ID A0A1F3A368_9PROT Unreviewed; 397 AA.
AC A0A1F3A368;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:OFW99243.1};
GN ORFNames=A3D94_08970 {ECO:0000313|EMBL:OFW99243.1};
OS Alphaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_66_14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1797225 {ECO:0000313|EMBL:OFW99243.1, ECO:0000313|Proteomes:UP000176194};
RN [1] {ECO:0000313|EMBL:OFW99243.1, ECO:0000313|Proteomes:UP000176194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFW99243.1}.
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DR EMBL; MEMN01000162; OFW99243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3A368; -.
DR STRING; 1797225.A3D94_08970; -.
DR Proteomes; UP000176194; 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..280
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 397 AA; 43437 MW; EE649DF0129545E6 CRC64;
MPVINRIASF HKDMTAWRHD IHSHPETAFE EVRTADVVAE KLKSFGLEVH RGLAKTGVVG
VLRSGTSRRA IGLRADMDAL DVHETNQFDH KSTIPGKMHA CGHDGHTVML LGAAKYLAET
KNFDGTVYFI FQPAEENEGG GRVMVEEGLF DKFPVEGVYG MHNIPGIPVG RFAVRPGPMM
AAYDIFEVII KGVGAHGAMP HHGIDPVVVG SHIVTALQSI VARNVDPMDT AVVSTTQIHA
GDTWNVIPQE CVLRGTVRTF KKPVQDMIEK QIEKIARNVA AGFGAEVTKW RYERRYPATV
NSVQETEFAA QAASALVGLE NVNRNPTPAM GSEDFAWMLL KKPGCYIWIG NGDGEGSCMV
HNPGYDFNDE ILPIGASYWS TLVEQQLARQ AVPQAAE
//
