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Database: UniProt
Entry: A0A1F6RYH8_9BACT
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Original site: A0A1F6RYH8_9BACT 
ID   A0A1F6RYH8_9BACT        Unreviewed;       525 AA.
AC   A0A1F6RYH8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=A3J76_01135 {ECO:0000313|EMBL:OGI25721.1};
OS   Candidatus Moranbacteria bacterium RBG_13_45_13.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1801635 {ECO:0000313|EMBL:OGI25721.1, ECO:0000313|Proteomes:UP000178026};
RN   [1] {ECO:0000313|EMBL:OGI25721.1, ECO:0000313|Proteomes:UP000178026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGI25721.1}.
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DR   EMBL; MFRT01000021; OGI25721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6RYH8; -.
DR   Proteomes; UP000178026; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR023100; D-aminoacylase_insert_dom_sf.
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.
PE   4: Predicted;
FT   DOMAIN          45..506
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   525 AA;  58586 MW;  01B8929B504DA37A CRC64;
     MYDILIKNGT VIDGTGKAGI PADVAISKNK IAKVGKIRWS KGRTEIDARG KIVCPGFIDV
     HNHSDAYWQL FLEPTLPSLV HQGITTIIGG NCGTSIAPLA EGRVIESIQK WTDLREVNVD
     WLSIEEFAEK LRARKMGLNF GTLVGHGTLR RGILHDEMRR LDRNELDEIE RILEIALFEG
     ALGFSTGLAY SHEKSATWDE LVELAEIAKS QDRIYSTHLR DEAGEVASAL QEAIDLSKQT
     GVSLQVSHLK VMGEKNWHLM DVVLSEIEKA HKAGVDINFD VYPYTQTGSV LYVYLPAWAA
     EGGKRMLVKR LKEKHLRKKI IEEMRETAGY HYENAVIAVC SFSKSLSNRK IAEIASERGV
     LAEEVIMDLL LASEGRVITI MECLGEENVK KAIKHPLSII ATDGAGYNVS RKESGELVHP
     RCFGTFAKVL GKYVREEKLM SFEEAIKKMT SLPAKKFGIE GRGRLEKGKF ADITVFDPKI
     VSDKATVENP YQYSDGIEQV ILNGKFLMRD MKLTGEMNGE FLMTN
//
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