ID L7F6Q8_9ACTN Unreviewed; 543 AA.
AC L7F6Q8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:ELP66804.1};
GN ORFNames=STRTUCAR8_09503 {ECO:0000313|EMBL:ELP66804.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP66804.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP66804.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP66804.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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:ELP66804.1}.
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DR EMBL; AEJB01000327; ELP66804.1; -; Genomic_DNA.
DR RefSeq; WP_006378071.1; NZ_AEJB01000327.1.
DR AlphaFoldDB; L7F6Q8; -.
DR STRING; 85558.T45_03820; -.
DR PATRIC; fig|698760.3.peg.4442; -.
DR Proteomes; UP000010931; 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:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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:ELP66804.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931}.
FT DOMAIN 45..537
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 57428 MW; AA77909C8EBD48FE CRC64;
MHADLLFTGG PVFAPGSPTA VAVTGGRITA VGRDEVHDLI GSGTEVVDLA GRLLLPGFQD
AHVHPLPAGL ELTQCDLTDL KTAEDTLAAV RAYAVAHPGR EWITGGGWSM EAFEGGTPTR
ELLDAVVPDR PVYLPNRDHH GAWVNSRALE LAGVTRDTPD PADGRFERDA SGEPTGMLQE
GAMEYVGRLT PPVTAAERLA ALLSAQRRLH SLGVTAWQDA LVGSFLGMED PSETYLAAVR
DGSLTARVVG ALWWDRERGA EQIPELVERR AALSQGRFRA GSVKLMLDGV AETGTAALLD
PYLDKCGCAT ANRGTSFVDA AELPKYVTQL DALGFQCHFH ALGDRAVRDA LDAVEAARAA
NGPSDTRPHL AHLQVVHPDD VPRFARLGAV ANIQALWAMH EPQMDDLTIP FLGPERAAWQ
YPFGALLRSG ATLAAGSDWP VSSPDPLQAI HVAVNRAAPG CPSSRVFLPA ERIGLTAALT
AYTAGSAYAN HLDDSGSLRV GALADLTILD RDPYAGPPEA IAETKVALTY VGGERVYAAE
GAA
//
