ID A0A0M4H3Z8_9ACTO Unreviewed; 320 AA.
AC A0A0M4H3Z8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cell filamentation protein Fic {ECO:0000313|EMBL:ALC98615.1};
GN ORFNames=AM609_02395 {ECO:0000313|EMBL:ALC98615.1};
OS Actinomyces sp. oral taxon 414.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC98615.1, ECO:0000313|Proteomes:UP000061022};
RN [1] {ECO:0000313|Proteomes:UP000061022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012590; ALC98615.1; -; Genomic_DNA.
DR RefSeq; WP_053585994.1; NZ_CP012590.1.
DR AlphaFoldDB; A0A0M4H3Z8; -.
DR STRING; 712122.AM609_02395; -.
DR KEGG; acq:AM609_02395; -.
DR PATRIC; fig|712122.3.peg.539; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000061022; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR013196; HTH_11.
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:SF38; PROTEIN ADENYLYLTRANSFERASE AQ_AA38-RELATED; 1.
DR Pfam; PF02661; Fic; 1.
DR Pfam; PF08279; HTH_11; 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR640198-2}.
FT DOMAIN 99..241
FT /note="Fido"
FT /evidence="ECO:0000259|PROSITE:PS51459"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT BINDING 219..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT SITE 55
FT /note="Important for autoinhibition of adenylyltransferase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ SEQUENCE 320 AA; 35347 MW; 7D33CA92D480AA13 CRC64;
MAHEPPLVRT AEINALCMEI AELVGALGSA SALSTSPVLH RELRITTIHS SLMIEGNTLS
REAVTAILDG KRVLGPARQI LEVDNARRAY RLMDDLDPLS PDDLLRAHGV MMRGLIDDAG
RYRAGNTGVF KEGGLIHAGT PARYIPEVMT DLFAWMTSTD LHPLTASCVF HYEFEFIHPF
SDGNGRTGRL WHTLLLSHWR PALAWLPIES VIRDRQEGYY EAIARSNARG SSETFVTFML
TVIRDALTPY ATAPSTRNRR EQVLLFLDAN PRATIKALAE HLGCSRRTAE RAVAALRDSG
RLAREGSARA GTWRVIADGP
//
