ID A0A158QLA8_HAEPC Unreviewed; 1598 AA.
AC A0A158QLA8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Kunitz/Bovine pancreatic trypsin inhibitor domain protein {ECO:0000313|WBParaSite:HPLM_0000611701-mRNA-1};
GN ORFNames=HPLM_LOCUS6109 {ECO:0000313|EMBL:VDO28023.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000611701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000611701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO28023.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO28023.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UZAF01016441; VDO28023.1; -; Genomic_DNA.
DR STRING; 6290.A0A158QLA8; -.
DR WBParaSite; HPLM_0000611701-mRNA-1; HPLM_0000611701-mRNA-1; HPLM_0000611701.
DR OMA; VPVNCAK; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 9.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 10.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
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 InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 10.
DR Pfam; PF14625; Lustrin_cystein; 3.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 10.
DR SMART; SM00211; TY; 1.
DR SMART; SM00289; WR1; 4.
DR SUPFAM; SSF57362; BPTI-like; 10.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 5.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 10.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1598
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041121927"
FT DOMAIN 307..357
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 422..472
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 518..568
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 584..634
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 645..695
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 853..898
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 946..996
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1011..1061
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1246..1296
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1539..1596
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 122..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1598 AA; 176626 MW; F2F292F01229C14F CRC64;
MRFLALLAAC AVVASIEAVD PCKRQPFRGR CPSKNGESPK RSQFVLRYYM RNGECVSYPY
GHCANDDSEP QLYRYKEECE DACINPPPAP LKLCISFILH ELLIFSCMFL FSPQAPLKST
TVEETTSTTT TPSTSTSEAP TTSKEAPTTT TTPVVPTTET SSTTIEDITA NKKTTMTTME
TAPTTPRMTT TTTKTSTTTT TTVEPTSTQS TTIRRNIHVK TTERLSVVQA DNTSRSVSSQ
SPATTGEYFH FSRAFLFFCI FQCEPDGRQC FCVDAKGIEI ANSRTRNGQK PDCDGIQLSS
APKTKECVGG AARGPCSAAL TRWYYDEQEA KCKRFTFSGC GGNGNNYDTE EACIRRCAPP
PMGLPKCEKG EPLKTKLGVP VNCAKSDCPY GYKCSVVQQT SVCCPENNKI IGLQTSGSAD
VCSLPKERGP CDKYELRFYY NAELKECKYF FWGGCQGNKN NFEKVEDCEA TCGINQRLPF
RTTQGIRITP GNLSKNDDGS VVERYVYMVS ILLPVNRCLH PKDPGTCRGQ FIRWYWDNER
KTCDVFTYTG CQGNGNNYAS REECLAICHK EATPVVAHDF SNVCKHDVDA GECNGVFQRF
AFDTESGECR PFTYGGCGGN GNNFATLAEC RIKCQKVALS PGNLCEHDIE VGECSGVFVR
FGYDKSTNDC RQFTYGGCGG NGNNFATIQE CRNVCIRKVC NPNPQCDLTR CQIVNDRNGC
PFCSCPPTSQ PSPPGTLISS VLSLCPEVNV DTCKEPCIII NNRKGCKDCV CPSLSGSIGQ
PPASFEDQDA SPIAPSTSRP VTPTVPPTSV GPPSGPTPNR SSPPGTITGH IPRRQGNIML
EYGFLFMHPM LQEPGPCKHF VDRWFFNGED GTCHPFKYGG CAGNRNHFFS QNECEIHCAR
FLPTTGKQLS AEPSTSQTQT TLTSTVTAAP VGVPTEREEI DARVLCSLPP DAGPCFEYVP
RWFFNAQSGQ CEQFSYGSCG GNENNFADRS VCEIKCLRAH STLLSHVPER CTYERDGGSG
KGYNVKWYFN MKNLRCEQFV YEGRGGNQNQ FETLSDCERY CSRKLLYQST SNFEPPRTLN
LGHPNMSLHQ RLQRFAHQHL TEGEESRKDL LSCPNGLKEL RYADGRPVMC LPGKNQCPEK
SVCYFNGVDF FCCPNEEDPY DKHVFGGYDG EETKHGYKVF GPLNIRRLMD EVPLRALRRQ
ASSNAFTAID SITAPLRFDE EKPRTVSRAQ RMRSNPSPPH HGNPICIEPL ATGDCGAAHL
RYYYDRDSDK CRLFYYTGCK GNNNNFGSMI DCQRLCVLGG QSELLFFFNC RFIVQTLTLI
AGPRPESDAS TPPPCPDGKS PLGGSAPVLC GNTTDSIGCP TGFFCLHGPP DICCPNGEVK
RKVSLNFSAH SRNVLLSTPK YMCPDASDPL MASNGEPTNC GAGFDGMKLC PKGFYCAIDV
EKQCAPLKSP GRFFFLVSML ETTTSVFAEE SEEFEDGEDE EDEEEGMAHL MLKPAENTTP
ATSTALPESE DHHIIDLPTE PPTVEEVHPV KTAEDKSVCQ IKPSEGRACR EDEKPPRTNL
HYFYSPKDRR CKLYFFRGCG GNANRFEKKA DCERLCLS
//
