ID A0A1L7X4P2_9HELO Unreviewed; 659 AA.
AC A0A1L7X4P2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Probable MTO1 protein {ECO:0000313|EMBL:CZR59993.1};
GN ORFNames=PAC_09888 {ECO:0000313|EMBL:CZR59993.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR59993.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR59993.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR59993.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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}.
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; FJOG01000015; CZR59993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7X4P2; -.
DR STRING; 576137.A0A1L7X4P2; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000184330; 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 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; 2.
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:UP000184330}.
FT DOMAIN 560..631
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 659 AA; 72958 MW; 075B12CAE02CE467 CRC64;
MKRALVRNYR PSTSWLCRSR TVRQQRRSFA DVASDTRPYD VVVIAQIDRK LYKKHMREEL
EAYPNLSIVP GSVADIIVTP EEGQNVGGRI TGGLFLEEKY TLASNEGPRA QIDRKLYKKH
MREELEAYPN LSIVPGSVAD IIVTPEEGQN VGGRITGVRL ESGEIIPTDR VIITTGTFLG
GEIHIGLECH PAGRMGEAAT FGLSKSLKDA GFKLGRLKTG TPPRLAKDSI DFGILAAQPG
DDPPMPFSYL NDSVLVQEQM LCYATYTNER THDIVRDNLD KSIHIRETVK GPRYCPSLES
KVIRFADKQK HIVWLEPEGF DSDVIYPNGI SMTVPAEAQE QLLKTIKGLE NVTMLQPGYG
VEYDYVDPRS LKSTLETKAI QGLYLAGQIN GTTGYEEAAA QGIIAGINAG LAAQSKPPIT
LSRSDGYIGI MIDDLITKGV SEPYRMFTSR SEYRMSARAD NADLRLTAKG REAGIVGDKR
WSSFCDEVAQ MDALKASLVA KVSSPPTWIK DGFKVGNDST RRSAFDVLRL AGVTVTDMAT
LVPEVLTHST RIRDRVGIEA VYAPYVQQQT AAMKVFQKDE NLKLPLDLNY ASIHGLSMHE
KAMLNETRPE SVGQARRIEG MTPSGTLRLL AYVQSRQRTV TKTAIFDEIA ARKKMYMVD
//
