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Database: UniProt
Entry: A0A191TIA8_9BACT
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ID   A0A191TIA8_9BACT        Unreviewed;       382 AA.
AC   A0A191TIA8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN   ORFNames=A9P82_03475 {ECO:0000313|EMBL:ANI88445.1};
OS   Arachidicoccus sp. BS20.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Arachidicoccus.
OX   NCBI_TaxID=1850526 {ECO:0000313|EMBL:ANI88445.1, ECO:0000313|Proteomes:UP000078308};
RN   [1] {ECO:0000313|EMBL:ANI88445.1, ECO:0000313|Proteomes:UP000078308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS20 {ECO:0000313|EMBL:ANI88445.1,
RC   ECO:0000313|Proteomes:UP000078308};
RA   Im W.T., Siddiqi M.Z.;
RT   "Arachidicoccus sp. BS20 whole genome sequincing.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP015971; ANI88445.1; -; Genomic_DNA.
DR   RefSeq; WP_066204224.1; NZ_CP015971.1.
DR   AlphaFoldDB; A0A191TIA8; -.
DR   STRING; 1850526.A9P82_03475; -.
DR   KEGG; arb:A9P82_03475; -.
DR   OrthoDB; 9807210at2; -.
DR   Proteomes; UP000078308; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078308}.
FT   DOMAIN          195..327
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   382 AA;  44446 MW;  046F7C13E16503D5 CRC64;
     MLLHNLKISD KDIVHLLIKE KKIEKISFNQ AEHNINKEEI YFENCFVFPG LINSHDHLDY
     NLFPKLGNRV YKNYLEWGTD IHLQNKEMIQ EILRVPKALR AMWGVYKNLI SGVTTVVQHG
     EAFELKEVPI TVFGECVSLH SVRLDKRWKY RLNKPFGEKL PYVIHIGEGT DKERYHEIDE
     LFEWNFFCRE IVGVHGIAMN VRQAKKFKAL VWCPDSNFFL YNKTAAIDEL KHHTKILFGT
     DSCVSADWNI WHHLREARET KMLDDEALIN SVTSLPADIW KINAGAIKEN CGADLMIVKQ
     KNKNYAESFF ATNPEDIQLI LHKGNIVLFD ASLMLQLKYL SLKTFSVVYV NGEKKYVYGN
     VPSLIKNIKK YSPEIKFPVD VE
//
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