ID   A0A0R3RJB0_9BILA        Unreviewed;       590 AA.
AC   A0A0R3RJB0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=P/Homo B domain-containing protein {ECO:0000313|WBParaSite:EEL_0000156901-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000156901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000156901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   AlphaFoldDB; A0A0R3RJB0; -.
DR   STRING; 1147741.A0A0R3RJB0; -.
DR   WBParaSite; EEL_0000156901-mRNA-1; EEL_0000156901-mRNA-1; EEL_0000156901.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR008979; Galactose-bd-like_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; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          474..590
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        199
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        397
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   590 AA;  65728 MW;  F575C3E9172DEC38 CRC64;
     MLISDYSRRD CAVNSFQLNN RILFVTVCHV LCPIPKLIVT KANDEEEYGN EWVVEIVGGP
     QEAKDIARAV GYKYIAPVRG FDNVYIFSKE NHRGKRKADS KSTLALCRHK HVLWAEQQRV
     HKRFKRDHID AASSALNDVN YSNNVFFNDP FWPQQWNLVS NEIIQKNSRT INGQPISMHV
     MKAWELGYTG KGVVVTILDP QASYDLNDND PDPMPKFNEL NRHGTRCAGE VVMTPNNSFC
     GVGIAYNAKI GGVRMLGGKV TDRTEAEALS YNIDHIDIFS ASWGPMDDGK TVEGPGRLTQ
     KAILKGIQQG RGGKGVIYVW ASGNGGIQDD DCGCDGYMDS IYTLSVSSVT KDGTSPWYAE
     KCAATLTSTF SNGHHEEQMI TTTDIENKCT GTFAGTSASA PMAAAIIALG LDANPSLTWR
     DVQHITVWTS DPMPLLNINE GWNKNARGLL VNSRFGFGLM DASAFVKLAK TWENVPEQHV
     CSTVFPTFSK REINDESITV IKFRTDGCEG QKNEINFLEH IHLILDAHYP IRGHLSISIT
     SPEGTKTQLL SVRRRDKSSA GFHHWPFMSV HTWGENPRGI WQLDIEDQVN
//