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Database: UniProt
Entry: S7RX58_GLOTA
LinkDB: S7RX58_GLOTA
Original site: S7RX58_GLOTA 
ID   S7RX58_GLOTA            Unreviewed;      1152 AA.
AC   S7RX58;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLOTRDRAFT_119876 {ECO:0000313|EMBL:EPQ57929.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ57929.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ57929.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ57929.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KB469298; EPQ57929.1; -; Genomic_DNA.
DR   RefSeq; XP_007863251.1; XM_007865060.1.
DR   AlphaFoldDB; S7RX58; -.
DR   STRING; 670483.S7RX58; -.
DR   MEROPS; M16.008; -.
DR   GeneID; 19300590; -.
DR   KEGG; gtr:GLOTRDRAFT_119876; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_2_1; -.
DR   OMA; WIFDEMK; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000030669; 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:UP000030669};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..183
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          270..444
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          456..760
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          765..948
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          208..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  129970 MW;  777E3F4B4EE1850A CRC64;
     MVDHANWRHV PASGTRPPYR VFTKPIDKSQ QDDREYRIIE LQNGLQATVI HDAKADKAAA
     SLDVAVGHLY DPDDMPGLAH FCEHLLFMGT EQFPRENEYS EYLSKNAGSS NAYTATSNTN
     YYFNVSTPAL AGALARFAAF FHCPLFAPSC TSRELNAVDS EHKKNHQSDM WRIFQLNKHL
     SKPGHVWRKF GSGNRESLSQ VAKELKQKGL LNGTNGKNTN SIKVNGNGSA SARSSLAPSP
     VPSRLPSPAP SEASANSELE ADGGAIGRET RRRLVEWWSK EYCAGRMRLC VIGKESLDEL
     CELVATLFSP IPNRGQESLP MINDHPFGSE EKGTLVAVQT IMDFHVLEIS FPLAYQPPFW
     RYKPANFLAH FVGHEGPGSL HSYLKNKGWI TSLSAGAQNL ARGFGMFKVT VHMTQDGFQN
     YRSIMLATYK YLNMLRSSEL PAWHSREIST IASIRFRFAE KRRPDDYAVW VAEHMAWPVP
     RELVISAPQL TWPWDEPGAQ KDANGSWIGE KEVREILNGL KVDNGRAVLM ARQAEHEKVA
     GNGVALDWQT EPWYGTGYRV VRLDEQFTRE AQSPNQLQEL FLPGPNEFIP TNLDVDKRDV
     AEPLEHPHLI RDTPLSTLWF KKDDRFWVPK ARVAIDVRSP LANPTPRSVV MTKLFGRLVT
     DSLTEYTYDA DLAGLSYDVI THGLGIWVIV SGYNDKVPVL TRRVFEAIKH LTIVPERLEV
     FKEQVKREWQ NFFLGQSYGM SDYFGRYLLT ERQWTLQEML PEIASVTADE VQSHAKQLLS
     EVNMRMLVTG NVHKEDAVHI AELAESILKS SPLPASSVIE RSLILPEASN HVWSIPVPNP
     NQTNSALTYY LHVGDLTDEQ LRVISSLLAQ ILSEPAFNVL RTQEQLGYIV SCSQWHLAGD
     SQKGLRIVIQ SERPPHYLES RVNAFLNNMR RAIEEMSEEE FAEQKQGLER KWTEKPKNLS
     EETNRFWMHI DSGYYDFLRR FRNAELLRSV TKQDVLDLFD SRIHPSAPKR AKLSVHLRSQ
     KPPPKKVSLA AMAAFEDLVR SAGMPVEKDA WKEEFDGSEG EPLLADFTKH WQGILASEST
     TAGLSEEITK NLLASIPKVV EQHPAQVSEE TSTDVLEGVT FIKDPKTFKS SLQPSPDPRP
     AGEWKDTTAA KL
//
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