ID   G0S501_CHATD            Unreviewed;       718 AA.
AC   G0S501;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
GN   ORFNames=CTHT_0023580 {ECO:0000313|EMBL:EGS20526.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS20526.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL988041; EGS20526.1; -; Genomic_DNA.
DR   RefSeq; XP_006692822.1; XM_006692759.1.
DR   AlphaFoldDB; G0S501; -.
DR   STRING; 759272.G0S501; -.
DR   GeneID; 18256396; -.
DR   KEGG; cthr:CTHT_0023580; -.
DR   eggNOG; KOG2311; Eukaryota.
DR   HOGENOM; CLU_007831_2_2_1; -.
DR   OMA; CNPAMGG; -.
DR   OrthoDB; 5486689at2759; -.
DR   Proteomes; UP000008066; 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; 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:UP000008066}.
FT   DOMAIN          603..674
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   718 AA;  78884 MW;  D8912BF7FE38A8D5 CRC64;
     MTIKLGLFRG LGRPLLRPIQ QHGSLCTPRI KRTFATVEDD FNARNFDVIV VGGGHAGSEA
     SAAAARAGAR TALITPDINN LGVCSCNPSF GGIGKGTILR EIDALDGLAG RIIDKAGVQF
     RVLNRKKGPA VWGPRAQIDR SLYKKYMREE LQSYPNLSVI LGRVSDIVTA DAHDDPNADG
     AKSKITGIRL ESGETLTTNQ VVITTGTFLG GEIHIGLESW PSGRIGEPPT YGLSKSLRAA
     GFKLGRLKTG TPPRLHKNSI KWNILEPQAG DEPPVPFSYM DDEVAVKDQL LCYATYTNTA
     THDIVRANLD KTIHIRETVK GPRYCPSLES KIIRFGDRER HIVWLEPEGF DTDVIYPNGL
     SMTVPAQAQE QLLRTIRGLE DVVMLQPGYG VEYDYVDPRS LKRSLETKAI RGLWLAGQIN
     GTTGYEEAAG QGILAGINAG RASKGLPPIT LSRADAYIGI MIDDLITKGV SEPYRMFTSR
     SEFRLSARPD NADVRLTPLG REAGVVSDAR WSRFSDDRAC AEHLLRLLRK TSLTVSQWRA
     AGLPINPVRD ETRRRDGFEA LRMPGVQPSH LRLILPFLKN HSSLSAASAD FPDRIIDRVA
     IEAVYEPYVR MQESEAARLR RDEGLCLPPD LDYDSVFGLS IVEKQVLKEA RPENIAQAKR
     IEGVTPAGLV RLLKYTTRGS SWDKSSAESV VVEGLDMSGV EDLEALDARS RVEDMKGL
//