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Database: UniProt
Entry: A0A0D8CS97_9GAMM
LinkDB: A0A0D8CS97_9GAMM
Original site: A0A0D8CS97_9GAMM 
ID   A0A0D8CS97_9GAMM        Unreviewed;       536 AA.
AC   A0A0D8CS97;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KJE39029.1};
GN   ORFNames=SG35_23410 {ECO:0000313|EMBL:KJE39029.1};
OS   Thalassomonas actiniarum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassomonas.
OX   NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE39029.1};
RN   [1] {ECO:0000313|EMBL:KJE39029.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5K-106 {ECO:0000313|EMBL:KJE39029.1};
RA   Olonade I., van Zyl L.J., Tuffin M.I.;
RT   "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT   actiniarum.";
RL   Submitted (JAN-2015) 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:KJE39029.1}.
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DR   EMBL; JYNI01000053; KJE39029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8CS97; -.
DR   STRING; 485447.SG35_23410; -.
DR   PATRIC; fig|485447.4.peg.5148; -.
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; 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; 2.
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:KJE39029.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..536
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002328030"
FT   DOMAIN          90..293
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          377..520
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   536 AA;  57744 MW;  EF461877DD4AF2C9 CRC64;
     MMNNMNLTSL AVISLAVLLT GCSFSYKAAD NRGNEQANLS SPVASADILI TGGRVYTGIG
     THEQMLDIAV CGEKICGLYP SGSEKIAAAE VINARGKIVS PGFIDPHTHT LEELSSRDKN
     HNLNYLTQGV TTVVNGNDGA GPVDIAKTAK SLEANGIGTN VALLVGHGSV REQVMGRAPR
     FATDQELEQM SALLNQAMQA GALGLSTGLY YVPGSFANTE EVVTLAKIAS QYNGIYDTHL
     RDESTFNIGF SAALDEAIFI AKSADIHLHL AHIKALGVDV WGQSTDAIKK IEQAQASGLS
     ISADQYPWLA SGTLLHSAVM PKWAMADSKQ AFFKRLNNPE LSEKLRREIK ENIRRRGGPG
     ALLITAFKDN ALVGLTLEEV ASMRAVDAVT AAIALVQQGD VRVASFNMSP QDVENFMVQP
     WVVTSSDGTN GHPRKYASFP KKYQEYVVKK GLLTLGEFIK KSSGQTAKIL GLQNRGILAQ
     GYQADIIVFD EQNLAANADF SRWNKYSSGV EYVLVNGQLV IKQGQYTDKL AGKFVR
//
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