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Database: UniProt
Entry: A0A2B4SWX2_STYPI
LinkDB: A0A2B4SWX2_STYPI
Original site: A0A2B4SWX2_STYPI 
ID   A0A2B4SWX2_STYPI        Unreviewed;       704 AA.
AC   A0A2B4SWX2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=PC3-like endoprotease variant B {ECO:0000313|EMBL:PFX33370.1};
GN   ORFNames=AWC38_SpisGene1693 {ECO:0000313|EMBL:PFX33370.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX33370.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFX33370.1}.
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DR   EMBL; LSMT01000012; PFX33370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4SWX2; -.
DR   EnsemblMetazoa; XM_022944685.1; XP_022800420.1; LOC111338242.
DR   OrthoDB; 2996461at2759; -.
DR   Proteomes; UP000225706; 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; 3.30.70.850; 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:SF30; ENDOPROTEASE AEX-5; 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   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:UP000225706};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..704
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013038566"
FT   DOMAIN          473..603
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          196..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
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   704 AA;  78570 MW;  AFDD7A7BE2071216 CRC64;
     MVNVVLFVFL VSLSVVYCES DHGDGEIYTN TWAVELDSHD EELAHNIAEN LGFKNNGPIA
     NLPGYFAFVH EKSERRQRRS SHTQLLDHPR VKWAEQQTVL IRQKRGFNTW DEALMLVERA
     QRNRRLFNDP LWKNQWYMGT LDFADTRGNL GVLQAWKMGY TGKGIVVTIV DDGLDHTHPD
     LSKNYDEAAS LDVNNKTSVG VDHDPTPDDT NLSNDHGTKC AGEVAAEADN NICGVGVAYN
     AKIGGIRMLD GTITDQIEAE ALGYNCDYID IFSASWGPKD DGKTFGKPER LGSGAMEKCV
     REGRDGKGVL YIWATGNGGA SQDDCSCDGY TSSIYTLSIA SVSANGCKTF YDESCPSTMG
     VVFTGDVGSQ CSKRESYSHL VTTSLFHKCV TSFSGTSCAA PLAAGIFALV LEANPDLTWR
     DMQHLVVKTA RKNEPDSPSW STNGAGHKYS RSYGFGVLNA EDLINAAKEW EHVDTQQKYT
     LRGLLTPDTA TLRSKGEVEL KLVNDKEDIQ KLEHVQFNVS IDHRRRGDLV IDLISPSGTT
     SRLLAKRPRD DGTRLAYWPF MTVEFWDEDP QGEWIVKIRD EKSENDYSPR SHGILFDEGE
     SRDEPSIAND LSHGRFKEDY MSLSKRSKEK RHEKFPQRSE DQPSFQRELI HGRFKEDYMK
     SVKGPNQPIN VASDESSMCS HSKSLQGPIA GCVRNWSLVM YGTA
//
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