ID A0A183SQV3_SCHSO Unreviewed; 480 AA.
AC A0A183SQV3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=P/Homo B domain-containing protein {ECO:0000313|WBParaSite:SSLN_0000681001-mRNA-1};
GN ORFNames=SSLN_LOCUS6601 {ECO:0000313|EMBL:VDL92986.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000681001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0000681001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL92986.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL92986.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; UYSU01033766; VDL92986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183SQV3; -.
DR STRING; 70667.A0A183SQV3; -.
DR WBParaSite; SSLN_0000681001-mRNA-1; SSLN_0000681001-mRNA-1; SSLN_0000681001.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; Unassembled WGS sequence.
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; 3.40.50.200; 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 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 SUPFAM; SSF49785; Galactose-binding domain-like; 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, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 288..422
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 480 AA; 51910 MW; CA753FEB06A7325B CRC64;
MINFHVQLND GSNPASPAAG LDINVAPVYL AGYSGSGVKL IIIDDALDSE HDDIKPNIDL
SLTDDIVDAE RTGPRGTDGK MPEKDNHGTR CASLAGAVAN NSKCAYGIAH NVTIGGIRLV
HGTVTSIMTA EAIVRFAHLA QVISSSWGPT DSGKLMIPVN SHVDRALRYA VTMGNHGLGA
AVFFPAGNGG MQFDHCGADS YVNHPATIAV TSVGHIGLPP YYTEKCPAIS VTVPSGGYAD
SEPDFVVKGT DMSALPVAAI NNECREDFYG TSAAVPIAAG AVALAYEAKS DQIYAGQTTK
FKFNIPEAKG RFETRNGRKG HCFVDSLEIV TVHMQWVHTN RGHLRVTLVS PGGMIVDLLG
PRKLDHFSGS SEISWKSLMN FGEAGSGEWH VLITDTKIST KKHDQTGCVW YIRLELHGTE
SGKDCFSKNR EIILPMWTQL QENARNLTKS HKLNAEEIAD IYNRQRWNAL KMELPQKDTR
//