GenomeNet

Database: UniProt
Entry: A0A1I7SI31_BURXY
LinkDB: A0A1I7SI31_BURXY
Original site: A0A1I7SI31_BURXY 
ID   A0A1I7SI31_BURXY        Unreviewed;       180 AA.
AC   A0A1I7SI31;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=Inhibitor_I29 domain-containing protein {ECO:0000313|WBParaSite:BXY_1270000.1};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1270000.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_1270000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A1I7SI31; -.
DR   WBParaSite; BXY_1270000.1; BXY_1270000.1; BXY_1270000.
DR   Proteomes; UP000095284; Unplaced.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF947; CATHEPSIN F; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..180
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018752289"
FT   DOMAIN          54..110
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
SQ   SEQUENCE   180 AA;  20428 MW;  8123003E264BA789 CRC64;
     MKFLLLPCLL AISAFGYVLV DNLKVSAGVE RTLKMAAEMR RGLGEGKEDV YGQFTDFIVK
     FEREYKDEQE VAQRFEIIEK SLKRIAELQK QSPTAQFGLT KMADLSEEEF GRIANLKVPA
     RNEDEEQDFL QLDISEEDLP KGHDWRKLNG VSSVKNQGDC GACFAFGTVG AIESQWRIKR
//
DBGET integrated database retrieval system