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Database: UniProt
Entry: A0A0Q4G2U3_9SPHN
LinkDB: A0A0Q4G2U3_9SPHN
Original site: A0A0Q4G2U3_9SPHN 
ID   A0A0Q4G2U3_9SPHN        Unreviewed;       545 AA.
AC   A0A0Q4G2U3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Metal-dependent hydrolase {ECO:0000313|EMBL:KQM68077.1};
GN   ORFNames=ASE75_00625 {ECO:0000313|EMBL:KQM68077.1};
OS   Sphingomonas sp. Leaf17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM68077.1, ECO:0000313|Proteomes:UP000051777};
RN   [1] {ECO:0000313|EMBL:KQM68077.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM68077.1,
RC   ECO:0000313|Proteomes:UP000051777};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM68077.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM68077.1,
RC   ECO:0000313|Proteomes:UP000051777};
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:KQM68077.1}.
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DR   EMBL; LMKL01000001; KQM68077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4G2U3; -.
DR   STRING; 1735683.ASE75_00625; -.
DR   OrthoDB; 9811399at2; -.
DR   Proteomes; UP000051777; 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:KQM68077.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051777};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..545
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006218295"
FT   DOMAIN          68..539
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   545 AA;  58447 MW;  2F727D1FD5A4FD40 CRC64;
     MTASLVALSL LATPAFADAL VDNVTGITLD KDGKVVRFTG LLMSLDGKVT RLLSAKDKRP
     DKLDWRADMK GRVLIPGFVD AHGHIMDLGF RALELDLSAA KSLDEALARI AAYAAANPDK
     KWIMGGGWNQ EAWGLGRFPT AAELDRAVPD RPVWLQRADG HAAWANSEAM RIAGVTAKSV
     APAGGRIEKA GAQPSGVFVD SAMNLVQAAV PKPLAKDRNA AFLKAQLMLL EDGITATADM
     GTTLDDWMTY RRIGDLGNLR VRIMSYGAGV DTTVTIGGTG PTPWLYGDKL KLVGVKLYSD
     GALGSRGAWL KAPYSDAPGQ SGAGFMSDDV IRNLMSRASM DKYQVAVHAI GDKANAQALD
     AIDEMSGTYK GDRRWRIEHA QIVDPADLPR FSKHGTIASM QPTHATSDRT MAEARLGPVR
     LTGAYAWATM LKNGVPLAFG SDYPVEDPNP FAGWAAAFTR MDAAGQPFGG WRPEEAVTRE
     QAWAAFTTGG AYAGFAENQF GRLAPGQLAD FIIVDRDPTL ASPSDLRATK VEETWIGGQK
     AWVRK
//
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