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Database: UniProt
Entry: A0A0D9RNI4_CHLSB
LinkDB: A0A0D9RNI4_CHLSB
Original site: A0A0D9RNI4_CHLSB 
ID   A0A0D9RNI4_CHLSB        Unreviewed;       692 AA.
AC   A0A0D9RNI4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN   Name=MTO1 {ECO:0000313|Ensembl:ENSCSAP00000010173.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000010173.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000010173.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000010173.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   EMBL; AQIB01132997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008011677.1; XM_008013486.1.
DR   AlphaFoldDB; A0A0D9RNI4; -.
DR   STRING; 60711.ENSCSAP00000010173; -.
DR   Ensembl; ENSCSAT00000012127.1; ENSCSAP00000010173.1; ENSCSAG00000014033.1.
DR   GeneID; 103243897; -.
DR   KEGG; csab:103243897; -.
DR   CTD; 25821; -.
DR   eggNOG; KOG2311; Eukaryota.
DR   GeneTree; ENSGT00390000011297; -.
DR   OMA; CNPAMGG; -.
DR   OrthoDB; 5486689at2759; -.
DR   BioGRID-ORCS; 103243897; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 17.
DR   Bgee; ENSCSAG00000014033; Expressed in liver and 7 other cell types or tissues.
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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT   DOMAIN          586..659
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   692 AA;  77256 MW;  890D3AFD2851691C CRC64;
     MFYFRGCGRW VAASFTKQQF PLARLSSDSA APRTPHFDVI VIGGGHAGTE AATAAARCGS
     RTLLLTHRVD TIGQMSCNPS FGGIGKGHLM REVDALDGLC SRICDQSGVH YKVLNRRKGP
     AVWGLRAQID RKLYKQNMQK EILNTPLLTV QEGAVEDLIL TEPEPEHTGK CRVSGVVLVD
     GSTVYAESVI LTTGTFLRGM IVIGLEMHPA GRLGDQPSVG LAQTLEKLGF LVGRLKTGTP
     PRIAKDSINF SILNKQTPDN PSVPFSFTNE TVWIKPEDQL PCYLTHTNPR VDEIVLKNLH
     LNSHVKETTR GPRYCPSIES KVLRFPNRLH QVWLEPEGMD SDLIYPQGLS MTLPAELQEK
     MITCVRGLEK AKVIQPGYGV QYDYLDPRQI TPSLETHLVQ RLFFAGQING TTGYEEAAAQ
     GVIAGINASL RVSRKPPFVV SRTEGYIGVL IDDLTTLGTS EPYRMFTSRV EFRLSLRPDN
     ADIRLTLRGY KDAGCVSQQR YERACWMKSS LEEGISVLKS IEFSSSKWKN LIPEVSISTS
     RSLPVRALDV LKYEEVDMDS LAKAVPEPLK KYTKCRELAE RLKIEATYES VLFHQLQEIK
     GVQQDEALQL PKDIDYLTIR DVSLSHEVRE KLHFSRPQTI GAASRIPGVT PAAIINLLRF
     VKTTRQRQAA MNESLKTDQC LRDADRLQER QL
//
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