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Database: UniProt
Entry: A0A1F9KAI9_9DELT
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Original site: A0A1F9KAI9_9DELT 
ID   A0A1F9KAI9_9DELT        Unreviewed;       260 AA.
AC   A0A1F9KAI9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGQ77645.1};
GN   ORFNames=A3F90_16835 {ECO:0000313|EMBL:OGQ77645.1};
OS   Deltaproteobacteria bacterium RIFCSPLOWO2_12_FULL_60_19.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1797894 {ECO:0000313|EMBL:OGQ77645.1, ECO:0000313|Proteomes:UP000177611};
RN   [1] {ECO:0000313|EMBL:OGQ77645.1, ECO:0000313|Proteomes:UP000177611}
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:OGQ77645.1}.
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DR   EMBL; MGSS01000158; OGQ77645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F9KAI9; -.
DR   STRING; 1797894.A3F90_16835; -.
DR   Proteomes; UP000177611; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01745; GATase1_2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR011697; Peptidase_C26.
DR   InterPro; IPR044668; PuuD-like.
DR   PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   260 AA;  28348 MW;  73C017A9042A1ACC CRC64;
     MTGRSRRQPL IGITPDVATA PTSKPDGKGE PLIVLQARYA RAIEQAGAVP MVLLITGSRA
     TMRTNLDRLD GLVVSGGNFD IHPEFYGEKP IDGLRHIRKE RTEFELGLIS LALKRDLPLL
     GICGGAQAIN VAVGGTLYQD IGTQIAGAGK HEQGALKDRG GHEVRIHEGT KLRAIVGRAS
     LEVNTTHHQA VKELGKGLLV NATAGDSVIE GIESKDHSFV LGVQWHPEFL THRDRWQKKI
     FSAFVTSCPQ KRLKPRTVRR
//
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