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Database: UniProt
Entry: A0A1S9DXV2_ASPOZ
LinkDB: A0A1S9DXV2_ASPOZ
Original site: A0A1S9DXV2_ASPOZ 
ID   A0A1S9DXV2_ASPOZ        Unreviewed;       645 AA.
AC   A0A1S9DXV2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   05-DEC-2018, entry version 9.
DE   SubName: Full=Peptidase S53 propeptide {ECO:0000313|EMBL:OOO13889.1};
GN   ORFNames=OAory_01024840 {ECO:0000313|EMBL:OOO13889.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO13889.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO13889.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO13889.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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:OOO13889.1}.
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DR   EMBL; MKZY01000001; OOO13889.1; -; Genomic_DNA.
DR   Proteomes; UP000190312; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000190312};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    645       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010537984.
FT   DOMAIN      225    644       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    301    301       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    305    305       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    562    562       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       603    603       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       604    604       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       622    622       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       624    624       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   645 AA;  70115 MW;  920AF3B610B8AF82 CRC64;
     MKTSFLLLHT LVAGVLAIPT RTDYVLHERR DAVPAHWTGE KRLDGQTVLP MRIGLTQSNL
     DRGHDLLMEV STPGSPRYGD HMTLDEVHNL FAPSQDSVDS VRSWLESAGI SPDRISQSTN
     KQWLQFDAGV DEVEQLLKTE YYRYSHAGTG RSHVACREYH VPESVQSHID YITPGIKHLE
     IREEKPVEKR SLDKRSFGIL PPILRPLTLP LEELLGQLLL LCDVAVTPAC IQAMYNVTDG
     DKATKGNELG IFEDLGDVYS QDDLDLFFST VAHKIPTGTH PILNAIDGAQ APADTTNAGT
     ESDLDFEISY PLIWPQNSIL FQTDDPIYQN NYTYNGFLNN FLDAIDGSYC SEASPLDPPY
     PNPADGGYKS PRQCGVYKPT NVISISYGGA EADLPIAYQR RQCQEFMKLG LQGVSIVVAS
     GDSGVQGRGG SPTPSGCLGK DNKVFAPDFP ATCPYLTTAG GTYLPPGADV HAHEEQATTS
     FPSGGGFSNI YQRPDYQNAA VEEYFNTAQL SYPYYESVDN SSFAANGGIY NRIGRAYPDV
     AAIADNVLVF NKGLPTLVGG TSAAAPVFAA LLTRINEERL AAGKKTVGFV NPVLYANPGV
     FFDVTKGSNQ GCGTDGFPAV KGWDPVTGLG TPNYPKLLEL FMGLD
//
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