ID A0A0A7KJP8_9DEIO Unreviewed; 405 AA.
AC A0A0A7KJP8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AIZ46320.1};
GN ORFNames=QR90_00580 {ECO:0000313|EMBL:AIZ46320.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ46320.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP010028; AIZ46320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7KJP8; -.
DR STRING; 1182571.QR90_00580; -.
DR KEGG; dsw:QR90_00580; -.
DR HOGENOM; CLU_009902_3_3_0; -.
DR Proteomes; UP000030634; Chromosome.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000030634}.
FT DOMAIN 11..155
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 162..335
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 405 AA; 43214 MW; FDDDC7579B1D78C0 CRC64;
MHVLPNGLTL LLEADPDAQT VAAGYFVNTG ARDEVPSEMG ASHFLEHLMF KGSERLSAAV
LNERLDDLGG QSNAFTGEEA TVYHAACLPE QTAELLDTLT ELMRPALRES DLEAERGVIL
EEIAMYADQP GVRVIDELRA DYWGTHPLGH LVLGTAQTVG ALSRDALAHD HARRYGAGRV
TLALTGAFEP AEVLEWATAN LADWPAAAPP AAELPPIPVH PGRVQVIADP ELSRVQVAAA
APGLPVTHPL REAAGVLADL IGGENGALYW ALLDTGLADS ADLAHLEYRD AGAFEGGFSC
DPERAQDVLS IFRAVLRDAA ALITEAAVRR AARKLAVSTL LRAETPQGRL FALGMDYLAT
GRAETTAELV NRYASVGVED VREVLRLCPL DRLTVVALGP LRALE
//