ID   V2WRF5_MONRO            Unreviewed;      1133 AA.
AC   V2WRF5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:ESK89443.1};
GN   ORFNames=Moror_16162 {ECO:0000313|EMBL:ESK89443.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89443.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK89443.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89443.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK89443.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWSO01000561; ESK89443.1; -; Genomic_DNA.
DR   RefSeq; XP_007851268.1; XM_007853077.1.
DR   AlphaFoldDB; V2WRF5; -.
DR   STRING; 1381753.V2WRF5; -.
DR   MEROPS; M16.002; -.
DR   KEGG; mrr:Moror_16162; -.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000017559; 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:UP000017559};
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..749
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          752..937
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   1133 AA;  127679 MW;  CBCC160945EAA8AD 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 GGTAGEEKVK EYLQGFQIDN SRVVLMGKEQ ELDKVKQFNN TIEKWQEEPW
     YRTKYRVVHF PEEFIKCSNS TSTTPELFLP QPNQFIPQNL NVDKKDITTP LCRPHLIYDT
     SLCQVWHKKD DHFWVPKAHV VIDICSPFAN STSQATLLTQ LFTDLITDSL TEFSYDASLA
     GLSYSCTSHS KGVYIALQGY NDKMHVLVRQ VLDKVKNLVV IPDRLDIMKE QTKKNLENFF
     LIQSHELADY YTFYLMSETA WTAEELLKEL PSITVEEVQK HGLYLLSQVH MNILVMGNVT
     QDQAVEIAEL AENIVGNLKD GLQPSDLNEY ALVLPPGSNF VYSTDVGNPD QTNNAITYYT
     HIGPVNDQHL HVVSSLLTQI MTEPTFNILR TKEQLGYIVS CGGILLPGST LKGIAIVIQS
     EKTPGYLESR VDAFLDYMKN MIEEMSEEAF TEQKAGLEKR WREDYKNLSE EANAYYWYID
     SGSWDFYRRE NDAEKLKDVT KDEVMKCFME YVHPSSQTRA KLSVHLHAKK SPPKKVSVAA
     AEAFGKLVQD ANLGLNGVVP DGALADDIPL VDNFQAYWDG VFKTVGKEDI TSSLLEAIPG
     LVEKYPLEGE GRDGPIEGAT YIEDPLAFRR SLKKSDYYPP VVIWQDNLID MGR
//