ID A0A158PB30_ANGCA Unreviewed; 586 AA.
AC A0A158PB30;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001033701-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0001033701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A158PB30; -.
DR STRING; 6313.A0A158PB30; -.
DR WBParaSite; ACAC_0001033701-mRNA-1; ACAC_0001033701-mRNA-1; ACAC_0001033701.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR Gene3D; 2.40.30.260; -; 1.
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; 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 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:UP000035642}.
FT DOMAIN 503..574
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 586 AA; 65012 MW; 48B6A85844BE3A65 CRC64;
LCSGGGHAGC EAASAAARCG ARTALLTHSR NTIGEMSCNP SFGGIGKGHL IRELDALDGV
CGRICDLSAI TYQALNRGQG PAVLGLRAQI DRLLYKSHMQ KEIFSTYNLE VIEGDVRAIS
TEIESDLRIS GVTLEDGRNL RSKAVVIATG TFLGGEIFVG NDRWSSGRIG EKSGTSLSKS
FRQLGFHIGR LRTGTPPRLV KDTIDLSKFQ LMPPDVVPIP FSFMTDEVWL LPSQQLPTYL
GYTNDRVREI VEENLADKQY IQGEVNGPRY CPSLESKVIR FPNLNHRVFL EHEGLESDLI
YPQGMSMTFS PDIQLKIMRS IKGLEKYGYG VHYDFVDPKQ LSPTLETKLV KGLFLAGQVN
GTTGYEEAAA QGVVAGINAA ARTREKEGMV IRRSQDNADM RLTELGRKWG SVGDARWSRF
LASKRAIDTL TSELKDIRMS LAKWSQVFPS YQWKNPAKVL SAYEMVHRHN VSLGEMKTAF
FDRLGHCIPN NFKNLEERIR CEGSYEAAHE RMKVKMQEID RESNTLIPDD IDYNSLPGLS
MECQEKLDSA RPLSLGAASR LPGVTPEAII TVLRYLKRPS KLSQSG
//
