ID   NDUF7_XENLA             Reviewed;         437 AA.
AC   Q6GQ37;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
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};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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; BC072911; AAH72911.1; -; mRNA.
DR   RefSeq; NP_001085543.1; NM_001092074.1.
DR   AlphaFoldDB; Q6GQ37; -.
DR   SMR; Q6GQ37; -.
DR   MaxQB; Q6GQ37; -.
DR   DNASU; 443969; -.
DR   GeneID; 443969; -.
DR   KEGG; xla:443969; -.
DR   CTD; 443969; -.
DR   Xenbase; XB-GENE-996605; ndufaf7.S.
DR   OMA; YYHPQRN; -.
DR   OrthoDB; 491869at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 443969; Expressed in egg cell and 19 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..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..437
FT                   /note="Protein arginine methyltransferase NDUFAF7,
FT                   mitochondrial"
FT                   /id="PRO_0000315676"
SQ   SEQUENCE   437 AA;  49031 MW;  84EF82718493063B CRC64;
     MSGLARLQRL QKFGFLMVSA SANRPIQRYQ CSRTEKPQKR TSANALLNHL IFKIKSTGPI
     TVSEYMREVL TNPVKGYYMH NDMLGEHGDF VTSPEISQIF GELLGVWCIS EWVSAGKPKA
     IQLVELGPGR GTLTDDLLRV FSNFGRLLDS CDISVHLVEV SPKLSDIQAQ RLTGKSIEVE
     LDSNSPVYKN GITKTGRPVC WYQDIQDVPN GYSFYIAHEF FDALPIHKLQ KIKDGWREML
     IDIDPKLPDK LRFVLGSNMS LVAKTFVQDD EPRDHVEVCP SAAVIIQKLA QQINSYGGAA
     LIADYGHMGE KTDTFRGFRA HQLHDVLTDP GTADLTADVD FNFMRRMVGE AASCLGPVTQ
     HVFLKNMGID IRLKVLLEKS NDVTVQKQLI HGYNVLMNPD QMGQRFKFFS VVPHSRLKNT
     LKTKMPPVAG FSTLLMT