ID E1QEF8_DESB2 Unreviewed; 374 AA.
AC E1QEF8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:ADK83944.1};
GN OrderedLocusNames=Deba_0572 {ECO:0000313|EMBL:ADK83944.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83944.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83944.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP002085; ADK83944.1; -; Genomic_DNA.
DR RefSeq; WP_013257399.1; NC_014365.1.
DR AlphaFoldDB; E1QEF8; -.
DR STRING; 644282.Deba_0572; -.
DR KEGG; dbr:Deba_0572; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_2_7; -.
DR OrthoDB; 5486471at2; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08659; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
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 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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 175..276
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 374 AA; 38873 MW; 74DD46E212407BA8 CRC64;
MAAPIPTPLT IAQELVRRPS REEQGEQACA DYLRGLLEAA GFAVRAIDLA PGRPNLIATL
PQAKPGPALA FSGHLDTVAL GQAPWSFEPC GGLVDGGRLL GRGASDMKAG VAAMVHAALR
LAQGPAPRPN VALIFSAGEE HGLKGALHLA KTPGALPPVG AMLIGEPTAN QPLLGHKGGL
WLGVEFTGKS AHASMPHLGD NAIDKAAAAI VALGGHRFAQ SHAVLGRPTL NVGLIRGGAA
ANIVADHCRL DLDTRLLPGM DPEAVIAELR RVMGPQARVV SRNYLPPTWT EPDHPWVAAA
LKLIAAQTGD RRPPGGAPYV TDASALGPAL GCPTLIIGPG EPGQAHQTDE WCQCERIDQA
AEIYHQLALA WPMD
//
