ID A0A0S2JHH3_9GAMM Unreviewed; 440 AA.
AC A0A0S2JHH3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ALO35447.1};
GN ORFNames=CMT41_12510 {ECO:0000313|EMBL:ALO35447.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO35447.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO35447.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO35447.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013145; ALO35447.1; -; Genomic_DNA.
DR RefSeq; WP_058027444.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JHH3; -.
DR STRING; 58049.CMT41_12510; -.
DR KEGG; com:CMT41_12510; -.
DR OrthoDB; 9802793at2; -.
DR Proteomes; UP000065319; 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; 1.
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 PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ALO35447.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..440
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006600246"
FT DOMAIN 278..414
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 206..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 46959 MW; FF2CF2C644E0BC26 CRC64;
MKNIQLITSL RYVLFGALAL TTSAVQAEKI AITNATVYTV AEQGVLLQAT VVIEGGKITA
VYSKDDVPDS LNADTIIDAK GRILTPGFIA TKNLLGLVEV GAVSDTRDGS DKKADLTFDA
SLAFNPKSSL IPYARKGGIT SNLVMPHGGE KVFTGQSFVV NLSGEFDSVI VSQNAVIVSL
GSTRKGSRAV KLQTLSNELE DAQKSLAKAE KAKAKKKKSQ GKDKEDKEEK EEKEAKTPSR
AEQVMYALLS GEKPLLAYAD RATDILALLK IKQKYNLDLI LVGASDAVLV SEEIAKAKVT
VMMSAIDNLP TSFDSLHTSL ANVAILSKAG VTVIITNSGE SHNINQLRFD AGVAIANGLA
ETTALAAITA NVADSFNLNS GRIVVGKNAD LVLWSSDPFE ISTKVDAMWI NGNAMSLTSR
QDALRQRYTA DTDMPRAYTK
//