ID A0A072NA20_9DEIO Unreviewed; 369 AA.
AC A0A072NA20;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:KEF33833.1};
GN ORFNames=RDMS_10230 {ECO:0000313|EMBL:KEF33833.1};
OS Deinococcus sp. RL.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1489678 {ECO:0000313|EMBL:KEF33833.1, ECO:0000313|Proteomes:UP000027898};
RN [1] {ECO:0000313|EMBL:KEF33833.1, ECO:0000313|Proteomes:UP000027898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL {ECO:0000313|EMBL:KEF33833.1,
RC ECO:0000313|Proteomes:UP000027898};
RA Lal R., Mahato N.K., Tripathi C., Verma H., Kumari R., Singh N.;
RT "Draft genome sequence of Deinococcus sp. strain RL isolated from sediments
RT of hot springs located at Manikaran, India.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KEF33833.1}.
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DR EMBL; JMQF01000045; KEF33833.1; -; Genomic_DNA.
DR RefSeq; WP_034405797.1; NZ_JMQF01000045.1.
DR AlphaFoldDB; A0A072NA20; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000027898; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03885; M20_CPDG2; 1.
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; IPR017150; Pept_M20_glutamate_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:KEF33833.1};
KW Hydrolase {ECO:0000313|EMBL:KEF33833.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KEF33833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027898}.
FT DOMAIN 174..266
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 369 AA; 38400 MW; C6B18A1849B78365 CRC64;
MVSLPPAPDL AALLEDLRVL TELESPSTDP AAIARVMDVA EAWALELGGT VQHLSGGTRR
FAFGETGAAR PLLLLAHADT VWPHGTLRAM PWRVEGDRAY GPGTYDMKAG LVGAFHALRT
LAGGWPRGGV VLLLTPDEET GSASSREHIE AAARESRAAL VLEPPVADTH ALKVGRKGVG
DLHLHFRGVA SHAGNKPEEG ASAITEAAHA VLAVQALARP ELGTTVSVGR IAGGGAINVI
PAECSLDADV RVATLAEADR VMAALEGLEP RDPRVTLTVT GGLNRPPFER GPGTQVLFEQ
AQAAARELGF EVTGEVVGGG SDGNFTAPLC PTLDGLGAPG DGAHAAHEHV RLDRWPAHVQ
LLTRLMQGL
//
