ID A0A165KEC7_EXIGL Unreviewed; 1119 AA.
AC A0A165KEC7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_747787 {ECO:0000313|EMBL:KZV96205.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV96205.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV96205.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV96205.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; KV425946; KZV96205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KEC7; -.
DR STRING; 1314781.A0A165KEC7; -.
DR InParanoid; A0A165KEC7; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000077266; 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; 5.
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:UP000077266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 62..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 269..437
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 456..746
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 750..931
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 220..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 126327 MW; 36030EEFF5892C4B CRC64;
MLALRLGQRT RAPSLLRSFA MSQAWRPVSS PEHDVYATPI QRSPNDDRDY RIIRLKNGLH
AMLIHDPNVD KAAASLAVTV GHLSDPDDMP GLAHFCEHLL FMGTEQFPRE NEYGEYISSH
GGHTNAYTSS SDTNYFFSVG SDALPGALER FSGFFHSPLL DASCTTRELS AVDSEHKKNL
QSDSWRLFQM SKSLSKPGHV WAKFGSGNMV SLTQAARAVA SLDRERSTGT PGRGDSLAPT
PAASRMPSPA PSLAPSENEP DGGAVGRETR RRLVEWWKSH YCASRMNLVI LGKEPLDELT
RLAIENFSPV PNRSLPTVKD VPELPWGEDH VGKFIHAKTI MDFQAVELQF QLPSQYYHWR
SKPSHFIAHL IGHEGPGSLH SYLKQKGLLV RLSCGNQPQA RGIDFFKITA FLTPEGFKRY
REVVLTMCKY LNLLRDTSSF PIHLFNELKV LAETRFNFAE KRTSDSYVSA LSEQMQRPFP
PENVLSGNTL LWDWDEPLVR RILAELLPEK GRVIVMAKDY APLGLEDPSV KWDQEKWYKT
TYNLQDMDDA FLMESRKPND LKELYLPPKN DYMPTNLAVD KCPVDKPLKR AEVVRKTPLS
ILWHKKDDQF WVPKANVFLF IRSPMAAPTP RHIVKTRLFC ELVTDALTEV AYAAELASLR
YDFSPDVYGV QVSLSGYNDK LPVLLETVLR KIKTIEINPG RFADMKEDLR QEWANFRMSQ
PVELADYYAR FTLSELTWPP DERLAELETV TLEEVHRHAQ ELLSRVKIEA FVHGNITQTE
AVALMETSES ILGARPLAPS EQLSNRSHVL PPNAKFVYQM DVPNVEDVNS GLSYYLHVGD
ITDKQLRAKL NLLAHIIHEP VFDQLRTKQQ LGYIVQSAMI IRTGIMGLRI HIQSERSPAY
LEQRVDAFLE GYKDMLSSMS EQDFEKQKNG LIMKKLEKCK NLAEEASRLW SAIDSGYHDF
LRREIDVETL RTLSKEDMID FVSTYFLPSS PERRKLSIHL KGRPKVDARF SVAASQAFLP
ILKEHGVPVT EADYTASSAA EPPVDAVKEF WKNTLEGMPN VSAESARVLI ENIERLALAH
PVQVVAATDA LPEGTVLIPD LAQFKLTLPL SAAATPVSS
//
