ID   NDUF7_XENTR             Reviewed;         430 AA.
AC   Q5BKM6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Protein arginine methyltransferase NDUFAF7, mitochondrial {ECO:0000250|UniProtKB:Q7L592};
DE            EC=2.1.1.320 {ECO:0000250|UniProtKB:Q7L592};
DE   AltName: Full=NADH dehydrogenase [ubiquinone] complex I, assembly factor 7 {ECO:0000250|UniProtKB:Q7L592};
DE   AltName: Full=Protein midA homolog {ECO:0000250|UniProtKB:Q7L592};
DE   Flags: Precursor;
GN   Name=ndufaf7 {ECO:0000250|UniProtKB:Q7L592};
GN   ORFNames=TEgg135j01.1 {ECO:0000303|Ref.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Arginine methyltransferase involved in the assembly or
CC       stability of mitochondrial NADH:ubiquinone oxidoreductase complex
CC       (complex I). Acts by mediating symmetric dimethylation of 'Arg-118' of
CC       ndufs2 after it assembles into the complex I, stabilizing the early
CC       intermediate complex. {ECO:0000250|UniProtKB:Q7L592}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC         Evidence={ECO:0000250|UniProtKB:Q7L592};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7L592}.
CC   -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
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DR   EMBL; CR761995; CAJ81481.1; -; mRNA.
DR   EMBL; BC091018; AAH91018.1; -; mRNA.
DR   RefSeq; NP_001016145.1; NM_001016145.2.
DR   AlphaFoldDB; Q5BKM6; -.
DR   SMR; Q5BKM6; -.
DR   STRING; 8364.ENSXETP00000001432; -.
DR   DNASU; 548899; -.
DR   GeneID; 548899; -.
DR   KEGG; xtr:548899; -.
DR   CTD; 55471; -.
DR   Xenbase; XB-GENE-996599; ndufaf7.
DR   eggNOG; KOG2901; Eukaryota.
DR   InParanoid; Q5BKM6; -.
DR   OrthoDB; 491869at2759; -.
DR   Reactome; R-XTR-6799198; Complex I biogenesis.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000653; Expressed in egg cell and 13 other tissues.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0019918; P:peptidyl-arginine methylation, to symmetrical-dimethyl arginine; ISS:UniProtKB.
DR   Gene3D; 3.40.50.12710; -; 1.
DR   InterPro; IPR003788; NDUFAF7.
DR   InterPro; IPR038375; NDUFAF7_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12049; PTHR12049; 1.
DR   Pfam; PF02636; Methyltransf_28; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..430
FT                   /note="Protein arginine methyltransferase NDUFAF7,
FT                   mitochondrial"
FT                   /id="PRO_0000315677"
SQ   SEQUENCE   430 AA;  48023 MW;  87DA980BBE00ADE3 CRC64;
     MSGLARLRKT AFLMVSASAN CRIQRYQSSR TEKHQDSTSA NALLNHLIFK IKSTGPITVS
     EYMREVLTNP VKGYYMHHDM LGEHGDFVTS PELSQIFGEL LGVWCISEWM SAGKPKSLQL
     VELGPGRGTL TDDLLRVFSN FGRLLNSCDI SVHLVEVSPK LSDIQAQRLT GKAIEVELDK
     NSPVYKKGIT KTGFPVCWYQ DIQDVPTGFS FYIAHEFFDA LPIHKLQKTK DGWREILIDI
     DPGIPDKLRF VLGPNVSLVA NTFVQDDEPR DHVEVCPSAA VIIQKLANQI NSYGGAALIA
     DYGHMGERTD TFRGFRAHKL HDVLSNPGTA DLTADVDFNF MRRIVGEAAS CLGPVTQHEF
     LKNMGIDIRL KVLLEKSSDV AVQKQLIHGY NILMNADQMG QRFKFFSVVP QSRLKTTMPP
     VAGFSKLLMH