ID A0A2T7UPH0_9RHOB Unreviewed; 384 AA.
AC A0A2T7UPH0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:PVE46529.1};
GN ORFNames=DDE23_15355 {ECO:0000313|EMBL:PVE46529.1};
OS Pararhodobacter aggregans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE46529.1, ECO:0000313|Proteomes:UP000244810};
RN [1] {ECO:0000313|EMBL:PVE46529.1, ECO:0000313|Proteomes:UP000244810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-19 {ECO:0000313|EMBL:PVE46529.1,
RC ECO:0000313|Proteomes:UP000244810};
RX PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA Foesel B.U., Drake H.L., Schramm A.;
RT "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT biofilter of a marine aquaculture.";
RL Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE46529.1}.
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DR EMBL; QDDR01000008; PVE46529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7UPH0; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000244810; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd05666; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PVE46529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244810}.
FT DOMAIN 179..277
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 384 AA; 41530 MW; 1103663F3EF18B82 CRC64;
MQTLPRIDAF AADLTALRHD FHAHPELGFE EHRTSARIAE LLESWGIAVT RGIGGTGLVG
VLEGRGPGRR IGLRADMDAL PMEELTNLPY ASKNAGVFHG CGHDGHITML LGAARYLAET
RDFDGTAVFI FQPAEEGLGG ARAMIADGLF ERFPCDELYG LHNSPYHPMG QVTLRPGLAQ
AGASFFDIRV QGQGAHGAYP HFAKDPVTIG AGLVKELQEI TARNADPLHP VVLSVTAFLA
GEAYNVIPDH ADLRGTFRFL RPEDRDLIDT RMRQICAGMA LAHNVTIEVD IRGVFSPLRN
DPQSVDHLVE AARDVVGDRA AADAEVIMGS EDMADLLAMV PGAFFNLGHG SGVPVHNPHF
TFDDRILPVG ASIFARLVER RGTR
//
