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Database: UniProt
Entry: E4XH71_OIKDI
LinkDB: E4XH71_OIKDI
Original site: E4XH71_OIKDI 
ID   E4XH71_OIKDI            Unreviewed;      1067 AA.
AC   E4XH71;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=GSOID_T00010841001 {ECO:0000313|EMBL:CBY10019.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY10019.1};
RN   [1] {ECO:0000313|EMBL:CBY10019.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; FN653050; CBY10019.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4XH71; -.
DR   InParanoid; E4XH71; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000001307};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1067
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003192954"
FT   TRANSMEM        1019..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          243..499
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        252
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        283
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        447
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1067 AA;  120965 MW;  72B367B6DFE6F9B0 CRC64;
     MTLFHFLPLY ICLLTTALAD TIRTSDPIAI VDITVKPCSS CLPQTSTAIA LTVYNAEDLR
     KSVLEWRRKR SKQQQEKLGE HENSESEISI KAVDDQWLVI FDGYYSQEHR HKVILTALSG
     QHVEIVARDN PAAVFESDFD VLLWPYDERK KLESLLDEHE DIKEVKQQKQ ISRKLQYIKS
     QDTYLPSEAR VHRAGQRKPQ SVSSSDYWFG SEKLRSRKLM RSVVKPVTDE LQADILWDLG
     FTGAGIKVAI FDTGLPKNHP HFRNVKDRTN WTNEKSLDDG LGHGTFVAGI IASSAECMGF
     APDADVHVYR VFTNQQVSYT SWFLDAFNYA ILSQDVLNLS IGGPDFMDTP FVDKVWEMSA
     NGIIMISAIG NDGPLYGTLN NPADQMDVIG VGGTDFAHNI AKFSSRGMTT WELPAGYGRV
     KPDIVTYGSS VRGSGIYSGC RTLSGTSVAS PVVAGVVTLL YSTVPEEKRH FVNPASMKQA
     LMHGAKRIDG TNMFEQGAGR VDLIQSWKIL KSYKPQATLS PPYIDFMDCP YMWPYCSQSL
     FHTGMPTIAN VTILNAISVS SKIVGIPIWR PYDQETGHFV DISVSHSSVI WPWTGYIALT
     IMINEKGAEF EGIISGHLEF FVHSKNDDNN EDIEENVVIS EMKLPLRISV IPTPKRWQRV
     LWDQFHNLRY PPGYFPRDNL KMKNDPLDWN GDHIHTNFRD LYERLRAAGY FIDVLGESFN
     CFDASNYGTL MIVDSEEEFF AEEIEKIAKD VEGGLNLIVF GDWFNTEVMK KVRFFDENTR
     QWWIPDTGGA NVPALNELLE PFEIGLGDIV SDGEFEFSER KMNFASGTSL VQFPDQGKVL
     VRNLRDQGAD ILRNEKDETF KPKENTVAIF GVHEYKLGKV AVYGDSNCID GAHMQKECYW
     LVEELLQYFR TELFAEELVS DLVEWSAVKE QFESFSTLPE RFVGNQLHRF SKVLVPGLSM
     KNKPIPECRE LTFLTPQYLN DSKSTLSWKN RPLLSIDWEE ENLEIQSYKP LPLSHPETFS
     SATVFIVFSA CGAALLFLLA QMRSRKNERS QKPLKFSKSR SNKNLST
//
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