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Database: UniProt
Entry: A0A0N4ZYY1_PARTI
LinkDB: A0A0N4ZYY1_PARTI
Original site: A0A0N4ZYY1_PARTI 
ID   A0A0N4ZYY1_PARTI        Unreviewed;       892 AA.
AC   A0A0N4ZYY1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=P/Homo B domain-containing protein {ECO:0000313|WBParaSite:PTRK_0001399600.1};
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_0001399600.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001399600.1}
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; A0A0N4ZYY1; -.
DR   STRING; 131310.A0A0N4ZYY1; -.
DR   WBParaSite; PTRK_0001399600.1; PTRK_0001399600.1; PTRK_0001399600.
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; cd00064; FU; 3.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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   PANTHER; PTHR42884:SF23; FURIN-LIKE PROTEASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00261; FU; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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          422..560
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          148..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   892 AA;  98605 MW;  D1F18C528B98D855 CRC64;
     MFCTGRPFLE ASYFVEHNDN NHYRRKRSVI HEKINSHPEV LSITLHHERK RVKRGYLYSD
     GKKPFFGPED DGKHLINKRD SNDLEIPSLP FKDPLYKDQW YLIGKAVGGY DMNVREAWLL
     GYAGRNVSIS ILDDGIQVNH PDLAKNYDPM ASTDINGGDN DPTPQNNGDN KHGTRCAGEV
     SAIANNNQCG VGVAFESKIG GVRMLDGPVS DAVEAASLSL NQQHIDIYSA SWGPEDDGKT
     FDGPGPQARQ AFYRGIKQGR NGKGNIFVWA SGNGGSRQDS CSADGYTTSI YTLSISSATY
     HNSRPWYLEE CPSTIATTYS SASINQPAIV TVDVPNGCTK SHTGTSASAP IAAGIIALAL
     EANPSLTWRD MQHIVLRTAN PTPLLNNPGW SVNGVGRRIS NQFGYGLMDA GALVKLAKVW
     TTVPEQHLCT YKYQMSEPSP RSVSGRFEMN FTLDVNGCAD GTPVLYLEHV QVISSIRYSK
     RGDLKLTLYS PKGTRSVMLP IRPQDYNSNG FHKWPFLSVQ MWGEDPRGTW TLKIESFTNN
     NKIGGTIHDW DLLLYGTEKP AQPSDPEYPP AIPSFNKAST KKGFFDQAAE TLQNKEEQND
     TRTSINNNKG DNSISFGDLH SVGNCHEQCL GCSESKSAVS CFACKVYTQS LRNRYGFKCV
     DKCDDGYYLD GDKCKQCGKH CKSCVKAEVC ETCYGAQLLI DVDHWGHFDH GQCVDICPEG
     LYADYDTNSY QARCVLKKNP CSDGYYMPFT GKACQVCDEA CGKCHGPGLQ MCDECANGYG
     NRTMGYCRKC CDMSENPHTS NCEDCANYKP LPDTKDEHSI LSNFLLKVLL FAITITGGIM
     YCIFKTTGSE LSNSFRNRSS NYTQLPIMSS SKLLTSEEDS ESEDDLDATL RV
//
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