ID A0A0H3C7L1_CAUVN Unreviewed; 544 AA.
AC A0A0H3C7L1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Metal-dependent hydrolase {ECO:0000313|EMBL:ACL94160.1};
GN OrderedLocusNames=CCNA_00695 {ECO:0000313|EMBL:ACL94160.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94160.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL94160.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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DR EMBL; CP001340; ACL94160.1; -; Genomic_DNA.
DR RefSeq; WP_010918544.1; NC_011916.1.
DR RefSeq; YP_002516068.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C7L1; -.
DR SMR; A0A0H3C7L1; -.
DR GeneID; 7330503; -.
DR KEGG; ccs:CCNA_00695; -.
DR PATRIC; fig|565050.3.peg.686; -.
DR HOGENOM; CLU_009942_1_0_5; -.
DR OrthoDB; 9811399at2; -.
DR PhylomeDB; A0A0H3C7L1; -.
DR Proteomes; UP000001364; Chromosome.
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:ACL94160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..544
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002605781"
FT DOMAIN 69..542
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 544 AA; 57633 MW; 04C9F2F7F04EED43 CRC64;
MRRLVLAALL AATSLTTAKA GDLLIHGGPI HTGVEAAPTA EAVLIRDDKI LFVGPLAAAK
AKAAKDVRAI DLKGAAAYPG FVDAHAHLTG IGLRELTLNL DQVKSVAELV AAVKAYAAAH
PEGPISGRGW IETHWPEKRF PTKADLDAAA PGRIVVLGRS DGHASVASSA ALAKAGITAA
TVPPPGGDIL KGPDGQPDGM LIDHAQALVR NVIPPPNQAL KREALRKAGQ LYAARGWTGM
ANMSVMAEDL SLLRDEAAKG NFHIRIDNYM DPSGAEEVLT KGPQTDATGL IRVQGIKLYM
DGALGSRGAA LLEPYSDADT LGLQLTQPEQ GLALMKRAKA AGAQVAMHAI GDRGNRLVLD
WFEQSLGAEA KAARWRNEHS QIVADTDVPR FAKLGVIASM QPSHAIGDLF FAPARLGKAR
LHEGYRWADF LKADVVVAAG SDAPVEVGDP RIEFYAAVYR HSLDGFANAD WHLDQAVSRA
EALKMLTLAP AYAVFREKEL GTLEAGKKAD VTAFDRDLMT VEPKAILTAQ PVLTVVDGKV
VYSR
//
