ID A0A0X8HW97_9SACH Unreviewed; 680 AA.
AC A0A0X8HW97;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=HHL101Cp {ECO:0000313|EMBL:AMD22669.1};
GN ORFNames=AW171_hschr84720 {ECO:0000313|EMBL:AMD22669.1};
OS Eremothecium sinecaudum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD22669.1, ECO:0000313|Proteomes:UP000243052};
RN [1] {ECO:0000313|EMBL:AMD22669.1, ECO:0000313|Proteomes:UP000243052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD22669.1,
RC ECO:0000313|Proteomes:UP000243052};
RA Dietrich F.S.;
RT "Genome sequence of the yeast Holleya sinecauda.";
RL Submitted (JAN-2016) 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; CP014248; AMD22669.1; -; Genomic_DNA.
DR RefSeq; XP_017989665.1; XM_018134063.1.
DR AlphaFoldDB; A0A0X8HW97; -.
DR STRING; 45286.A0A0X8HW97; -.
DR GeneID; 28726030; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000243052; Chromosome viii.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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 SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 586..657
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 680 AA; 75903 MW; 100E25C956165B02 CRC64;
MLLFRNFYSH KATRAISRRY ISLTSDLRTV LNDLPDSGVV VIGGGHAGCE ASAGAARSGA
PTVLVTPAVD KIGTCSCNPS MGGVGKGTLL REVDALDGLA ARVTDLAGIQ FKMLNRSRGP
AVWGPRAQID RKIYMREMQG MLKNYQNLQI RQGKVSDLII DKDGRSPAAG TPNGIVRGVI
LDNGDIIKSS KVVITTGTFL GGEIHIGMKS FPAGRIGENP TYGISDTLRE LGFQLGRLKT
GTPARLDGKT INFISLKKEY GDDPPHPMSY TNNEVAIKDQ RLCYGTNTTA ELHEYIKNNL
HQTLHIRETI KGPRYCPSIE AKVLRFPDKT SHMIWLEPEG LDTDVIYPNG ISNSMPEDVQ
EVMMRMVPGL ENVKIVQPAY GVEYDYIDPR ELKQTLETKR IDGLFMAGQI NGTTGYEEAC
AQGIIAGINA GLAFQNKPEL RLSRSEAYIG VLIDDLITKG VEEPYRMFTS RSEFRISVRA
DNADFRLTEL ARRLGAISDW RWAKFVPDKA IYDEVKSKLE NFYQPSNKWD NILDSNVRNT
HVKYNAWEML RYTNNSVELI AKGFPELALD LDEIPQHIVL KLDVEAKYTP FLRRQKQFIK
AFEADESIYL PQDIDYNTVA SLSNECKGIL NTVKPITIGQ ARRIQGMTPA SLFELYKLVR
GRQPELQNFY RESTDKGAST
//
