ID   M0B5F3_NATA1            Unreviewed;       417 AA.
AC   M0B5F3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:ELZ04889.1};
GN   ORFNames=C481_03882 {ECO:0000313|EMBL:ELZ04889.1};
OS   Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS   P-10747 / NBRC 102637 / 172P1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ04889.1, ECO:0000313|Proteomes:UP000011554};
RN   [1] {ECO:0000313|EMBL:ELZ04889.1, ECO:0000313|Proteomes:UP000011554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ04889.1,
RC   ECO:0000313|Proteomes:UP000011554};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:ELZ04889.1}.
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DR   EMBL; AOIO01000011; ELZ04889.1; -; Genomic_DNA.
DR   RefSeq; WP_006107631.1; NZ_AOIO01000011.1.
DR   AlphaFoldDB; M0B5F3; -.
DR   STRING; 29540.C481_03882; -.
DR   PATRIC; fig|29540.5.peg.782; -.
DR   eggNOG; arCOG01107; Archaea.
DR   OrthoDB; 133929at2157; -.
DR   Proteomes; UP000011554; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT   DOMAIN          222..311
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          49..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  44058 MW;  81A503FA2CF21C6F CRC64;
     MPPTESIVTL TRELVSIPSH EDETEAGEFI ESWLRRETDA DVRRDAVGNV FARTDESGGA
     DESETETETE IESGTGIASG SEPRTAETAE GETDDRNADT LALVGHHDVV APAEPQTDET
     GSYVVREQDA RLYGRGAADM KGALAAAMLA FRDNEMRRTS EAGTDTGDAD PGGELVFASF
     VGEEIGGTGA RHAIDEGFAP EFAVVGEGST NYSGSAVTDV AVAHKGRRGS TITTRGSAAH
     ASEVEAGENA IYRATDAIEQ IRDLEPPTVT VAGETLAGTV AVTEIEGGTA MNVIPARCEF
     TIDERTVPGE RAPLADIADR PGVEWTIEQD LPPMRCDDAA FIDAVQSAAD AAQSGAPELV
     TKPHATDAGW LSDAGTECVI YGPAEPGEAH TDDESVSIAA LERCYETYRR IAERWPQ
//