ID A0A0N4Z460_PARTI Unreviewed; 2927 AA.
AC A0A0N4Z460;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Kunitz/Bovine pancreatic trypsin inhibitor domain protein {ECO:0000313|WBParaSite:PTRK_0000178100.1};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000178100.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000178100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR STRING; 131310.A0A0N4Z460; -.
DR WBParaSite; PTRK_0000178100.1; PTRK_0000178100.1; PTRK_0000178100.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 8.
DR CDD; cd22638; Kunitz_amblin-like; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 11.
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; 2.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 10.
DR SMART; SM00211; TY; 1.
DR SMART; SM00289; WR1; 3.
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.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2927
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005891234"
FT DOMAIN 136..195
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 209..259
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 285..335
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 399..449
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 469..519
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 811..861
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1732..1782
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1798..1848
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2515..2565
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2867..2924
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 667..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2036..2056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2259..2293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 164..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 2927 AA; 327760 MW; FBB9E81748A585A7 CRC64;
MKRSLALLII SCLLIRNILS SDVDPCKRQP FRGRCPVSGN GIQARSQFVL RYYLRNGECV
SYPYGHCAND ENEPKLFRYK EECQDACLNK KDDSNIDDSE SQRRLAPKKT FSTSVPDEQT
YATNKPISQS ETPVILSECE KQRSNGDGFK LECDIDGNYK ALQCNADKQE CFCVDAAGKE
VPYSRSQPDG VAPDCSAIAK AERRLTDKCT GGPSYGPCKA NLTKWYFDDN ENICKTFQYS
GCGTNGNIYE NELSCKDRCV KRKTTTSSET ESHTTIPQAD RNTICSLPKE RGPCDKYDLR
FYYNKELNEC KYFFFGGCEG NQNNFLKVED CEATCGAKPA QFREEIPKKP EDVTTGPKIV
ETLPTRENSN RFTQQTVPQT IPPRVLQTTT EFPFTENRCT PPKDPGHCSG NFVRWFWNSE
RKICETFSYS GCGGNSNNFA NREECLSVCH INAMPKEAEP ETLNPFDVCS HKIDPGECGG
NFLRFAFDKQ SGQCVKLRYT GCMGNGNNFA TEEDCARKCL PNRKPVQQSP ACFHPIDIGD
CEGVFPRFGY DRNTNECKKY IYSGCNGSPN NFGTYQDCAD SCIRSPCLPL TNCDLSRCHV
