ID A0A0V1PJY1_9BILA Unreviewed; 1064 AA.
AC A0A0V1PJY1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Endoprotease bli-4 {ECO:0000313|EMBL:KRZ96519.1};
GN Name=bli-4 {ECO:0000313|EMBL:KRZ96519.1};
GN ORFNames=T08_830 {ECO:0000313|EMBL:KRZ96519.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96519.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96519.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96519.1};
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 -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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:KRZ96519.1}.
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 EMBL; JYDM01000007; KRZ96519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PJY1; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 4.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR043601; Rspo_Fu-CRD_dom.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF23; FURIN-LIKE PROTEASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF15913; Furin-like_2; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00261; FU; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..585
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1064 AA; 118105 MW; 2DE474245AD7AF1E CRC64;
MEFNAYSLFW GYLMFKIVIL LWLWQQMVAS GPSDGDFSKI GNVTSNVVVQ LQFDDSEHAD
IVANKHGYKN MGKVGSLKGV YWFKKYDHYI SKREIKERLD GDPEVLWHEF ETPKKRVKRD
GLLDDESNRQ STRESSVEWP DPLYSQQWYL NGFVGDGMRV REAWSMGYSG KNVVVSILDD
GIQGDHPDLA ANYDAMASHD VNDGDDNPYP RDNGDNRHGT RCAGEVAAVA GNSFCGVGVA
YNARIGGVRM LDGPVSDRVE GSALSLRQQH IDIYSASWGP EDDGKTFDGP GRLAKMAFYQ
GVTEGRNGKG NIYIWASGNG GTFKDSCSCD GYTVSIYTLS VSSTTFDHKQ PWYLEECPST
LASTYSSGLI NQPAIVTTDM PNTCTTHHTG TSASAPIAAG IVALVLEANS NLTWRDMQHL
VVRTSDPTPL LNNPGWIVNG VGRKVSSKFG YGILNAEKLI RLGKKWKTVP TQHVCTFVYE
MPDPILLNGQ FLKNITINVN GCPQGAPVRY LEHVQLVMSV QSELLPPRLN DGSDGGFIKW
PFMSVQQWGE NPEGKWIVTL ENVGNPNNRG TFHDCLLTLY GTEEMAQPSE LEMDEELGKN
SPPALFGTSN FVSDMAGHQV QNRSNIIRSN QFFFTHVEFG IGVNFGDVIL KENCHPECEN
GCRMVNSSLD CVSCKHYYQE LRNRGGSKCV SKCEPGYYLD TNARRCNLCL RGCATCSSAT
LCDTCLPSMF LIVSDPEHLW HGKCETECPD GFLAEENKIN GARRCLFKCD EGCLNCTAEG
PCRFCKFGYF LNSFGHCVKS CGDGYYDDVN KRKCVKCPQN CEQCSKNANI CQVCKFDYAL
NSVGQCEPQK LRPCDRNEQC PLNSYCEKSG HVCQACHPDC AKCIGPGFDQ CTLCKDGQAP
NPKSNDCSCK RGYYFNAKFV TCEKCHIACA VCNGPGTNFC SECNPGYSLL GSSCIRCCGN
NESSSLRCLG SFTSSQYSIK TVVIGSCISA AILFIVIFGA LMTCDWYRKS RNVYEYSNVP
IYFNSDSVKL LENEYDEKFE EHDNQLSHVQ DDSDVVIDVL MERA
//
