ID D2RNI8_ACIFV Unreviewed; 384 AA.
AC D2RNI8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Peptidase dimerization domain protein {ECO:0000313|EMBL:ADB46614.1};
GN OrderedLocusNames=Acfer_0206 {ECO:0000313|EMBL:ADB46614.1};
OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS 106432 / VR4).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB46614.1, ECO:0000313|Proteomes:UP000001902};
RN [1] {ECO:0000313|EMBL:ADB46614.1, ECO:0000313|Proteomes:UP000001902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC {ECO:0000313|Proteomes:UP000001902};
RX PubMed=21304687; DOI=10.4056/sigs.1002553;
RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acidaminococcus fermentans type strain
RT (VR4).";
RL Stand. Genomic Sci. 3:1-14(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP001859; ADB46614.1; -; Genomic_DNA.
DR RefSeq; WP_012937604.1; NZ_CP085936.1.
DR AlphaFoldDB; D2RNI8; -.
DR STRING; 591001.Acfer_0206; -.
DR GeneID; 78333957; -.
DR KEGG; afn:Acfer_0206; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_1_9; -.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000001902; Chromosome.
DR GO; GO:0016787; F:hydrolase 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; IPR001261; ArgE/DapE_CS.
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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001902};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 185..286
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 384 AA; 42268 MW; 547004C92FCA407A CRC64;
MEQQQEKIRE AVESFRQDML DFWKDLINFQ AGSKEKDRME TLMEKVSAYL ERQGMESELV
ESGAAPLIRA WSGKERAGQP ILLSGHLDTV FPNGSYPADP FTIWEGKAYG PGVCDMKGGI
VMAVYLARVL EKIGYDRHPI KLLFVPDEEI THQGSRAAQL LAEEARGCLC AFNLETGRMD
NCLTVGRKGC MDVWITVHGK AGHVGNAYTR SANAIEEMAH KIIALRALTD LEKGRIVSTD
IISGGTVSNA VADTCRIEVD CRYDYNEDKE KLQEAIRAIC AETHVPGTRT EVEFPAFMPV
FERTEGNDRL LDLVNQEARA FGIPAFGAAH PGGCSDASFM AQAGIPILDS VGVQGDGAHT
LQEYAIVETM FERTMLLAAA ICRL
//
