ID A0A1M3PH10_9PROT Unreviewed; 390 AA.
AC A0A1M3PH10;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:OJY65822.1};
GN ORFNames=BGP12_18475 {ECO:0000313|EMBL:OJY65822.1};
OS Rhodospirillales bacterium 70-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1895826 {ECO:0000313|EMBL:OJY65822.1, ECO:0000313|Proteomes:UP000184399};
RN [1] {ECO:0000313|EMBL:OJY65822.1, ECO:0000313|Proteomes:UP000184399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-18 {ECO:0000313|EMBL:OJY65822.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJY65822.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKWE01000051; OJY65822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3PH10; -.
DR STRING; 1895826.BGP12_18475; -.
DR Proteomes; UP000184399; 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}.
FT DOMAIN 186..277
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 390 AA; 41728 MW; D59D822C335B570D CRC64;
MPVINRIAAD AEQLTEWRRD LHMHPELGLE EHRTSQVVAD KLASWGIEVT RGLAGTGLVG
TLRNGASPRS IGIRADMDAL PMEEMNDFAH KSQNPGRMHA CGHDGHTTML LGAAKYLAET
RNFDGTVHFI FQPAEENAGG GRIMVEEGLF ERFPCDMVFG AHNDTSLPVG VMTAVEGSVS
AASDRFIITI AAKGGHAARP HQTIDPVVIG SHIVLALQSI VSRRTDPLHS AVVSITQFHA
GSAHNVIPDT AMLSGTVRTL RPEVQDEVQR LLPMIAETTA LAHGAQASVD YRRGYPPVVN
AAAPTERAAA AAARLLGADK VLRNRPPSMG GEDFSYMAQA VPGCFVRIGQ ADGARGSVAV
HHPKYDFNDD ILPIGASFWA GLVEQELAKG
//
