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Database: UniProt
Entry: A0A1X7VDL0_AMPQE
LinkDB: A0A1X7VDL0_AMPQE
Original site: A0A1X7VDL0_AMPQE 
ID   A0A1X7VDL0_AMPQE        Unreviewed;       771 AA.
AC   A0A1X7VDL0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   Name=109580538 {ECO:0000313|EnsemblMetazoa:Aqu2.1.38116_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.38116_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.38116_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   RefSeq; XP_019849385.1; XM_019993826.1.
DR   AlphaFoldDB; A0A1X7VDL0; -.
DR   STRING; 400682.A0A1X7VDL0; -.
DR   EnsemblMetazoa; Aqu2.1.38116_001; Aqu2.1.38116_001; Aqu2.1.38116.
DR   GeneID; 109580538; -.
DR   KEGG; aqu:109580538; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   InParanoid; A0A1X7VDL0; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000007879; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   3: Inferred from homology;
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:UP000007879};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..771
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010857469"
FT   DOMAIN          133..376
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        180
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        340
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   771 AA;  83961 MW;  607E12FDD0172227 CRC64;
     MNLGWSLVLL FLQFLSIAEP AKVIRAAPED TTTGNYIIAL SEGTSQERFR EIEEGVKNSG
     SVIYTKVNGE YAKIISANLS EQTLEKFSEF EDIEFIEEET YATASSEVSW ALDRINQQNN
     NKLDGYTNYN GDGQGVAIYI LDSGINYEHC EFGGRAMFSG YDPVDKIMGT NYKGRDCSGH
     GTHTASIAAG ASSGVASKAK VYSVRVLDCD NRIPWSAVID GLNHVGEKIT EAKAGKNPSV
     ILLPLSGPVS LGMDHTLEKL LNQNIPIVAA GGNDGGDACS KSPASTPGVI TVSASSNGDE
     ASSTTNAGPC IDLFAPGVSV VGANHSCTGC ECKSIRSGTS VSSGLVAGVV SLYLQESPRL
     TPSEVRDKLL NSCTRNTLHF ESLPQHLSGL TNNCLLYINT TIKMGDNLAL DPTNVVTTKT
     VTVSIQASPT PETVCCQMVK NFESFELSLG NIVEREMYKA TQMLQSNITS LFTLNSTQSA
     VAPSDKPDDN NVAVRKSLRQ KTYVHGTAVK SCKDLSHYGP LDSDYYPIIM QTGDEAMVYC
     ELDKEIMGQR GFMRIANVNM SDPNTDCPDG LLLRTDGNLR TCQRSQHESG CSTTYFSSSG
     VEYSRVCGRI KGYQWASPNA FYFSYQNKMK ILPMIDEAFV DGVILTYKEG ESRKHIWTFA
     AATDEIDRSQ SYACPCTNTY SRASSAIPAF VGNDYFCETG SRSTFEYNTL YTEDPLWDGK
     GCGEVSTCCD KGEWFCKDVP KTSSDIELRL CGNEPRENED TPIELIELFV Q
//
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