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Database: UniProt
Entry: B9U0R4_CRYGA
LinkDB: B9U0R4_CRYGA
Original site: B9U0R4_CRYGA 
ID   B9U0R4_CRYGA            Unreviewed;       193 AA.
AC   B9U0R4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:ACB41938.1};
DE   Flags: Fragment;
GN   Name=IDE1 {ECO:0000313|EMBL:ACB41938.1};
OS   Cryptococcus gattii (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=552467 {ECO:0000313|EMBL:ACB41938.1};
RN   [1] {ECO:0000313|EMBL:ACB41938.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=5032738 {ECO:0000313|EMBL:ACB41939.1}, F2863
RC   {ECO:0000313|EMBL:ACB41947.1}, Joe {ECO:0000313|EMBL:ACB41941.1}, LA1
RC   {ECO:0000313|EMBL:ACB41938.1}, LA175 {ECO:0000313|EMBL:ACB41945.1},
RC   LA584 {ECO:0000313|EMBL:ACB41946.1}, TP0688
RC   {ECO:0000313|EMBL:ACB41943.1}, TP1414 {ECO:0000313|EMBL:ACB41944.1},
RC   and WM179 {ECO:0000313|EMBL:ACB41940.1};
RX   PubMed=19517012; DOI=10.1371/journal.pone.0005862;
RA   Ngamskulrungroj P., Gilgado F., Faganello J., Litvintseva A.P., Leal A.L.,
RA   Tsui K.M., Mitchell T.G., Vainstein M.H., Meyer W.;
RT   "Genetic diversity of the Cryptococcus species complex suggests that
RT   Cryptococcus gattii deserves to have varieties.";
RL   PLoS ONE 4:E5862-E5862(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; EU408581; ACB41938.1; -; Genomic_DNA.
DR   EMBL; EU408582; ACB41939.1; -; Genomic_DNA.
DR   EMBL; EU408583; ACB41940.1; -; Genomic_DNA.
DR   EMBL; EU408584; ACB41941.1; -; Genomic_DNA.
DR   EMBL; EU408586; ACB41943.1; -; Genomic_DNA.
DR   EMBL; EU408587; ACB41944.1; -; Genomic_DNA.
DR   EMBL; EU408588; ACB41945.1; -; Genomic_DNA.
DR   EMBL; EU408589; ACB41946.1; -; Genomic_DNA.
DR   EMBL; EU408590; ACB41947.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9U0R4; -.
DR   MEROPS; M16.020; -.
DR   VEuPathDB; FungiDB:CGB_D1300C; -.
DR   VEuPathDB; FungiDB:CNBG_4635; -.
DR   VEuPathDB; FungiDB:I306_01873; -.
DR   VEuPathDB; FungiDB:I308_04444; -.
DR   VEuPathDB; FungiDB:I311_02542; -.
DR   VEuPathDB; FungiDB:I314_04542; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 1.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..101
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          129..177
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACB41938.1"
FT   NON_TER         193
FT                   /evidence="ECO:0000313|EMBL:ACB41938.1"
SQ   SEQUENCE   193 AA;  22444 MW;  08E24BCC1D4AB8E8 CRC64;
     EHLLFMGTKT HPSENAYQQY LSSHNGHSNA WTAMTSTNYY FDVSPDALEG ALDRFSGFFS
     EPLFNEDCTE REIKAVDSEH KKNLQNDVWR FYQLEKHLSK PGHPYGKFGT GNYESLWSVP
     KEAGRDPRRQ LIEWWEKEYC ARRMKLAVAG KEDVDTLEKW VKEKFENVPV RTEGKPEVGR
     EGVRVVFDES PYG
//
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