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Database: UniProt
Entry: A0A0D0CQ44_9AGAR
LinkDB: A0A0D0CQ44_9AGAR
Original site: A0A0D0CQ44_9AGAR 
ID   A0A0D0CQ44_9AGAR        Unreviewed;       642 AA.
AC   A0A0D0CQ44;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   SubName: Full=Unplaced genomic scaffold GYMLUscaffold_24, whole genome shotgun sequence {ECO:0000313|EMBL:KIK61117.1};
GN   ORFNames=GYMLUDRAFT_59078 {ECO:0000313|EMBL:KIK61117.1};
OS   Gymnopus luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Omphalotaceae; Gymnopus.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK61117.1};
RN   [1] {ECO:0000313|EMBL:KIK61117.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK61117.1};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (APR-2014) 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};
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DR   EMBL; KN834772; KIK61117.1; -; Genomic_DNA.
DR   MEROPS; S53.007; -.
DR   EnsemblFungi; KIK61117; KIK61117; GYMLUDRAFT_59078.
DR   OrthoDB; 1294880at2759; -.
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   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    642       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002208760.
FT   DOMAIN      223    641       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    550    550       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       593    593       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       594    594       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       619    619       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       621    621       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   642 AA;  68693 MW;  5266CA3EDB7BFA0C CRC64;
     MFFPLVFLAL GPIAFENGVA ASSSIIHSDH VVHEIRALEP FDWSISHQPR AHKRLPLRIG
     LSQRNVENLE SMLMAVSHPD SPNYGKHWTP QQVMDTFAPS EESAQNVIAW LKDAGFSPEK
     IRISANKGWI QVDTTVAEAE DLLKTEYHVY THPCHNYSVP AAIQEHVELI RPTVHFTHRP
     SLKSEAKFKR AGILGKPSPG TGPITSSIDT LPVPPGLIEC AQMMTPGCLR ALYNVPQFNP
     LAMDKNSYGI VEFTPQAFLA DDLDLFFSTF SPNVVGARPQ IVLVDGAVVQ NTSQGSDFNG
     ESDLDLEYAM ALTYPQNVTL LQTGDLVEGA GFDNWLDAVD GSFCTFDGGD DPFQDGIYPD
     TLPGGFDGPE SCGIVAPPLV VSVSYGEQEW QITSSSATRQ CNEYGKLGLM GTTILYSSGD
     NGVAGLGGQC LDSSARPVSS GGTRFNPQFP ASCPFVTSVG ATQMNPNSTI VDPEAACETH
     IFSGGGFSDI FSMPDYQKSA VSSYLTNDPP PYTSSQFNTS GSRAYPDLSA NGANYVAGVN
     GQLMLEFGTS AATPVVGSFI TMINDARLAA GKGPVGFINP AIYSDAFKDG FNDITEGSNP
     GCMLSLYLID TVGFIATDGW DPVTGVGTPN VSKLISLFLA LP
//
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