ID   A0A0W0G928_9AGAR        Unreviewed;      1145 AA.
AC   A0A0W0G928;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WG66_2369 {ECO:0000313|EMBL:KTB45068.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB45068.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB45068.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB45068.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTB45068.1}.
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DR   EMBL; LATX01000791; KTB45068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0G928; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
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; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..183
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          265..433
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          452..761
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          764..949
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          223..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  128882 MW;  D11C947170B3E55A CRC64;
     MAIDASLWKR ITSGHDIPPY SILTKTIEKS PQDDREYRII KLENGLEAML VHDAKADKAA
     ASLDVAVGHL SDPDDIPGMA HFCEHLLFMG TENFPKENEY SKYLAKNNGY CNAYTSDSNT
     NYYFDVSTSH LSGALARFAA FFHCPLFSPS CTSRELNAVD SEHRKNDQAD LRRVFQVNKH
     LSKEGHPWNK FGSGNRESLS KHAKELKAKG KLAANGMLDL DSESATPQVL PSPIPSRMAS
     PAPSDVSTAS ELGNEADGGA VGRETRRRLV EWWEKEYCAG RMHLCVIGKD SLDHLSELVS
     TLFSPIPNHG LDPLPTISDH PFGPNEKGTL ISVQTIMNLH VLEIFIPLEP QANNWRHKPA
     NFLAHLIGHE GPGSLLSFLK AKGLVASLNS GPLELGRGFD VFVVVIELTQ EGFRNYQSVI
     LATFKHFNLL RSQLSFDAYH QREIATLSSI WFRFIEKQRP DNYATYIAEN MAKPYPRELL
     LVAPSVTWNW GDQYQGDPAL SGGTAGEEKV KEYLQGFQID NSRVVLMGKE QELDKVKQFN
     NTIEKWQEEP WYRTKYRVVH FPEEFIKACS NSTSTTPELF LPQPNQFIPQ NLNVDKKDIT
     TPLCRPHLIY DTSLCQVWHK KDDHFWVPKA HVVIDICSPF ANSTSQATLL TQLFTDLITD
     SLTEFSYDAS LAGLSYSCTS HSKGVYIALQ GYNDKMHVLV RQVLDKVKNL VVIPDRLDIM
     KEQTKKNLEN FFLIQSHELA DYYTFYLMSE TAWTAEELLK ELPSITVEEV QKHGLYLLSQ
     VHMNILVMGN VTQDQAVEIA ELAENIVGNL KDGLQPSDLN EYALVLPPGS NFVYSTDVGN
     PDQTNNAITY YTHIGPVNDQ HLHVVSSLLT QIMTEPTFNI LRTKEQLGYI VSCGGILLPG
     STLKGIAIVI QSEKTPGYLE SRVDAFLDYM KNMIEEMSEE AFTEQKAGLE KRWREDYKNL
     SEEANAYYWY IDSGSWDFYR RENDAEKLKD VTKDEVMKCF MEYVHPSSQT RAKLSVHLHA
     KKSPPKKVSV AAAEAFGKLV QDANLGLNGV VPDGALADDI PLVDNFQAYW DGVFKTVGKE
     DITSSLLEAI PGLVEKYPLE GEGRDGPIEG ATYIEDPLAF RRSLKKSDYY PPVVIWQDNL
     IDMGR
//