ID A0A0Q7RHT7_9CAUL Unreviewed; 531 AA.
AC A0A0Q7RHT7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQY72587.1};
GN ORFNames=ASD25_27680 {ECO:0000313|EMBL:KQY72587.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY72587.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY72587.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY72587.1,
RC ECO:0000313|Proteomes:UP000051815};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQY72587.1}.
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DR EMBL; LMFL01000052; KQY72587.1; -; Genomic_DNA.
DR RefSeq; WP_056621461.1; NZ_LMFL01000052.1.
DR Proteomes; UP000051815; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KQY72587.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..531
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006321441"
FT DOMAIN 402..462
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 30..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 55878 MW; 831D96A5EE38A7B9 CRC64;
MRLHALRGSS LAVLACVLAG SLALSACATT GGDDASDANG SSDEEAREPL ARGLDHAANP
DPFPSTYRGL PRENMAIVGG TVFDGAGRKI ENGVVIVTDG KVAAVGDAST PVPGGHRVVD
ARGRFVTPGI IDVHSHLGVY PSPGVQGMSD GNEATNPNTA QVWAEHSLWP QDPGFNAARA
GGVTTLQILP GSANLFGGRG VTVRNVPSVT MQGMKMPGAP YGLKMACGEN PSRVYGGRNT
SPATGMGNVA GYRAAFIAAR EYKAKWDKWR DDGEGSPPTR NLQLETLAGV LDGSVLVQNH
CYRADEMAVM IDIAKEFGYR ITAFHHAIEA YKVAPLLARE GICADMWTGW WGFKMEALDA
VEANAALVDA PQGSCAVIHS DDAELTQRLN QEAAAGLAAG RRMGMNISEE RAISWITLNP
ARSLGIADQT GSLEAGKRAD VVIWSANPFS VYARADQVFI DGGLSFDRMN PADRIAGGAN
PFSVYARADQ VFIDGGLSFD RMNPAYQPLS DYELGQPGXG LSAANVPQGA R
//
