ID A0A1A9WNB1_9MUSC Unreviewed; 665 AA.
AC A0A1A9WNB1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI025923-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI025923-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI025923-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A1A9WNB1; -.
DR STRING; 37001.A0A1A9WNB1; -.
DR EnsemblMetazoa; GBRI025923-RA; GBRI025923-PA; GBRI025923.
DR VEuPathDB; VectorBase:GBRI025923; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000091820; 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}.
FT DOMAIN 578..650
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 665 AA; 74897 MW; 2C98DCC11FBD661C CRC64;
MFRFYSKNFK NVITTVVRFN SFARNTSLEY DVLVIGGGHA GTEACAAAAR MGARTLLVTH
KRETIGEMSC NPSFGGIGKG HLVREVDAMD GVCAKCCDKS GVQYKILNRR RGPAVWGPRA
QIDRILYKKA IQEYIFNMEN LDILSAPVDN LLIEPTAEGE SMQCKGIILQ NGQILKSRTV
VLTTGTFLRA NINFGLEVRP AGRMGDAPAM ALGKNLEDLG FRMGRLKTGT PPRLLRNTID
FSQLSKNIGD NPPVPFSFMN DCVWIQADAQ LPCYLTYTTM KVNQIVKDNL HVNRHVTEEI
TGPRYCPSIE SKVLRFGEKS HQIWLEPEGF ESDVIYPQGL SCTLPYEQQE ELVHSIPGLQ
KAQIKQPGYG VEYDYIDPRE LFSTLETKRV QNLFFAGQIN GTTGYEEAAA QGIIAGANAA
AKTVHKDVKN LTISRTEGYI GVLIDDLTTL GTNEPYRMFT SRSEFRLMLR PDNADLRLTE
KAFNFGLVRK ERYERYLAIR NQLSEAADLL KSIKKRTNDW RQSLHLPTAK VSVEKSAFDM
LGIPSDNITL KQLIDLLPQE LGHLNNVKAL EDRIKIQALY SYFIEEQMHQ VNEVRREENL
IIPRDIDYFS KSLSLSNEER QKLTMIQPQT IAAASRIQGV TPSTVVRLLK FVKRIDQANI
MLCNP
//