ID   NDUF7_DANRE             Reviewed;         422 AA.
AC   Q08BY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=zgc:153989 {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].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24838397; DOI=10.1093/hmg/ddu239;
RA   Zurita Rendon O., Silva Neiva L., Sasarman F., Shoubridge E.A.;
RT   "The arginine methyltransferase NDUFAF7 is essential for complex I assembly
RT   and early vertebrate embryogenesis.";
RL   Hum. Mol. Genet. 23:5159-5170(2014).
CC   -!- FUNCTION: Arginine methyltransferase involved in the assembly or
CC       stability of mitochondrial NADH:ubiquinone oxidoreductase complex
CC       (complex I) (PubMed:24838397). Acts by mediating symmetric
CC       dimethylation of 'Arg-118' of ndufs2 after it assembles into the
CC       complex I, stabilizing the early intermediate complex.
CC       {ECO:0000250|UniProtKB:Q7L592, ECO:0000269|PubMed:24838397}.
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   -!- DISRUPTION PHENOTYPE: Impaired NADH:ubiquinone oxidoreductase complex
CC       (complex I) assembly. {ECO:0000269|PubMed:24838397}.
CC   -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
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DR   EMBL; BC124508; AAI24509.1; -; mRNA.
DR   RefSeq; NP_001070231.1; NM_001076763.1.
DR   AlphaFoldDB; Q08BY0; -.
DR   SMR; Q08BY0; -.
DR   STRING; 7955.ENSDARP00000067396; -.
DR   PaxDb; Q08BY0; -.
DR   Ensembl; ENSDART00000067397; ENSDARP00000067396; ENSDARG00000033134.
DR   GeneID; 767796; -.
DR   KEGG; dre:767796; -.
DR   CTD; 55471; -.
DR   ZFIN; ZDB-GENE-060929-628; ndufaf7.
DR   eggNOG; KOG2901; Eukaryota.
DR   GeneTree; ENSGT00390000001588; -.
DR   HOGENOM; CLU_024840_3_1_1; -.
DR   InParanoid; Q08BY0; -.
DR   OMA; YYHPQRN; -.
DR   OrthoDB; 491869at2759; -.
DR   PhylomeDB; Q08BY0; -.
DR   TreeFam; TF314312; -.
DR   Reactome; R-DRE-6799198; Complex I biogenesis.
DR   PRO; PR:Q08BY0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000033134; Expressed in gastrula and 20 other tissues.
DR   ExpressionAtlas; Q08BY0; baseline.
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:0043009; P:chordate embryonic development; IMP:ZFIN.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP: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..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..422
FT                   /note="Protein arginine methyltransferase NDUFAF7,
FT                   mitochondrial"
FT                   /id="PRO_0000315675"
SQ   SEQUENCE   422 AA;  46928 MW;  E12545C86EDACACE CRC64;
     MRTLLRLKRL MPEVLWTKRS CSSSSINKSI LKHLASKIIA TGPISVAEYM REALTNPVLG
     YYVKNDMLGA GGDFITSPEI SQIFGELLGV WCISEWMAAG KSSALQLVEL GPGRGSLTSD
     ILRVFSQLKG VLGETGISIH LVEVSPKLSQ VQAECLTGNQ TQTYDNNHTF YRSGTTCTGL
     PIYWYHSIED VPRGFSIFLA HEFFDALPIH KFQRTENGWR EVLVDIDPEN PGKLRFVVSH
     RPTLASSTLI QKDESRRHVE VCAEAGVIVQ KLASRIAEDG GAALIVDYGH DGTKTDTFRG
     FKGHQIHDVL EAPGLADLTA DVDFSYLRKM AGDQVICLGP ITQRSFLKNM GIDSRMQVLL
     SSNDPSIRAQ LIHSYDMLIN PEKMGERFQF FSVLNTARLA QREQMQKSTV MPVAGFTELE
     MQ