ID A0A0K6G4E5_9AGAM Unreviewed; 651 AA.
AC A0A0K6G4E5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000313|EMBL:CUA73238.1};
GN ORFNames=RSOLAG22IIIB_10651 {ECO:0000313|EMBL:CUA73238.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA73238.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA73238.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA73238.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC {ECO:0000256|ARBA:ARBA00002739}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
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DR EMBL; CYGV01001361; CUA73238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6G4E5; -.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
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 NCBIfam; TIGR00136; gidA; 1.
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 Pfam; PF21680; GIDA_C_1st; 1.
DR PRINTS; PR00411; PNDRDTASEI.
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 Reference proteome {ECO:0000313|Proteomes:UP000044841}.
FT DOMAIN 567..638
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 651 AA; 71184 MW; E1141C4182C1C4C8 CRC64;
MISSRSRLGA QIQRYATWAR KYDVCVIGGG HAGCEAAAGA ARTGARTVLL TQKLETVGEM
SCNPSIGGVG KGTLVREVDA LGGVMGRAAD EAGIQWHMLN RSKGPAVWGP RAQMDRTLYK
QAVQSALART PNLETRAASV HDLVLQPHSS ANPLTQQKVM GVRLDTGETI ECSEVVICTG
TFLAGEIHIG HKSFPAGRHN DAASPASGLS ASLHRAGFKL GRLKTGTPAR LDKQGINFDR
LERQDGDIPA SRFAYWGPGV KYEDRQVACY KTTTTPETHR IITDNIDKTM HIRETVKGPR
YCPSLEAKVL RFTEKSGHII WLEPEGFDSD LIYPNGLSNS MPEDVQELLV RSVPGLENAK
IVRPAYGVEY DHIDPRELNH TLETKRIRGL FLAGQINGTT GYEEAAAQGI LAGINAGLSA
LGKKPIVIGR AEGYLGVMVD DLIGKGVEEP YRMFTSRAEY RMSIRSDNAD LRLTPKGRAA
GVVCDGRWSE FESMKRDIEK AVELLERCVL SPRKWEAHGV PAKRDGVPRS GLDMLRNPGM
DCQKLTRAIP ELGKLNPKAL ERVEIEGQYM HHLKRQEADI RAFASDEMLT LDPSLDYDSV
IGLSTEVRER LKRARPGNIG AAKRMEGMTA SSAVLLLRHA RRTMSAGPTV A
//
