ID A0A3S1GYM4_ELYCH Unreviewed; 621 AA.
AC A0A3S1GYM4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
DE Flags: Fragment;
GN ORFNames=EGW08_023454 {ECO:0000313|EMBL:RUS68783.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS68783.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS68783.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS68783.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS68783.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) 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 -!- 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:RUS68783.1}.
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DR EMBL; RQTK01002014; RUS68783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1GYM4; -.
DR STRING; 188477.A0A3S1GYM4; -.
DR Proteomes; UP000271974; 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 Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 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:UP000271974}.
FT DOMAIN 541..612
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RUS68783.1"
SQ SEQUENCE 621 AA; 68831 MW; 60E1A5FDA9059458 CRC64;
YDVIVIGGGH SGTEAATAAA RAGAKTLLLT HNIDTIGQMS CNPAIGGIGK GHLVREIDAM
GGVMGKAIDM AGIQFRTLNS RKGPAVRATR AQADRVLYRK AVNSLLSQYD NLDIFQDSVD
DLEVQNNTVT GAITQTGITF RAKKVILTVG TFLGGKIHIG KISQSGGRAG DKPSNALAAR
LRALPFRVDR LKTGTPPRID RRSVDFSVME VQHGDTPAPY FSFFSKGKIE HPAQVPCHIT
YTNAETHKII TDNLDKSAMY GGLIEGIGPR YCPSIEDKVV RFADKDRHQI FVEPEGLESL
ELYPNGLSTS LPFDVQMQYI RSIKGFENAL IMRPGYAIEY DFFDPRDLKP TLETKFIKNL
YFAGQINGTT GYEEAGAQGL VAGINAAISI DSDKSWYPTR ADGYIGVLID DLITKGTKEP
YRMFTSRAEY RLILREDNAD LRLSPTACKL GLLTPEDKAI FKKKEQLISS NIEYLKKTWI
GPQTQKARDL EQFLDKKMTR EATLFDLLKR PELDYSKLKQ ISDLDLNLAD EYVIEQIEIS
AKYSGYIDRQ NKDVSRATLL EDKKIPDDFD YKCVKGLSNE VLQKLSEQKP TTLGEASRIP
GITPAAISLL TIYMKKTGFI K
//
