ID A0A3R8IRD2_9BACT Unreviewed; 427 AA.
AC A0A3R8IRD2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800};
GN Name=mnmG {ECO:0000313|EMBL:RRJ95251.1};
GN ORFNames=Ga0100231_013955 {ECO:0000313|EMBL:RRJ95251.1};
OS Opitutaceae bacterium TAV4.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278959 {ECO:0000313|EMBL:RRJ95251.1, ECO:0000313|Proteomes:UP000078325};
RN [1] {ECO:0000313|EMBL:RRJ95251.1, ECO:0000313|Proteomes:UP000078325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV4 {ECO:0000313|EMBL:RRJ95251.1,
RC ECO:0000313|Proteomes:UP000078325};
RA Rodrigues J., Kotak M., Lin J.;
RT "Draft genome sequences of strains TAV3 and TAV4 (Verrucomicrobial:
RT Opitutaceae) isolated from a wood-feeding termite and in silico analysis of
RT their polysaccharide-degrading enzymes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-binding protein involved in the addition of a
CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
CC {ECO:0000256|ARBA:ARBA00003717}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948}.
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
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:RRJ95251.1}.
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DR EMBL; LXWU02000003; RRJ95251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8IRD2; -.
DR Proteomes; UP000078325; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000078325};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 329..400
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 263..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46836 MW; 6B7B02193BA224E5 CRC64;
MTYTTADTAR IARENLTRSA MYSGNITGTG ARYCPSFEDK IVRFADKPRH LLFLEPEGRS
TDEYYVNGLS TSMPFDVQLQ LVRSVPGLEN AILMRPAYAV EYDFAPPTQL FPSLESKKVE
NLFFAGQING TSGYEEAACQ GLVAGVNAVN KVRGAAPLII ARHEAYIGVL IDDLVTKGTT
EPYRMFTSRA EYRLLFNHGS AELRLLHHAR AHGLVSATRL ARIEEKKRRI EHWITTLETT
RIPADIAATA GQGTWGDFIR RAGSAAGQGR GGEGGREASP RPPSDAENTI ETQEPSKRVD
GGLGETSLPL PSDFTALPDE LRHEVLYRVG YKGYLEREQR QIEKLSHVEK IKIPPDFDYR
AVRGLRLESA QKLIAARPYN LGQASRISGV NPADISILMV ALAARNAPAG GRGATGSIEQ
DNGCRHA
//
