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Database: UniProt
Entry: A0A2G8K2U7_STIJA
LinkDB: A0A2G8K2U7_STIJA
Original site: A0A2G8K2U7_STIJA 
ID   A0A2G8K2U7_STIJA        Unreviewed;       381 AA.
AC   A0A2G8K2U7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   31-JUL-2019, entry version 8.
DE   SubName: Full=Serine proteinase {ECO:0000313|EMBL:PIK42293.1};
GN   ORFNames=BSL78_20854 {ECO:0000313|EMBL:PIK42293.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa;
OC   Holothuroidea; Aspidochirotacea; Aspidochirotida; Stichopodidae;
OC   Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK42293.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK42293.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK42293.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK42293.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X.,
RA   Xing L., Huo D., Sun M., Wang L., Mercier A., Li F., Yang H.,
RA   Xiang J.;
RT   "The sea cucumber genome provides insights into morphological
RT   evolution and visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|SAAS:SAAS01201832}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PIK42293.1}.
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DR   EMBL; MRZV01000944; PIK42293.1; -; Genomic_DNA.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 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; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000230750};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01077244};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|SAAS:SAAS01201830};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Serine protease {ECO:0000256|SAAS:SAAS01201831};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     39     58       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       65    136       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      164    374       Peptidase_S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   381 AA;  39658 MW;  86F7F3FE3ADC0673 CRC64;
     MQYLIAFNAI ALSTLGLLKP CNGILHQPKL SNVKCMKFLL IALFATAASA MIAPLHTVKE
     KIDGSYIVVF NDDAKTLASV STIKNSPFFS SLGGRVDRVY GSALNGFAAT LAPKALELVR
     RFNFVKYVEE DQIMRIDAVA SWGLDRVDQQ DLPLDNSFTP RNDGEGVNVY VIDTGINPTH
     VDFGGRAYTE ASMDFVSINR GGVDCNGHGS HCAGTVGGTT YGVANQANLF GVRVLSCLGS
     GSNTGVIGGM DWVADNHVKP AVASMSLGGG PSQSSDDAVT RMHNAGVTVV VAAGNDNEDA
     SNHSPARAPL AITVASSASD DTRSSFSNFG SLIDIFAPGS SITSAGGAAI LLAQDSSRTP
     DDVVNTMTSE ATSGALTDPN L
//
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