ID A0A0C9LW58_9FUNG Unreviewed; 705 AA.
AC A0A0C9LW58;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Mitochondrial translation optimization protein {ECO:0000313|EMBL:GAN07950.1};
GN ORFNames=MAM1_0183c07455 {ECO:0000313|EMBL:GAN07950.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN07950.1};
RN [1] {ECO:0000313|EMBL:GAN07950.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN07950.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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; DF836472; GAN07950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LW58; -.
DR STRING; 91626.A0A0C9LW58; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.40.30.260; -; 1.
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 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:UP000053815}.
FT DOMAIN 621..692
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 705 AA; 78288 MW; C8B3FDC6F1C7F048 CRC64;
MLRGLSSLRY RSSRLQCQHH FHTCHPWKQA TIAADIPTQR EFDVIVIGGG HAGTEACAAA
ARSGAKTLLL TQNKDTIGEM SCNPSFGGVG KGVLVREIDA LDGVCGRISD LAGIQFKVLN
KSKGPAVYGP RAQIDRKLYK KHLQSYLKDY PNLTIQSGSV SDLVLNDSVT EEEQQKMASK
GASQIVKGVR LENGQVIRAS NVIITTGTFL GGEIHLGLKV WPAGRIGENP SIGLSNSLKS
AGFQLARLKT GTPARLDGRT INYEGLIIQE GDNPPAPFSY LNTTVPHADH QILCHQTRTN
PQVHKYIADH FDQSIHIRET VKGPRYCPSL ESKIKRFSTK EAHNIWLEPE GLDTSVVYPN
GISNTMPEDV QLTFLRMIRG LENVDMLKPG KTRVLMVGHT EMAKLVFLTA YGVEYDHIDP
RELRSTLETK RISGLFLAGQ INGTTGYEEA AAQGVMAGIN AGLHAQGKAP FILDRSDAYI
GVLIDDLITK GVEEPYRVFT ARSEYRLLLR ADNADTRLTE KGYNAGVIGK ERWEHYQTSS
KALKSAMDAL QSLRMPAKRW AEHDISPSTR VSTDHLNDHG ALRSGMDLLT WPNVALEQFQ
DLLPELKHLA PSLKERVMIE GRYKPFLKRQ ELEVAALKRD EHLTLDINLD YLQMDQLSNE
VRQKLAEVRP ETLGAAKRIE GMTPAAMVVL MKYAKRTYNR KVFAN
//