ID   NDUF7_BOVIN             Reviewed;         441 AA.
AC   Q2KHV5; A6QQB0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 72.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 167-441 (ISOFORM 1).
RC   STRAIN=Hereford; TISSUE=Heart ventricle, and Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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   -!- SUBUNIT: Interacts with NDUFS2. {ECO:0000250|UniProtKB:Q7L592}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7L592}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2KHV5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2KHV5-2; Sequence=VSP_030603, VSP_030604;
CC   -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI49743.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AAFC03083630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC112868; AAI12869.1; -; mRNA.
DR   EMBL; BC149742; AAI49743.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001094519.2; NM_001101049.2.
DR   AlphaFoldDB; Q2KHV5; -.
DR   SMR; Q2KHV5; -.
DR   STRING; 9913.ENSBTAP00000001470; -.
DR   PaxDb; Q2KHV5; -.
DR   PRIDE; Q2KHV5; -.
DR   GeneID; 504290; -.
DR   KEGG; bta:504290; -.
DR   CTD; 55471; -.
DR   eggNOG; KOG2901; Eukaryota.
DR   InParanoid; Q2KHV5; -.
DR   OrthoDB; 491869at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..441
FT                   /note="Protein arginine methyltransferase NDUFAF7,
FT                   mitochondrial"
FT                   /id="PRO_0000315671"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         138..144
FT                   /note="FSQLGSL -> SNKVSCT (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_030603"
FT   VAR_SEQ         145..441
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_030604"
SQ   SEQUENCE   441 AA;  49265 MW;  9E133A75FADE6FA8 CRC64;
     MNFLAAAGVR RLCAMRAVLP CLWRGKYFSS GNEPAENNTV TPMLRHLIYK IKSTGPITVA
     EYMKEVLTNP AKGYYMNRDM LGEEGDFITS PEISQMFGEL LGIWFISEWI AAGKNAAFQL
     VELGPGKGTL LGDILRVFSQ LGSLLKNCDI SLHLVEVSQK LSEIQALTLT EEKVPLERNA
     ESPVYMKGVT KSGIPVSWYR DLQDVPKEYS FYLAHEFFDV LPVHKFQKTP HGWREVLVDI
     DPQVSDKLRF VLAPCATPAG AFIQNDETRD HVEVCPEAGV VIQELSQRIS LTGGAALIAD
     YGHDGTKTDT FRGFCGYRLH DVLTAPGTAD LTADVDFSYL RRMSQGKVAS LGPVEQQTFL
     RNMGIDVRLK ILLDKTDDPS LRQQLLQGYN MLMNPMKMGE RFNFLALVPH QRLHGRNHQT
     NARQSKPSPS PVAGFGELAW Q