ID F6CVR2_MARPP Unreviewed; 542 AA.
AC F6CVR2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AEF56536.1};
GN OrderedLocusNames=Mar181_3520 {ECO:0000313|EMBL:AEF56536.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF56536.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF56536.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
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DR EMBL; CP002771; AEF56536.1; -; Genomic_DNA.
DR RefSeq; WP_013798002.1; NC_015559.1.
DR AlphaFoldDB; F6CVR2; -.
DR STRING; 491952.Mar181_3520; -.
DR KEGG; mpc:Mar181_3520; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_6; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR PANTHER; PTHR46577:SF2; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 19..87
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
FT REGION 470..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59971 MW; 8A64E8F8B0B6CE02 CRC64;
MIDNSYKQIS LRRYKAVADF LYKGVVDWFL EQVSQDVLSP GDKMPSLRAL SKQLELSLNT
VIHGYELLVK DGWIESRPKS GYFVCHRSDV KPALLLAGES QYVLEGQETK SAWACLAHHG
ALVDQASGYG QASAKQEDSA LPVLGKGHLA VREVVNDYLK DMGIKSRASQ LWLGRSPLAM
LTQSIQTLTE KGDSVLVITP CDPRLTSTLQ SLGRRVITIT AGDRGVDLDL AIRCLREEPI
RLIVLPGQFS FPTGQLISNL SLRRWLAIIE ETQLPVIEWD LCSHLAYRSG PLLTYKSLDQ
SDHIVYIGGV ENKASEMTMA WCLPGRHHEL LDGAFLAADM ALNDVQQACL SDMLKINSKA
SVMRRARDVW ANSERLKAYL DEQLGDQISL VTSKGGMALW MRLAKPVNKE TMPTLIASFR
HAIVPGDLLS PEQDAAHWLA LNVTVADVEP LVSRLKDYLL VSDLASSEVV SDTNVETTPA
TPQEALDKED LSTADLVEAT DDQASEHAEV KTSQNKSAED EERKTPEPLY NPMLDLINHD
FG
//