TKDERGCPAC SCPPTISNPA ISPPPFPLSG NKIQINCPIV DAASCIEPCM IFSNRKGCQE
CVCPQAPTSE KPSSTQSQVF ETPTSARQFV RPQQPDERQF ARPQPTLQNT EKPFIRTQPT
LPETERPTQT TSRFETRPPS THFTSQSTFE STSGSTFEPT FESTFEPTLT PHAPSPPAPP
APKSVEIDIN SVDNRNVPVA PTFTDVVGDK CTLPVDPGPC KNFIERWYFN IKTGTCEPFK
FGGCGGSRNH FFTRHECEVH CARFANLTPL PHFKILTHAP FIKSLPILRS ENTLNNVIPI
PPSIIMKQNN ENNKVNMPIV KQNQKVIKDN EIKKNTSLIS TQQFLKIPIV VDTIKKIQKE
EERRPVEMIE EGDTKEILEI KEELVSRGVW IPESMMSENV PSTTERSIFI SSRLTTLIPT
ERSTLISTDR STLLPNQSLE ILGNPNNRLM WIQNIDTKTG KIDKILPNQI KPQIPGAIGS
VMWVKRWNRK LEKYELINPS QYAFEEYQRQ LNNNRKGEVI VDMPIKNTER IFENTRIQST
TQIPQIFVFS TQDVEIKSTI NPIPNQGNEI VTEIPINNIE PTRHNLPIPE KFPLNTINSE
SKPFIIKNES QIMWINVWNE ETQKKEIIGV PKDILQKSTT RIVLESVTVA PVKIIKPPIH
ENVSQGFDNK FHDKIEEERV LKFIKNIEEN KEDDIIIDST LSVEPNKESS VVPVTFEMKE
KIELNKDDGK VVTKEDILTI ADKESSIAPV TFKLEKEIKP TFKEYTREPI NYKTTKIHKP
TVYATKLPDV SPLHTIFEEL IIADKSIYFS TASPEKSQFS KTTKDVIPIT EGTSKKIIKF
IEPLIYESTT QKIVHLQKET EVINSDNEFT SLSEQKIVKN DDVETTTTQI DDVKTSLSPN
THKINENVET SKSTVRMDII EPSLSLNTIK NDNIESTKAT IYTMKPSLST FINNNTWTTK
STVKIDGNSQ TTRPTIKIDT TKTLLSLRTF EDDNSINEIT ESVTESRPDN KLSRVFITKV
PPKHNSKIVT MVPIEFTSKF TTKAPTEIDL KKLDNINVLT KEIVTPYFIN ITSSTAPSTI
ITKDIISGLS TVQPTRSPIK AQVPISTQRQ QNKLTTQRQQ SKQTSEELVD ICNLPADAGH
CFNYAPRWYF NSQIGKCEQF SYGSCGGNKN NFFDRQSCEA KCSPVIIPKV VASLPRECTF
EKDEGFGGGY HPKYYFNFRN LHCEQMIYQG QGGNENRFDN KIKCENSCIN VDGSNIRNEE
IKPKFVVQPP RFVPESKDGE TFGKDNLKNS FNNDNKNFKA AKIAQTADRL GNTGYPSPVT
DVQTEITATA NTYAQYNAKT LQPESTASIQ ESTLSAINIG STVVPDNGGY PEVSLVPSSA
KSSESTTPSP VTASSTTTGY ETAESIKNGE VKPSTTIKEI ETTPYEVETT QTFETTASPQ
TVKIQTSEQQ TTQRQTKYES TETTIYVNQN INEVEIQQTI APIPVTESVP IVTKNENEIK
ETVRTLPTIK IESIKEKSTD RQTLPTVETT PEVHIETEPP TQPTEEIIKV AENIETTRHI
ERILVSSTTE RVPISPTVNI ATNLAIGDKK IIHPPSTIVT TNITEIEDIT SEKSDVKKLN
IKPITTTTRQ QTTDEEIATT PLEEVSTTNI ELSTQKIELS TQDLTSQEST TQHLTTEEST
TQTKESIEET FPHGGQSSED DKDLLNVNEI PRKDEPEKKD EYKTELLNKN IISKLPKENL
PTVAPSPPSK HDYQNRGGIV AGGLPNVEVS KDSSHLEELS VTLHPKIPVC PNKKNALADR
FGHPLSCLPG KQACPTKSAC IYNGVNFYCC PSSEDPYDHH VFGGYNGEES KNGYKPLAKT
LNILSLSSNR PINRVKRESL GLDHVYKSIR FEGAPVKQVS RANRLHVNGK MLSICTLEVS
RGNCEESHIR YFYDARLDQC RMFYFSGCQG NGNNFATQSD CERLCKAKVE EIKSNVDEQK
SSIKKDICGV DKVPFGGENP LTCGNGKDSI GCPVGYECRN ESPFICCPKT VEESEDVNQL
TIKDIISKKN EKDSASITKL NKPYNPYKSN LPRLRTQSGI VVASSTDICP DGSDSLKDIK
SGRSVDCGTG GDGHPLCPVG YYCSMDSFTN TRLCCQLGSI GTKLHAPVNE SPFINQRKAN
SGEVVSKPTL PIDANVVSTT PKSSEPLPIA IPSVIEKKVN TKTYDHMMIK PTNRANNQRE
LVVEENPRLA IDETKEVGIK HNEDSSILMV DEIGTVESKI VADKTACHIR PSEGRACRED
EPSPRTNLQY FYSIKDKKCK LFFYRGCGGS INRFESKKAC EALCMMD
//
