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Database: UniProt
Entry: A0A0Q7SPQ5_9CAUL
LinkDB: A0A0Q7SPQ5_9CAUL
Original site: A0A0Q7SPQ5_9CAUL 
ID   A0A0Q7SPQ5_9CAUL        Unreviewed;       552 AA.
AC   A0A0Q7SPQ5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQY85882.1};
GN   ORFNames=ASD25_23340 {ECO:0000313|EMBL:KQY85882.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY85882.1, 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:KQY85882.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY85882.1,
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:KQY85882.1}.
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DR   EMBL; LMFL01000020; KQY85882.1; -; Genomic_DNA.
DR   RefSeq; WP_056617387.1; NZ_LMFL01000020.1.
DR   AlphaFoldDB; A0A0Q7SPQ5; -.
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; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KQY85882.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..552
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006323013"
FT   DOMAIN          68..549
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   552 AA;  58313 MW;  12BB3BEA8B84D9A4 CRC64;
     MIRTLALTLL LAGAAASAEA QDMLIKGGPI YTGVDAAPTA EAVLVRDGRI AWVGKLADQP
     AVPTEIPTID LKGAALFPGF TDGHAHLDGI GWRELTLNLE GSVSLADAMA RLTAWAAAHP
     EGPIAGRGWI ETRWPEARFL TAADLDAAAP GRVVLLGRAD GHAVVASTPA LAAAGIDAST
     VAPAGGEILK GPDGKPTGLL VDAADQLVTS LTPQADPAAL REAYRAGFRV EASYGWTGVH
     FMSAPWEDIP LLEDMAADGE APLRIYNSIT PEGAAELIAG GPRSVADGRI ITRAIKYYAD
     GALGSRGAAL FEPYADRPDT TGLMQITEQE IVPLYQAALK GGIQIATHAI GDRGNASVAE
     WYQQALAGVA PSERPNGADV RWRIEHAQIL RPTDYHWFRD LPIIASMQPS HAIGDLYFAP
     ARLGDARLDG AYAWRSLVDL GVIVVGGSDA PVERGAPLIE FYAAVARADL EGHQGPDWRP
     NEAVDRATAL KMFTLWPAWA SFREAELGTI EVGKRADLTA FNVDLMTAPV ADIPKGHATL
     TVVDGVVVYR KD
//
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