ID   A0A0N4ZN75_PARTI        Unreviewed;       714 AA.
AC   A0A0N4ZN75;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=P/Homo B domain-containing protein {ECO:0000313|WBParaSite:PTRK_0000999000.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000999000.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000999000.1}
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; A0A0N4ZN75; -.
DR   STRING; 131310.A0A0N4ZN75; -.
DR   WBParaSite; PTRK_0000999000.1; PTRK_0000999000.1; PTRK_0000999000.
DR   Proteomes; UP000038045; Unplaced.
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; 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; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_2; 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; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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          525..658
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          245..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        276
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        450
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   714 AA;  80260 MW;  46B4D0E68EFE52D8 CRC64;
     MLKGYEIRLR KKEKKMLNFT NPVRLYKKLS ITFTLISFLI VYSNILCGYV TLAASNDDQK
     LSHSFKKTFK NEFAVKIVGG GADPSKAETL ANKHHLINLG PIIEGSDYFL FRNPNLKQRS
     RRKTRSLDTI SLSREHDVVW MEQQVAKRRV KRGYKKQNNI EELSPKMRLL SKKGSLNFFD
     EEKQNIKLLN PNDALWEDMW YLHRSDNEPY FNDHNVKEAW GLGYTGNGVV VTILDDGLEY
     NHPDIKPNYD PKASYDVNDD DDDPTPRYDY TDENRHGTRC AGEVAAVFNN SLCITGVAYK
     AKIGGIRMLD GEVTDAVEAK SLSYNTQHID IYSASWGPDD DGKTVDGPAK LTREAFENGI
     KNGRGGLGSV FVWASGNGGK EGDSCNCDGY TNSIYTLSIS SASEFGHIPW YSEACSSTLA
     AAYSSGSTSE RMIVTTDLHH SCTKGHTGTS AAAPIAVGIV ALTLEANPML TWRDIQHIVV
     QTSKPDGLIS EDWVTNGARR NVSHSFGYGL LDAGAMVKKA TKWKNVPRQR KCKITYPARY
     KTIPNNKRIV LLQHTSACSN TENHVRYLEH VQAIITLTAP KRGDIQVFLT SPRGTRSKLL
     QKRSKDISRV GFREWAFMTT HSWGELSEGT WSLEIENGGW DDAELQRWDL VFYGTLEEVS
     EFGGTEHKKL SGSHVTLRSA DSTKKISKIT SSHKFSFIQM FLSMVTFVLL RRIY
//