ID A0A1F8QCQ5_9CHLR Unreviewed; 389 AA.
AC A0A1F8QCQ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=A2Z29_00850 {ECO:0000313|EMBL:OGO33223.1};
OS Chloroflexi bacterium RBG_16_56_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797649 {ECO:0000313|EMBL:OGO33223.1, ECO:0000313|Proteomes:UP000177333};
RN [1] {ECO:0000313|EMBL:OGO33223.1, ECO:0000313|Proteomes:UP000177333}
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 -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
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:OGO33223.1}.
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DR EMBL; MGNQ01000003; OGO33223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8QCQ5; -.
DR STRING; 1797649.A2Z29_00850; -.
DR Proteomes; UP000177333; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd05672; M20_ACY1L2-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 InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
FT DOMAIN 170..255
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 389 AA; 41701 MW; E60F758296807939 CRC64;
MDTGALKKDV RAEIDKRRRE LGDISRKLHQ HPEVAFQENQ ASSWLAEYLE ENSFAVERGL
CRLPTAFSAR YGRGRPVIAF LAEYDALPKV GHACGHNLIA TASLAAAVAS RLAVDKLGGG
VMVFGTPGEE LYGGKAIMAA RGAFTDVDMA MICHPGGGNR AVLNTLACLT LEVEFHGVAA
HASARPEAGV NALEAMILSF NSINSLRQHI RDHARIHGII TDGGEAANIV PAHSAGTFMV
RADDDRYLDK LKDRVIGCFT GAAMATGAKL EYKWGEKYTA MVNNMTMARL FRNNMRSLGH
RMPLGDSSRW GGSSDVGNVS QLVPAIQPLV SIASASVLIH TPQFAVAAAS GDALARMLDA
ARAMAMTAVD LLASPETVEK VQAEFFRNK
//
