ID   A0A1Q4E6J1_9PSEU        Unreviewed;       445 AA.
AC   A0A1Q4E6J1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OJY52283.1};
GN   ORFNames=BGP03_17690 {ECO:0000313|EMBL:OJY52283.1};
OS   Pseudonocardia sp. 73-21.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY52283.1, ECO:0000313|Proteomes:UP000186163};
RN   [1] {ECO:0000313|EMBL:OJY52283.1, ECO:0000313|Proteomes:UP000186163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-21 {ECO:0000313|EMBL:OJY52283.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OJY52283.1}.
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DR   EMBL; MKVV01000018; OJY52283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4E6J1; -.
DR   STRING; 1895809.BGP03_17690; -.
DR   Proteomes; UP000186163; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          30..176
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          184..364
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  46916 MW;  9C45985A099E980C CRC64;
     MTSLITPPGA GASAPAPGGV SRTSLPGGLR VVTETVPGVR SVSLGIWIAI GSRDEAPEQA
     GAAHYLEHLL FKGTSRRTAA SIAEDLDAVG GDLNAFTAKE HTCYYSHVLD EDLPLAMSVL
     ADVVTDATLN DADVEVERGV VLEEIAIRDD DPEDLLGELF DETLFGAHPL GRPVVGSEES
     IKGMTRATLH DFWRGGYTTP RMVVAAAGNL DHAHVVELVA ATLGPAMARA GDVAPVAPRR
     PEPAVLEPGP RLVLMDEDCE QAHLMLGVTG LSRHDPRRSA LSVLNTALGG GPSSRLFQQV
     REQRGLAYSV YSSTIGYSDT GSFAVYAGCA PERLDEVTSV IRGVLADVAD GGLTPAEVVR
     AQGNLRGGLV LGLEDTPSRM NRIGRSELDH GRQRTVAESL DRIAAVTPEQ VTDLARDLLA
     QPLTAAVVGP YEQEKDLPAS LRALA
//