ID   D9ZDR5_9ZZZZ            Unreviewed;       940 AA.
AC   D9ZDR5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Insulinase family protein {ECO:0008006|Google:ProtNLM};
OS   uncultured organism.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=155900 {ECO:0000313|EMBL:ADD61469.1};
RN   [1] {ECO:0000313|EMBL:ADD61469.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20841432; DOI=10.1101/gr.108332.110;
RA   Tasse L., Bercovici J., Pizzut-Serin S., Robe P., Tap J., Klopp C.,
RA   Cantarel B.L., Coutinho P.M., Henrissat B., Leclerc M., Dore J., Monsan P.,
RA   Remaud-Simeon M., Potocki-Veronese G.;
RT   "Functional metagenomics to mine the human gut microbiome for dietary fiber
RT   catabolic enzymes.";
RL   Genome Res. 20:1605-1612(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; GU942931; ADD61469.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9ZDR5; -.
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   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          56..190
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          210..395
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          692..870
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   940 AA;  107063 MW;  22B54E064AE64F26 CRC64;
     MMKHLLRNLW IAALIVCCNF QQVSAQQLPP IPIDQDVRIG KLDNGLTYYI RKNSLPANRA
     DFYIAQKVGS IQEEDNQRGL AHFLEHMCFN GTTHFPGKSL IQYLERIGVK FGENLNAYTS
     IDETVYNISN VPVNTPGAID SCLLILHDWS NDLILDPKEI DKERGVINEE WRTRMSAMQR
     FQEKMLPAMF AGTKYANCFP IGTMDVVMNF KPQTLRDYYE KWYRPDLQGI MVVGDVDVDA
     TEALIKKMFA DIPAQPNGAK REYYPVNDNK EPIILVARDK EQPYVQTFIF NKHETTPREE
     KSNVGYLMQD YAATLITNML NARLNELLQA ANPPYIYAAT YDDDFFVAKT KDAFTGIVVC
     KEDAIENGIS TVLREIERAR QFGFTETEYS RARAEYLRHL ESAFQERDKR KNESYVKEYV
     RHFLDNEPIP GIANEYTIIN QIAPAIPVTA LNQMMQQMVT DSNQVVALFG PEKEGLKLPT
     EEAIKNLLKA VKSEKLTPYV DKVSNEPLMK EAPKGGKIVS EKKDDIFGTT MLTLSNGVKV
     IIKKTDFKAD EIRMKGVSMG GSSLFPDSEI ININGLDAVA LGGLGNFSAI ELEKVLAGKK
     ASVNYGIGDK TEAVTGSCSP KDFETMMQLT YLTFTAPRRD DNAFASYKNR SKAELQNMDL
     NPSSSFSDSI TSTLYMKHPR TLRMKADMVD KMDYDKILSM YQDRFKDASD FTFILVGNVD
     VEAVKPLIES YLGSLPSINR KETFKDNHIE MRKGIYKNEF IRQQETPKVN NFISYSGTCA
     YTLRNDILMS MTDQLLNLIY TEKVREDEGG TYGVYPMGQL VKYPTERAVL QIFFNTAPDK
     QDKLMKIIYA EAETFAKNGP DEASLNKVKE YMLKKHNENL KENGYWLNSI DEYLYTGINP
     IKDYEQIVNE ITVKDVQKFA NELLKQKNQI TVSMISPEKK
//