ID   A0A0G1UA42_9BACT        Unreviewed;       342 AA.
AC   A0A0G1UA42;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Fic family protein {ECO:0000313|EMBL:KKU90984.1};
GN   ORFNames=UY21_C0014G0015 {ECO:0000313|EMBL:KKU90984.1};
OS   Microgenomates group bacterium GW2011_GWA1_48_10.
OC   Bacteria.
OX   NCBI_TaxID=1618496 {ECO:0000313|EMBL:KKU90984.1, ECO:0000313|Proteomes:UP000034718};
RN   [1] {ECO:0000313|EMBL:KKU90984.1, ECO:0000313|Proteomes:UP000034718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU90984.1}.
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DR   EMBL; LCPD01000014; KKU90984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1UA42; -.
DR   Proteomes; UP000034718; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   InterPro; IPR040198; Fido_containing.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13504; FIDO DOMAIN-CONTAINING PROTEIN DDB_G0283145; 1.
DR   PANTHER; PTHR13504:SF34; PROTEIN ADENYLYLTRANSFERASE FICD; 1.
DR   Pfam; PF02661; Fic; 1.
DR   Pfam; PF13463; HTH_27; 1.
DR   SUPFAM; SSF140931; Fic-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51459; FIDO; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR640198-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR640198-2}.
FT   DOMAIN          106..256
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT   BINDING         137..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   BINDING         197..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   SITE            61
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ   SEQUENCE   342 AA;  39449 MW;  0B105EED5E956ED5 CRC64;
     MRYTPVVFKP KYSLTPKILL NINEIERLYG RLEGMTIPQQ LLLNLERDNL IQSSFASNSI
     EGNPLSEAQV SNLILNDRVP VNRDEKEVVN YFQILKELPT KVNRDLNLNH VLDTHKHLLT
     GVKENIKGKI RNTRIVVGSH DVIDRLVIKY NPPFHTKREI VEALEGLLLW VKKTKEPPTL
     KAGIFHHQFV FLHPFEDGNG RVCRLLTALI FLKHNYLINK YFVLDDYYDI DRSLYSDSLH
     SADSGDKTTW LEYFTDGVKY SLAGALGKVE TGLTQLTFDI RLTPKEQEVL KIIQKYRELN
     SSDLTKELAI SRQQAFNLLK SLTKKGYLEK KGSTKSSYYV LK
//