ID A0A1M5R6B9_9FLAO Unreviewed; 349 AA.
AC A0A1M5R6B9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Helix-turn-helix domain-containing protein {ECO:0000313|EMBL:SHH21580.1};
GN ORFNames=SAMN05443373_10957 {ECO:0000313|EMBL:SHH21580.1};
OS Flavobacterium granuli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=280093 {ECO:0000313|EMBL:SHH21580.1, ECO:0000313|Proteomes:UP000184384};
RN [1] {ECO:0000313|Proteomes:UP000184384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19729 {ECO:0000313|Proteomes:UP000184384};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQWO01000009; SHH21580.1; -; Genomic_DNA.
DR RefSeq; WP_072944645.1; NZ_PVUB01000008.1.
DR AlphaFoldDB; A0A1M5R6B9; -.
DR STRING; 280093.SAMN05443373_10957; -.
DR OrthoDB; 9814400at2; -.
DR Proteomes; UP000184384; 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:0003677; F:DNA binding; IEA:InterPro.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR040198; Fido_containing.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_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; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF140931; Fic-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS51459; FIDO; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR640198-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR640198-2}.
FT DOMAIN 5..59
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT DOMAIN 195..334
FT /note="Fido"
FT /evidence="ECO:0000259|PROSITE:PS51459"
FT COILED 79..117
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT BINDING 312..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT SITE 145
FT /note="Important for autoinhibition of adenylyltransferase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ SEQUENCE 349 AA; 39758 MW; ED886272AA430BF8 CRC64;
MKTLLKTARE QKGLKTREVA QILSIDQALI SKFETGTRKP TREQLIKLAA LLEIDLEPLM
IIWLKEKIIQ EIGHEEFALQ ALKAAKEEIK SNRESSVKKV SALLQKLLDE IDLLKAKLHP
FRPLENSTLQ QIIELEFTHS SNWIEGNTLT LTETDLVVNE GQTIEGKSMR EHLEAINHQE
ALAFIKSVIQ KNTPFGEKEL LSLHSIILRG IVPKEAGHYR NISISIKDNS FIPAEPPTIS
KEIDALFNWY ESNKNSIHPI ILAATVKERL MTIHPFINGN GKVSRLIMNL ILLQHGYQIA
NIKANENERM LYYQTLKASL TRENKENFIV FVAQNEKANL EKCLESSSQ
//
