ID H9EWT8_MACMU Unreviewed; 692 AA.
AC H9EWT8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN Name=MTO1 {ECO:0000313|EMBL:AFE66847.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE66847.1};
RN [1] {ECO:0000313|EMBL:AFE66847.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE66847.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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 EMBL; JU323091; AFE66847.1; -; mRNA.
DR AlphaFoldDB; H9EWT8; -.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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 2: Evidence at transcript level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 586..659
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 669..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 77162 MW; 3FAC234E6D581B3B CRC64;
MFYLRGCGRW VAASFTKQQF PLVRLSSDSA APRTPHFDVI VIGGGHAGTE AATAAARCGS
RTLLLTHRVD TIGQMSCNPS FGGIGKGHLM REVDALDGLC SRICDQSGVH YKVLNRRKGP
AVWGLRAQID RKLYKQNMQK EILNTPLLTV QEGAVEDLIL TEPEPEHTGK CRVSGVVLVD
GSTVYAESVI LTTGTFLRGM IVIGLEMHPA GRLGDQPSIG LAQTLEKLGF VVGRLKTGTP
PRIAKDSINF SILNKQTPDN PSVPFSFTNE TVWIKPEDQL PCYLTYTNPR VDEIVLNNLH
LNSHVKETTR GPRYCPSIES KVLRFPNRLH QVWLEPEGMD SDLIYPQGLS MTLPTELQEK
MITCIRGLEK AKVIQPGYGV QYDYLDPRQI TPSLETHLVQ RLFFAGQING TTGYEEAAAQ
GVIAGINASL RVSRKPPFVV SRTEGYIGVL IDDLTTLGTS EPYRMFTSRV EFRLSLRPDN
ADIRLTLRGY KDAGCVSQQR YEGACWMKSS LEEGISVLKS IEFSSSKWKN LIPEVSISTS
RSLPVRALDV LKYEEVDMDS LAKAVPEPLK KYTKCRELAE RLKIEATYES VLFHQLQEIK
GVQQDEALQL PKDIDYLTIR DVSLSHEVRE KLHFSRPQTI GAASRIPGVT PAAIINLLRF
VKTTQQRQAA MNESPKTDQC LRNADRLQER QL
//
