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Database: UniProt
Entry: A0A1H4DZ47_9FIRM
LinkDB: A0A1H4DZ47_9FIRM
Original site: A0A1H4DZ47_9FIRM 
ID   A0A1H4DZ47_9FIRM        Unreviewed;       304 AA.
AC   A0A1H4DZ47;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Cro/C1-type HTH DNA-binding domain-containing protein {ECO:0000313|EMBL:SEA78053.1};
GN   ORFNames=SAMN05216349_12833 {ECO:0000313|EMBL:SEA78053.1};
OS   Oribacterium sp. KHPX15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=1855342 {ECO:0000313|EMBL:SEA78053.1, ECO:0000313|Proteomes:UP000199483};
RN   [1] {ECO:0000313|EMBL:SEA78053.1, ECO:0000313|Proteomes:UP000199483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHPX15 {ECO:0000313|EMBL:SEA78053.1,
RC   ECO:0000313|Proteomes:UP000199483};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNRG01000028; SEA78053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4DZ47; -.
DR   Proteomes; UP000199483; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:SF38; PROTEIN ADENYLYLTRANSFERASE AQ_AA38-RELATED; 1.
DR   Pfam; PF02661; Fic; 1.
DR   Pfam; PF13443; HTH_26; 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   DNA-binding {ECO:0000313|EMBL:SEA78053.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR640198-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199483}.
FT   DOMAIN          7..60
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   DOMAIN          151..298
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-1"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   BINDING         267..268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-2"
FT   SITE            101
FT                   /note="Important for autoinhibition of adenylyltransferase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640198-3"
SQ   SEQUENCE   304 AA;  34938 MW;  092DDAA15A08B465 CRC64;
     MISYEGLEKA LKEKGIGKTV LSTELGLSTR TIAKIKKGEK LSKRSIQKIA DYLCESPDVI
     MREISDNRIL QVLRDEKAIR MPGGLYHELQ VRMTYNSNHI EGSKLSEDQT RLIFETNTID
     VGDGIPVDDI LETVHHFRAI DYVIDVAEDQ LTEDMIKHLH YILKHDTKDS TLGWFAVGDY
     KKRANIVGGR ETSKPSEVHK HMKALIDGYN AKDNVTIEDI IAFHAEFEYI HPFQDGNGRV
     GRLVALKECL RYNVIPFIIE DAKKNYYYRG LSEWRNEKGW LMDTCLDGQD TFKSLLDMLE
     ILQE
//
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