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Database: UniProt
Entry: R6K9K6_9FIRM
LinkDB: R6K9K6_9FIRM
Original site: R6K9K6_9FIRM 
ID   R6K9K6_9FIRM            Unreviewed;       297 AA.
AC   R6K9K6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Filamentation induced by cAMP protein Fic {ECO:0000313|EMBL:CDB67759.1};
GN   ORFNames=BN564_01424 {ECO:0000313|EMBL:CDB67759.1};
OS   Eubacterium sp. CAG:252.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262887 {ECO:0000313|EMBL:CDB67759.1, ECO:0000313|Proteomes:UP000017970};
RN   [1] {ECO:0000313|EMBL:CDB67759.1, ECO:0000313|Proteomes:UP000017970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:252 {ECO:0000313|Proteomes:UP000017970};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDB67759.1}.
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DR   EMBL; CBEA010000064; CDB67759.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6K9K6; -.
DR   Proteomes; UP000017970; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   InterPro; IPR040198; Fido_containing.
DR   InterPro; IPR041657; HTH_17.
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; PF12728; HTH_17; 1.
DR   SUPFAM; SSF140931; Fic-like; 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          143..293
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT   BINDING         227..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   BINDING         259..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   SITE            92
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ   SEQUENCE   297 AA;  34603 MW;  705A35DE38447156 CRC64;
     MYLNVKETAE KWKISERSVR NYCSQGKIPG AIIDGKSWKI PKNAVKPVRK KRNAMIPRDL
     LTRLTIEKES GISGGIYHKI QIDLTYNSNH IEGSRLSHDQ TRYIFETNTI GIQNETVNVD
     DIVETANHFK CIDLIIDLAN YPLSESLIKQ LHLILKSGTS DNRKSWFTVG DYKRIENEVG
     GMPTTKPENV CKELKALLKS YNNIKQKSLK EIIEFHYEFE KIHPFQDGNG RVGRLIMFKE
     CLRNGITPFI IEDDIKEFYY RGLKEWKNEQ GYLIDTCLTA QDRFKTYLDY FAIEYKD
//
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