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Database: UniProt
Entry: A0A5B1QIP4_9AGAM
LinkDB: A0A5B1QIP4_9AGAM
Original site: A0A5B1QIP4_9AGAM 
ID   A0A5B1QIP4_9AGAM        Unreviewed;      1128 AA.
AC   A0A5B1QIP4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DENSPDRAFT_835009 {ECO:0000313|EMBL:KAA1469392.1};
OS   Dentipellis sp. KUC8613.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Dentipellis.
OX   NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1469392.1, ECO:0000313|Proteomes:UP000322482};
RN   [1] {ECO:0000313|EMBL:KAA1469392.1, ECO:0000313|Proteomes:UP000322482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1469392.1,
RC   ECO:0000313|Proteomes:UP000322482};
RX   PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA   Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA   Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA   Grigoriev I.V., Kim J.J., Choi I.G.;
RT   "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT   hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT   KUC8613.";
RL   Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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:KAA1469392.1}.
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DR   EMBL; NSJX01000006; KAA1469392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B1QIP4; -.
DR   InParanoid; A0A5B1QIP4; -.
DR   Proteomes; UP000322482; 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:UP000322482};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          53..187
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          269..442
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          455..749
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          753..935
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1128 AA;  127681 MW;  BC6AC582011BED6B CRC64;
     MTAGIPEDEA NWRPAKSLKG TNYFIFDKSI EKSQQDDREY RLIRLENGLQ AMIVHDATAD
     KAAASLDVAV GHLNDPDDMP GLAHFCEHLL FMGTEQFPKE NEYNEYLSKN NGSSNAYTAA
     SNTNYYFTVA TPALTGALAR FSGFFHSPLF APSCTNRELN AVDSENKKNL QSDVWRIFQL
     NKHLTKPGHP WSKFGTGNKE SLTKVGRDLK ARQTAANGVD KKARLSAATS IDNSLAPSPL
     SSRAVSPAPS VNSAVSEIEA DGGTVGRETR RRLIEWWTEN YCASRMRLCV IGKESLDDLS
     ETVIEFFSPV LNRGKDPLPM ITDHPFGPAE KGKLISVQTI MAFHAIEISF PLADQVPLYR
     YKPANLLSEF IGHEGPGSVH SYLKEKGWIT SLNAGPQSLG RGFAMFKVTI HLTKEGFRHY
     REAALAVFNY LSLLRSTEVP AWYSQEFSKI METRFRFTEK GRPEDYAVWV SEHMGRPVPR
     ELVLKASQVM SEWDPEGVAE KEMRRALEGL RIFEGRAVLM ARKDDHEEVA GRKEWDTEPW
     YQTAYRVEKF DDDFVQKAEG PNVIPQLHLP NPNNFVPQNL DVDKREVEKV EKRPHLIRQT
     PSSTLWHKKD DRFWIPRAHA LLDIRTPYAS STPEAAVLTR LFVNLVNDAL NEYAYAADLA
     GLNYNLTSFR LGIYVGVGGY NDKLHVLLKT VLERIKSLQV RSDRLEVSRE QMKRDWENFL
     LGQSYTISDY YSRYLMTDSQ WTIPELLDAL AVVTVQQVQD HATKLLSKIH TLMLVQGNLY
     KDEAVNIAKM SEEILGGAPM GPYDCTESAC FPKESTNLVW STPVPNPNEP NSALTYYLHL
     GSYNERPLRV ASSLLSQIIS EPAFNILRTK EQLGYIVGAS LWQSNGSHEI GLRIVVQSER
     GPVYLEERVE AFLNHMKGVL EAMSDAEFQE QKDGLEKKRR EEPKNLSEEV QRFWSQIDSG
     YLDFYRRSED ADYLKTVTKT DVIALFSKYL LPSSTERKKL SVHVKSQMPR TKHVSSAAMD
     AFAQHLKDAN VALEDVNWRE ELEGEPTVAD FKKYWTGVFT ERSIKDTDSL LSVVSGLVEK
     YPATKDAEGA LRSDVKQIED IKAFKASLRI TDPPKPLVEW NDLPVPKF
//
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