ID N1JCN1_BLUG1 Unreviewed; 676 AA.
AC N1JCN1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme gidA {ECO:0000313|EMBL:CCU77329.1};
GN ORFNames=BGHDH14_bgh04222 {ECO:0000313|EMBL:CCU77329.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77329.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU77329.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU77329.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU77329.1}.
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DR EMBL; CAUH01003577; CCU77329.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JCN1; -.
DR STRING; 546991.N1JCN1; -.
DR EnsemblFungi; BLGH_04131-mRNA-1; BLGH_04131-mRNA-1; BLGH_04131.
DR eggNOG; KOG2311; Eukaryota.
DR HOGENOM; CLU_007831_2_2_1; -.
DR InParanoid; N1JCN1; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IEA:EnsemblFungi.
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:UP000015441}.
FT DOMAIN 578..649
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 676 AA; 74649 MW; CD6934102AEA2431 CRC64;
MKKRFSSTLT LCRGLKKSHQ NLINTRKLHS SGIFETNNKQ YDVVVIGGGH AGSEACTGAA
RSGAKTVLIT PKLDNIGVCS CNPSFGGIGK GTMLREIDAL DGVSSRIIDN AGVQFKVLNR
KKGPAVWGPR AQIDRKLYQR FMRSELESYP NLQILLGSVA DIVVSKDEDE KKITGVRLES
GEVIMTKKVV ITTGTFLGGE IHIGLVVYPS GRMGEAATHG LSKSLKDAGF TLGRLKTGTP
PRLLKGSIDF KLMEKQFGDD PPVPFSFLNE TVSVQDQLVC YSTYTNEAAH DVVRANLDKS
IHIRETVKGP RYCPSLESKI IRFADRDKHI IWLEPEGFDS EVIYPNGISM TIPAEAQEQV
LKKIKGLENV SILQPGYGVE YDYVDPRSLK STLETKAIQG LYLAGQINGT TGYEEAAAQG
IVAGINAGLS SQFRPSLILS RADGYIGIMI DDLITKGVSE PYRMFTSRCE YRMSSRADNA
DIRLTRKGRE AGIVGDSRWR TFSDERTQIQ ELTSILQAKF ASSPTWIDAG FKVSNGSTKR
SAFDLLRVTG VTPLDIAHIL PEINNYSPRI QTRVGIESTY APYILQQETQ LNQFKRDEST
KLPIDLDYNS IFGLSMHEKS LLDATKPETL GQAKRIEGLT PAGILRLLAF IQDRRRASAR
EAALQEVQNR KELYIV
//
