ID A0A4P9XDI0_9FUNG Unreviewed; 934 AA.
AC A0A4P9XDI0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=CXG81DRAFT_9446 {ECO:0000313|EMBL:RKP03512.1};
OS Caulochytrium protostelioides.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Caulochytriales;
OC Caulochytriaceae; Caulochytrium.
OX NCBI_TaxID=1555241 {ECO:0000313|EMBL:RKP03512.1, ECO:0000313|Proteomes:UP000274922};
RN [1] {ECO:0000313|Proteomes:UP000274922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52028 {ECO:0000313|Proteomes:UP000274922};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; ML014122; RKP03512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9XDI0; -.
DR STRING; 1555241.A0A4P9XDI0; -.
DR Proteomes; UP000274922; 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:UP000274922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 224..402
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 409..703
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 721..893
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 934
FT /evidence="ECO:0000313|EMBL:RKP03512.1"
SQ SEQUENCE 934 AA; 104566 MW; 4D3B887BBC87D03C CRC64;
MVARSADASA APGAAITPTP AATRRRAPIP PSTTLSGLEK PTLDQREYRR VVLPNGLEAM
LISDVHADRA GAALDVNIGY FQDPEDYPGL AHFLEHLLFL GTAKFPKENE YSAYLQDHSG
WSNAYTDSEN TNYHFEVDAP AFEGAIDRFA QFFIAPLFDP SCTDRELKAV DSEHKKNLQA
DAWRLQQVDA ELAAPEHPYH KFGTGSSETL KDRVSEDGQT VIPTRDRVMA FYKEYYSANL
MRVALVGPQS LDTLESWLTT YFSPIPNQNL ALPSYVGQPF DARHVGRVVY AVPIRDEPYL
SLTWQFDDQR PHYGKAGLQY LGDLLGQETK GSLLSLLKAK SYAHELFAGA DDSGRGFAFF
NIQIGLTRRG AHHWVAVLAH AFQWIRMIQS HGVLRWYWDE CRDLADMSFR FSEAGAPGDY
AVTVSNHMHL YAPNHVLSGS TLFREYDADH LGALLQHLTF DQCRVLLVSQ SLCDEAPPPP
PPGWKILPWG YACQYQAQPC PPELRASIAM LKAHPDLHLP PPNPFIPNVP DEQGVPNPKL
PQPTRPALVK ETPLYRLWHL TDQQFAVPKS VIHLYVRNPR VYGSVHMAAA HLMWIAALRD
ALNETTYQAS LASVEVHIDA SLEGTVIVLS GYTEILPTVF ARIWAAMWAK PFTAPSHRWD
AVKRHLIRNL RNTRYKSAQS FAVYSCLLAI QSALYMWNDK AAALEGITQS DVERLVHTSR
EQLSMEVLIT GNMTAAASEA LIADALAQIR GPDTARPAPL PTSIRYALSR NHLIPTQRDW
IYPLVLPNED DVNSAIEWYV QLSPGLTAKD RLAVQLFDQI TNEACFDVLR TQQQLGYLVH
SGVRRHVGLI GFYVLIQSDR APTDLHDRIE AFIAGTPARI RALSPQAFRK HRESLAATLT
TRERNLAEEH ARVWSAIYMG TWNFSVSHDD AAAL
//