ID A0A1F4ZT43_9BACT Unreviewed; 842 AA.
AC A0A1F4ZT43;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN ORFNames=A2Y86_01630 {ECO:0000313|EMBL:OGD09562.1};
OS Candidatus Aminicenantes bacterium RBG_13_62_12.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797269 {ECO:0000313|EMBL:OGD09562.1, ECO:0000313|Proteomes:UP000178836};
RN [1] {ECO:0000313|EMBL:OGD09562.1, ECO:0000313|Proteomes:UP000178836}
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:OGD09562.1}.
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DR EMBL; MEXX01000082; OGD09562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4ZT43; -.
DR STRING; 1797269.A2Y86_01630; -.
DR Proteomes; UP000178836; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..842
FT /note="Amidohydrolase-related domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009516051"
FT DOMAIN 321..412
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 754..829
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 842 AA; 90391 MW; 7B84D665CB7BEAC3 CRC64;
MSKKTVLLFA LLVLGTLLAV SAQAAEGNSC LIKAKKIYTV SQGIIENGMI LVEKGKIIQV
GKNMPVPKGV PVLEAEVVIP GLIDAHTHVG VYSLPNVDEN SDGNEMTNPI TPQVRALDSF
NFDDPAIQAG LAGGVTTVIS RPGSGNVIGG TSVAVKLKNA PPQEMVLKEV CDLKMAIEGN
PVGVYGTKNQ MPGTLMAVYY LARKAFIEAQ EYIKNWETYE KDKKDGKDVT PPKRDLGKEA
LALALKREIP VHIHCATASE IVTCIRLADE FNLRLSLGHC YWAYLIVDEL AKRKDVHYNV
GPPMFFNYFE DPLSFKNNPA ILSEAGLKVS LQTDALGGAQ QNLRHLALLC VRYGMKEDEA
LKSVTLHGAE AVGLEARIGS IAPGKDADLV FLDGEPFDLL TSVRKVLVDG RVEYKNEAGQ
RPALGESVPS ARAALTLPPG LEAGSSLAIK AGRIFPISGP AFSDGVILIE NGKIKSIGKG
AAIPAGVPVV DAREFTVMPG LISARSYVGI TSNWRMQSSI DEPSKPVVPE LEVKHAVEPQ
APLFTFAREL GITSVMVTPG NRNVMGGQGA VLKTEGAVVD KMIIKDRAVM VFGVGASARR
QNQMPSTRMG IAALLRETLV KAQEYGETIE KYEKDKKGKE PQRDLSLEAL LPVLRGEMPV
LIHCERKDDI LTALRLADEF KLKVALDGAT DAYKVVDELK KRGVAVILED IFRGAGNIED
RGFNPQNAAI LARAGITIAF RPGEGSWYVP AAGEAGGDLL ETAAFAFRNG LSEEEALKAV
TINAARITGL ESRIGSLEPG KDADILILRG HPFATGSVPE AVFVDGKPVF LKKEGAHRGK
SR
//
