ID A0A1Q7WQ30_9CHLR Unreviewed; 376 AA.
AC A0A1Q7WQ30;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HTH merR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUG45_08855 {ECO:0000313|EMBL:OLE32874.1};
OS Ktedonobacter sp. 13_1_20CM_3_54_15.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805224 {ECO:0000313|EMBL:OLE32874.1, ECO:0000313|Proteomes:UP000186882};
RN [1] {ECO:0000313|EMBL:OLE32874.1, ECO:0000313|Proteomes:UP000186882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE32874.1}.
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DR EMBL; MNJJ01000163; OLE32874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7WQ30; -.
DR Proteomes; UP000186882; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd02065; B12-binding_like; 1.
DR CDD; cd01104; HTH_MlrA-CarA; 1.
DR Gene3D; 1.10.1660.10; -; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR047057; MerR_fam.
DR InterPro; IPR036594; Meth_synthase_dom.
DR PANTHER; PTHR30204:SF67; HTH-TYPE TRANSCRIPTIONAL REGULATOR MLRA-RELATED; 1.
DR PANTHER; PTHR30204; REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF02607; B12-binding_2; 1.
DR Pfam; PF13411; MerR_1; 1.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT DOMAIN 31..90
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
FT DOMAIN 249..376
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 118..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 42064 MW; 8E5EFAEC1F92ADE2 CRC64;
MTVRDGQSEW LDLERYSDNP IFNTKAVVQQ TGVPAPTLRA WERRYDILSP ERANNDYRLY
SERDIATIHW LKERVDEGMS ISQAIALFRH MKEEYQRLIE ERSPSATGSP SFYVSLPEAS
AEERPAGSKK QSSPEIEETQ AQPPVKEWSL TDAERGNYQV IFNLRTVQEH LLAAFKKFDE
STASTLMTSV LSIYTVEQAC TDLIAPTMWQ IGKMWEVGTI TVSVEHFASG FFRGLLTNLL
HVSPSSNAGP LVIVCCAPGE AHELAPLMLA LFLRRAGIRV AYLGQSIEAV GLLQTIKQIA
PTLICVSLSI PAYLATLIEL ARQVQELPLP RPFFVFGGQV FVHYPHLIPQ VPGIHLGGEL
KKSTAQLQRM IAERDS
//
