ID A0A2N5V5K8_9BASI Unreviewed; 677 AA.
AC A0A2N5V5K8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
GN ORFNames=PCANC_05817 {ECO:0000313|EMBL:PLW53066.1}, PCANC_11396
GN {ECO:0000313|EMBL:PLW16996.1}, PCASD_03998
GN {ECO:0000313|EMBL:PLW45275.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW45275.1, ECO:0000313|Proteomes:UP000235392};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW16996.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW45275.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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}.
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:PLW45275.1}.
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DR EMBL; PGCJ01000858; PLW16996.1; -; Genomic_DNA.
DR EMBL; PGCI01000050; PLW45275.1; -; Genomic_DNA.
DR EMBL; PGCJ01000068; PLW53066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5V5K8; -.
DR STRING; 200324.A0A2N5V5K8; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; 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 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:UP000235388}.
FT DOMAIN 600..671
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 75242 MW; 88B034809AB3AADC CRC64;
MFAWLSSTRA IARRYLPPSV PASRRLPSTR RFSRTNDTFA TPHDAQIPAP DSPDTWDVVV
LGGGHAGVEA ASAASRTNSR TLLVTSNWNT VGEMSCNPSF GGIGKGTLIR EVDALGGECG
RACDEAGIVF QMLNRSKGPA VYGPRAQMDR GLYKEAIQRQ INSHANLVVK EGTVTDLLLS
DDPSEPKTNS SRRVVGLQLE TGETLHCKAV VIATGTFLGG EIHIGGKTSA FGRMGERSST
SLSNSLRQCG FKLARMKTGT PPRISKRSIN FEDLMVQLGD VPPKPFSFLN KTVRHADQQL
CCWKTQTTKA THQIVQENLH LSSYVREEVH GPRYCPSLEA KVTRFSQRDA HMIWLEPEGF
HSDLIYPNGI STTMPEDAQL KMMRTIPGLE DVEMVQPGYG VEYDHIDPRE LKNTLETKAI
HGLFLAGQIN GTTGYEEAAA QGVLAGINAG LQCREASPLI LTRADSFIGV LVDDLITKGV
QEPYRMFTSR SEFRVALRVD NADLRLTEKA WQCGVIDEGR WKVMQDTKSK IDGLILALQS
VSLPQQTWAR HGIKVREDAI QKTAFDVLRV QGVKMECLKP IVPELEGLEE EIWRRVEVEA
LYGPIIKRYE ANVEELMQDE HMMLPRSLNY SELEYLSSEA RQKLSECRPL TLGVAKRLQG
IDPSELILLR KHLRHMA
//
