ID A0A3M8GIC9_9FLAO Unreviewed; 552 AA.
AC A0A3M8GIC9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:RNC90027.1};
GN ORFNames=ED555_11360 {ECO:0000313|EMBL:RNC90027.1};
OS Allomuricauda sp.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=192149 {ECO:0000313|EMBL:RNC90027.1, ECO:0000313|Proteomes:UP000280438};
RN [1] {ECO:0000313|EMBL:RNC90027.1, ECO:0000313|Proteomes:UP000280438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin2 {ECO:0000313|EMBL:RNC90027.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-2018) 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:RNC90027.1}.
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DR EMBL; RHLF01000002; RNC90027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8GIC9; -.
DR Proteomes; UP000280438; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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 PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000280438};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..552
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018096032"
FT DOMAIN 437..526
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 531..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 60456 MW; F0BFB5C331AB2E7E CRC64;
MRLLCLSFVC SILLFSCQRQ PGTTYDVVIK NGMVYDGNGD NPMLGDVGIS ADTIAAIGEP
NTLKGAEEID ATGLSVSPGF INMLSWANVA LLEDGRSQSD IRQGVTLEIM GEGRSMGPLN
DAMKESMAKN QGDIKYDVAW TTLGEYLQYL EDKGVSTNVA SFVGNGTLRS HVIGFDNRPA
TDDEMEAMKA LTQQAMEEGA VGISSSLLYA PSMYADTQEL IELSKVAAAH DGLYISHIRN
EGDYLLESLD ELIQISKEAD IRAEVYHLKA SSQHNWGKMD LAIAKIDSAR QAGLPITADI
YTYNASSTGL HVQLPDWVRE NGIAAMLRRL SNPANRQKAI DELEFRNQPE TILLVGFRSE
EMRKYGGKYL HEVAEEWGKS PEETLVDLII KDGSRIQVVY FSMSEENIKK KVAIPWVSFC
SDSGSLTNEG VFIKQNTHPR AYGSFIRVLG KFARDEGVIS LQEGIRKLTS LPADNLKLKK
RGRLAVGHFA DVVVFDAESV TDKATFTEPH QYAEGVVHVF VNGGQVLKDG AHTGATPGRF
VKGPGYKPQS AQ
//