ID   NDUF5_PONAB             Reviewed;         345 AA.
AC   Q5RBS1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
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};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- SUBUNIT: Interacts with NDUFAF8, leading to stabilize NDUFAF5.
CC       Interacts with NDUFS7. {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; CR858563; CAH90789.1; -; mRNA.
DR   RefSeq; NP_001125447.1; NM_001131975.1.
DR   AlphaFoldDB; Q5RBS1; -.
DR   SMR; Q5RBS1; -.
DR   STRING; 9601.ENSPPYP00000011981; -.
DR   GeneID; 100172355; -.
DR   KEGG; pon:100172355; -.
DR   CTD; 79133; -.
DR   eggNOG; KOG2940; Eukaryota.
DR   InParanoid; Q5RBS1; -.
DR   OrthoDB; 691814at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
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..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..345
FT                   /note="Arginine-hydroxylase NDUFAF5, mitochondrial"
FT                   /id="PRO_0000307215"
SQ   SEQUENCE   345 AA;  38910 MW;  E1B6C5D52600D1CF CRC64;
     MLRPAGLWRL CRLSWAARVP AENLGRRDVT SGVSPRGSTS PRTLNIFDRD LKRKQKNWAA
     QQPEPTKFDY LKEEVGSRIA DRVYDIPRNF PLALDLGCGR GYIAQYLNKE TIGKFFQADI
     AENALKNSLE TEIPTVSVLA DEEFLPFREN TFDLVVSSLS LHWVNDLPRA LEQIHYILKP
     DGVFIGAMFG GDTLYELRCS LQLAETEREG GFSPHISPFT AVNDLGHLLG RAGFNTLTVD
     TDEIQVNYPG MFELMEDLQG MGESNCSWNR KALLHRDTML AAAAVYREMY RNEDGSVPAT
     YQIYYMIGWK YHESQARPAE RGSATVSFGE LGKINNLMPQ GNKSQ