK
PY
//
