ID A0A0V1PJV5_9BILA Unreviewed; 1043 AA.
AC A0A0V1PJV5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Endoprotease bli-4 {ECO:0000313|EMBL:KRZ96515.1};
GN Name=bli-4 {ECO:0000313|EMBL:KRZ96515.1};
GN ORFNames=T08_830 {ECO:0000313|EMBL:KRZ96515.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96515.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96515.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96515.1};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KRZ96515.1}.
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DR EMBL; JYDM01000007; KRZ96515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PJV5; -.
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:InterPro.
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; 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; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRZ96515.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW 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 961..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 453..588
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"
SQ SEQUENCE 1043 AA; 115847 MW; A625E98223E8217A CRC64;
MEFNAYSLFW GYLMFKIVIL LWLWQQMVAS GPSDGDFSKI GNVTSNVVVQ LQFDDSEHAD
IVANKHGYKN MGKVGSLKGV YWFKKYDHYI SKREIKERLD GDPEVLWHEF ETPKKRVKRD
GLLDDESNRQ STRESSVEWP DPLYSQQWYL NGFVGDGMRV REAWSMGYSD HPDLAANYDA
MASHDVNDGD DNPYPRDNGD NRHGTRCAGE VAAVAGNSFC GVGVAYNARI GGVRMLDGPV
SDRVEGSALS LRQQHIDIYS ASWGPEDDGK TFDGPGRLAK MAFYQGVTEG RNGKGNIYIW
ASGNGGTFKD SCSCDGYTVS IYTLSVSSTT FDHKQPWYLE ECPSTLASTY SSGLINQPAI
VTTDMPNTCT THHTGTSASA PIAAGIVALV LEANSNLTWR DMQHLVVRTS DPTPLLNNPG
WIVNGVGRKV SSKFGYGILN AEKLIRLGKK WKTVPTQHVC TFVYEMPDPI LLNGQFLKNI
TINVNGCPQG APVRYLEHVQ LVMSVQFSRR GDLRIRITSP SGTESELLPP RLNDGSDGGF
IKWPFMSVQQ WGENPEGKWI VTLENVGNPN NRGTFHDCLL TLYGTEEMAQ PSELEMDEEL
GKNSPPALFG TSNFVSDMAG HQNFGDVILK ENCHPECENG CRMVNSSLDC VSCKHYYQEL
RNRGGSKCVS KCEPGYYLDT NARRCNLCLR GCATCSSATL CDTCLPSMFL IVSDPEHLWH
GKCETECPDG FLAEENKING ARRCLFKCDE GCLNCTAEGP CRFCKFGYFL NSFGHCVKSC
GDGYYDDVNK RKCVKCPQNC EQCSKNANIC QVCKFDYALN SVGQCEPQKL RPCDRNEQCP
LNSYCEKSGH VCQACHPDCA KCIGPGFDQC TLCKDGQAPN PKSNDCSCKR GYYFNAKFVT
CEKCHIACAV CNGPGTNFCS ECNPGYSLLG SSCIRCCGNN ESSSLRCLGS FTSSQYSIKT
VVIGSCISAA ILFIVIFGAL MTCDWYRKSR NVYEYSNVPI YFNSDSVKLL ENEYDEKFEE
HDNQLSHVQD DSDVVIDVLM ERA
//
