NDUF5_DANRE
ID NDUF5_DANRE Reviewed; 321 AA.
AC A3KP37;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Arginine-hydroxylase NDUFAF5, mitochondrial;
DE EC=1.-.-.- {ECO:0000250|UniProtKB:Q5TEU4};
DE AltName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 5 {ECO:0000250|UniProtKB:Q5TEU4};
DE AltName: Full=Putative methyltransferase NDUFAF5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ndufaf5 {ECO:0000250|UniProtKB:Q5TEU4};
GN ORFNames=zgc:162919 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Arginine hydroxylase involved in the assembly of
CC mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-
CC ND1) at early stages. Acts by mediating hydroxylation of 'Arg-111' of
CC ndufs7. May also have methyltransferase activity.
CC {ECO:0000250|UniProtKB:Q5TEU4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q5TEU4}. Note=Peripherally localized on the
CC matrix face of the mitochondrial inner membrane.
CC {ECO:0000250|UniProtKB:Q5TEU4}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; BC134146; AAI34147.1; -; mRNA.
DR RefSeq; NP_001076363.1; NM_001082894.1.
DR AlphaFoldDB; A3KP37; -.
DR SMR; A3KP37; -.
DR STRING; 7955.ENSDARP00000113500; -.
DR PaxDb; A3KP37; -.
DR PeptideAtlas; A3KP37; -.
DR GeneID; 794020; -.
DR KEGG; dre:794020; -.
DR CTD; 79133; -.
DR ZFIN; ZDB-GENE-070410-110; ndufaf5.
DR eggNOG; KOG2940; Eukaryota.
DR InParanoid; A3KP37; -.
DR OrthoDB; 691814at2759; -.
DR Reactome; R-DRE-6799198; Complex I biogenesis.
DR PRO; PR:A3KP37; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0030961; P:peptidyl-arginine hydroxylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..321
FT /note="Arginine-hydroxylase NDUFAF5, mitochondrial"
FT /id="PRO_0000307216"
SQ SEQUENCE 321 AA; 35928 MW; CA05999618747305 CRC64;
MNVSVKSLRG VSRTWRSFSS RQGMNVFDRS MKRRQKDWAS SLLDSSKYDY LREEVGSRVA
DRVYDVARTF PLALDVGCGR SHIAEHLSKE VVERLFLTDI SSSSLRNRKT SDIPAQCVMA
DEEFLPFKEN TFDLVLSSLS MHWINDLPGA LRQIHQVLKP DGVFIGAMVG GETLYELRCS
LQLAELEREG GFAPHISPYT AVTDLGNLLG QAGFNMLTVD IDEVQVNYPG MLEVMRDLQG
MGESNCAWNR KLLLQRDTML AAAAIYKEMY GNEDGSVPAT FQILYMIGWK PHDSQAKPAK
RGSANVSFAD LSKIGKLQSD Q