ID A0A0N4WU04_HAEPC Unreviewed; 654 AA.
AC A0A0N4WU04;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN ORFNames=HPLM_LOCUS15093 {ECO:0000313|EMBL:VDO55358.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001510101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001510101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO55358.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO55358.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAF01018831; VDO55358.1; -; Genomic_DNA.
DR STRING; 6290.A0A0N4WU04; -.
DR WBParaSite; HPLM_0001510101-mRNA-1; HPLM_0001510101-mRNA-1; HPLM_0001510101.
DR OMA; CNPAMGG; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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 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:UP000268014}.
FT DOMAIN 571..642
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 654 AA; 72704 MW; BB38039040CC815B CRC64;
MFALHRSALQ PIYWSVIKSS VDRALATYTC FVGGGHAGCE GAAAAARCGA RTILLTHNKN
TIGEMSCNPS FGGIGKGHLI REVDALDGLC GRICDKSAIT YQALNSGQGP AVLGLRAQID
RSLYKAHMQK EISTTENLMV VEGGVDSLIV EDGNERRVTG VVLEDGSKLK TKTVLIATGT
FLGGEIFLGK KRWPAGRIGE KSATSLSQSF KELGFRLSRL RTGTPPRLWK NSIDFTQFQL
MPPDPVPIPF SFMTDQVWLP PEQQLPTYIG YTNDLVREIA EENIAENVHI KADARGPRYC
PSLEAKIIRF PQLHHRLFLE HEGLHSDLIY PQGMSMTFPP EIQLKIMRAI KGLEKVEIAQ
HGYGVQYDFV DPKQLLPTLE TKSVKGLFLA GQINGTTGYE EAAAQGVVAG INAAARVRGV
EGMVVRRSQG YVGVLIDDLT SLGTNEPYRM FTSRAEHRLH LRPDNADMRL TELGRKWGAV
RDVRWSRFID EKNAVDKATE ALRSIRMSIS KWSRVLPKLQ SKNLAKVLSA YEMLYRHNIS
LEVLKAALPD QLGHSLPDKL ENLEKRLKYE ASYEVAQERM KNKMKEIDQE SSSLIPEDID
YSKLQGLSAE CWEKLDRARP LNLAAASRVP GVKPEAIVAI LRYLKRNNIV SQSA
//