ID A0A4Q7ZG03_9ACTN Unreviewed; 430 AA.
AC A0A4Q7ZG03;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:RZU49687.1};
GN ORFNames=EV385_1440 {ECO:0000313|EMBL:RZU49687.1};
OS Krasilnikovia cinnamomea.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Krasilnikovia.
OX NCBI_TaxID=349313 {ECO:0000313|EMBL:RZU49687.1, ECO:0000313|Proteomes:UP000292564};
RN [1] {ECO:0000313|EMBL:RZU49687.1, ECO:0000313|Proteomes:UP000292564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45162 {ECO:0000313|EMBL:RZU49687.1,
RC ECO:0000313|Proteomes:UP000292564};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (FEB-2019) 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:RZU49687.1}.
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DR EMBL; SHKY01000001; RZU49687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7ZG03; -.
DR Proteomes; UP000292564; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000292564}.
FT DOMAIN 19..166
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 173..351
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 430 AA; 46326 MW; C57AF87E1BE9D80B CRC64;
MTRTIQDGVR RTVLPSGLRV LTEHIPTAHS VSLGVWVGIG SRDEAPAMSG ASHFLEHLLF
KGTHKRTALD ISAQIEAVGG ETNAFTTKEY TCYYARVLDA DLPLAVDVLC DAVADSVLHP
ADVETERAVI LEEIAMHDDE PGDEVHDVFT EAIFGNHPLG RPISGTTDTI SPMTRATING
FYRRRYTPPR IVIAAAGNLD HAAVVRLVRK ALAGTALDTP AAAPALCRPA DHRVRTQRAH
TVVRNRDTEQ AHMVLGCPGI GRRDERRFAL GILNNVLGGG MSSRLFQEIR EKRGLAYSVY
SYGSQYADAG VFGVYAGCAP GKAEEVLDLI RAELATVAAN GITAEEVARG KGMVKGSYVL
GLEDTGSRMS RIAKSELLYG DLLTVSELLA RVDAVTLDEI NELAVELLSR PMSLAVVGPF
DESAFPDTAR
//