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Database: UniProt
Entry: Q2UHY2_ASPOR
LinkDB: Q2UHY2_ASPOR
Original site: Q2UHY2_ASPOR 
ID   Q2UHY2_ASPOR            Unreviewed;       645 AA.
AC   Q2UHY2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE58833.1};
GN   ORFNames=AO090023000263 {ECO:0000313|EMBL:BAE58833.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE58833.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE58833.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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};
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DR   EMBL; AP007157; BAE58833.1; -; Genomic_DNA.
DR   RefSeq; XP_001820835.1; XM_001820783.1.
DR   MEROPS; S53.007; -.
DR   EnsemblFungi; BAE58833; BAE58833; AO090023000263.
DR   GeneID; 5992837; -.
DR   KEGG; aor:AO090023000263; -.
DR   HOGENOM; HOG000217860; -.
DR   KO; K01279; -.
DR   OMA; ACREYHV; -.
DR   Proteomes; UP000006564; Chromosome 3.
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:UP000006564};
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:UP000006564};
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_5004217159.
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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