ID A0A0V1D8V3_TRIBR Unreviewed; 1067 AA.
AC A0A0V1D8V3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Endoprotease bli-4 {ECO:0000313|EMBL:KRY57911.1};
DE Flags: Fragment;
GN Name=bli-4 {ECO:0000313|EMBL:KRY57911.1};
GN ORFNames=T03_2800 {ECO:0000313|EMBL:KRY57911.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57911.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY57911.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57911.1};
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:KRY57911.1}.
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DR EMBL; JYDI01000026; KRY57911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D8V3; -.
DR Proteomes; UP000054653; 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:UP000054653};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1067
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876522"
FT TRANSMEM 980..1004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..591
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 106..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY57911.1"
SQ SEQUENCE 1067 AA; 118412 MW; D4AC1D82BD7FA091 CRC64;
LMFKIVILLW LWQQMVASGP SDGEFSKIGN VTSNVVVQLQ FDDSEHADIV ANKHGYKNMG
KVGSLKGVYW FKKYDHYISK REIKERLDGD PEVLWHEFET PKKRVKRDGL LDDESNRQST
RESSVEWPDP LYSQQWYLNG FVGDGMRVRE AWSMGYSGKN VVVSILDDGI QGDHPDLAAN
YDAMASHDVN DGDDNPYPRD NGDNRHGTRC AGEVAAVAGN SFCGVGVAYN ARIGGVRMLD
GPVSDRVEGS ALSLRQQHID IYSASWGPED DGKTFDGPGR LAKMAFYQGV TEGRNGKGNI
YIWASGNGGT FKDSCSCDGY TVSIYTLSVS STTFDHKQPW YLEECPSTLA STYSSGLINQ
PAIVTTDMPN TCTTHHTGTS ASAPIAAGIV ALVLEANSNL TWRDMQHLVV RTSDPTPLLN
NPGWIVNGVG RKVSSKFGYG ILNAEKLIRL GKKWKTVPTQ HVCTFVYEMP DPILLNGQFL
KNITINVNGC PQGAPVRYLE HVQLVMSVQF SRRGDLRIRI TSPSGTESEL LPPRLNDGSD
GGFIKWPFMS VQQWGENPEG KWIVTLENVG NPNNRGTFHD CLLTLYGTEE MAQPSELEMD
EELGKNSPPA LFGTSNFVSD MAGHQELLQY YQIESIFFTH VEFGIGVNFG DVILKKNCHP
ECENGCRMVN SSLDCVSCKH YYQELRNRGG SKCVSKCEPG YYLDTNARRC NLCLRGCATC
SSATLCDTCL PSMFLIVSDP EHLWHGKCET ECPDGFLAEE NKINGARRCL FKCDEGCLNC
TAEGPCRFCK FGYFLNSFGH CVKSCGDGYY DDVNKRKCVK CPQNCEQCSK NANICQVCKF
DYALNSVGQC EPQKLRPCDR NEQCPLNSYC EKSGHVCQAC HPDCAKCIGP GFDQCTLCKD
GQAPNPKSND CSCKRGYYFN AKFVTCEKCH IACAVCNGPG TNFCSECNPG YSLLGSSCIR
CCGNNESSSR FCSSFTSSQY SIKTVVIGSC ISAAILFIVI FGALMTCDWY RKSRNVYEYS
NVPIYFNSDS VKLLENEYDE KFEEHDNQLS HVQDDSDVVI DVLMERA
//
