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Database: UniProt
Entry: A0A158PSX1_9BILA
LinkDB: A0A158PSX1_9BILA
Original site: A0A158PSX1_9BILA 
ID   A0A158PSX1_9BILA        Unreviewed;       950 AA.
AC   A0A158PSX1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=BTMF_LOCUS5956 {ECO:0000313|EMBL:VDO20518.1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000784201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0000784201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO20518.1, ECO:0000313|Proteomes:UP000280834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   EMBL; UZAG01015459; VDO20518.1; -; Genomic_DNA.
DR   STRING; 42155.A0A158PSX1; -.
DR   WBParaSite; BTMF_0000784201-mRNA-1; BTMF_0000784201-mRNA-1; BTMF_0000784201.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; 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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000280834};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          692..843
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          352..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        383
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        587
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   950 AA;  105736 MW;  F10224A42E6F5B51 CRC64;
     MALSRKCANP TYKHSVWDNQ KSAHGIYRVK INNETSVHTL NSVAKNELAC CSNADVFKFP
     IMNEENSVLK GNCTTYQICP LDRNYRSLSR QHFRIPVTSL LFIVLSLAFL SMPQFSSVAA
     DELNSSDAVI ELTPVGGSNN HNNGSYGTGT SQSSSTALRK AYTNQFAVRI TGGDTLEADK
     LAAKYGFINL GRVLPNDEYF LFESRQTRKR STRRRRNAQT NSIAREPKVE WIEQQIAKKR
     VKRDYMLMNT LSSTVHLQRF KGNEISDDLT IIGSDDVQQQ YASSRNRNAD IRSVGNYNLN
     DPLWSDMWYL NAAAYDRGLD HNVREAWDLG YTGRGVVVTI LDDGLERTHP DIAPNYDSKA
     SYDVNDRDED PTPRYDYTDE NRHGTRCAGE VAAIFNNSLC IVGIAYNARI GGTILPEFIQ
     AYRSKKMFFG EKTSTKSQLL IGIRMLDGDV TDAVEATSLA HNSDHIDIYS ASWGPDDDGR
     TVDGPAKLTR RAFEKGIREG RRGLGSIFVW ASGNGGKDAD SCNCDGYTNS IYTLSISSAT
     EHGNIPWYSE ACSSTLATAY SSGATGEKMI VTTDLHHSCT NAHTGTSASA PLAAGIVALT
     LEANPXXXXX XXXXXXXXXX XXXXXXXXXX LEANPKLTWR DMQHIVVRTA RPLNLRAGDW
     VTNGVGKKVS HSFGFGLMDA GAMVRLANNW TTVPEQRKCV VFYPARYKLN SLSFNLYFFN
     ILLFRIVPHG NRLQLQLYTD GCSSYSRNKV GYLEHVQAII TLTAPKRGDI QIYLTSPSGT
     RSTLLAKRAR DTSRTGFREW AFMTTHNWGE MAVGLWTLEI NNDGWDDAEL IRWDLVLYGT
     ATEVSNIGGT PSASSSSLTP RSLSSKVRNR YGALWEDTSA ASIITASNII ALFFLLCFIY
     LNFPSAEKSV KYYFGVFLLP ANVSLRHSDY FMVPKCYRLG CLTFNLKSEQ
//
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