ID T1EEI4_HELRO Unreviewed; 694 AA.
AC T1EEI4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN Name=20194986 {ECO:0000313|EnsemblMetazoa:HelroP108353};
GN ORFNames=HELRODRAFT_108353 {ECO:0000313|EMBL:ESN91521.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP108353, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN91521.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP108353}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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; AMQM01002097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMQM01002098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097700; ESN91521.1; -; Genomic_DNA.
DR RefSeq; XP_009030366.1; XM_009032118.1.
DR AlphaFoldDB; T1EEI4; -.
DR STRING; 6412.T1EEI4; -.
DR EnsemblMetazoa; HelroT108353; HelroP108353; HelroG108353.
DR GeneID; 20194986; -.
DR KEGG; hro:HELRODRAFT_108353; -.
DR CTD; 20194986; -.
DR eggNOG; KOG2311; Eukaryota.
DR HOGENOM; CLU_007831_2_1_1; -.
DR InParanoid; T1EEI4; -.
DR OMA; CNPAMGG; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
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:UP000015101}.
FT DOMAIN 619..689
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 441..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 78113 MW; AF24D17FBCA9C314 CRC64;
MNNLTNLKLL IQLTFKRNYC KIISNNVNIS SLVFDKFKFD VVVVGGGHAG SEAAAASARM
GSSTALITHK WSTVGAMSCN PAFGGIGKGH LVREVDALDG LCARACDQSG VHYRVLNRKK
GPAVWGPRAQ IDRNLYRNFI QDELSKTPNL VCLEGSVEDL ILEEYEKDFN DGDSVKCSGV
VLANGQKIFS KTVVITTGTF LKGEILIGQE VWPAGRLNDD SSIGLADTFQ RLGIRLGRLK
TGTPPRLEKL SINFNKLLPS QPDNPPMPFS TMNERVWIEP DKQLKCYYTK TNEAIIDLIN
KNVHLNRMID RGTTGPRYCP SIESKVLKFP HLSHQIWIEP EGLNSDLVYP QGLSCTMPRD
VQHRIVQSIP GLEDAVIAVH GYGVEYDYVD ARQLKKTLEM KCLPHLFLAG QVNGTTGYEE
AAAQGLLAGI NASLTSKYLH VQEEHRTSAS QQPQRDKQHK RLQQQQQQHH QQEFVLGRYE
SYIGVMIDDL TTLGVSEPYR MLTSRAEFRI RLRQDNADLR LSGRGYEVGC VSEGRYKKFA
KTRDALHEWI ERTKEFIQPA SVWRREMNLN QLMNNHIPKS AFSLLSGSLG LDTLLRFYPE
NFKDLPHDEH LLARVKVEAL YDNATKDQLI EIERLKKDEG MKLPIGLDYH KLNISQEAKE
KLSFVRPETI ADASKIPGVT PAAVITLFRY VVKN
//
