NDUF7_RAT
ID NDUF7_RAT Reviewed; 436 AA.
AC Q5XI79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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:0000312|RGD:1311578};
DE AltName: Full=Protein midA homolog {ECO:0000250|UniProtKB:Q7L592};
DE Flags: Precursor;
GN Name=Ndufaf7 {ECO:0000312|RGD:1311578};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
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DR EMBL; BC083810; AAH83810.1; -; mRNA.
DR RefSeq; NP_001008319.1; NM_001008318.1.
DR AlphaFoldDB; Q5XI79; -.
DR SMR; Q5XI79; -.
DR STRING; 10116.ENSRNOP00000007000; -.
DR PaxDb; Q5XI79; -.
DR PRIDE; Q5XI79; -.
DR GeneID; 298748; -.
DR KEGG; rno:298748; -.
DR UCSC; RGD:1311578; rat.
DR CTD; 55471; -.
DR RGD; 1311578; Ndufaf7.
DR VEuPathDB; HostDB:ENSRNOG00000005279; -.
DR eggNOG; KOG2901; Eukaryota.
DR HOGENOM; CLU_024840_3_1_1; -.
DR InParanoid; Q5XI79; -.
DR OMA; YYHPQRN; -.
DR OrthoDB; 491869at2759; -.
DR PhylomeDB; Q5XI79; -.
DR TreeFam; TF314312; -.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR PRO; PR:Q5XI79; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005279; Expressed in heart and 20 other tissues.
DR Genevisible; Q5XI79; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
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..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..436
FT /note="Protein arginine methyltransferase NDUFAF7,
FT mitochondrial"
FT /id="PRO_0000315674"
FT REGION 413..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 48716 MW; DD9703759B4D454C CRC64;
MNALVRRCVA RTGIPSIWRR KCFSSGNEPA ESNHVTPMLR HLMYKIKSTG PITVAEYMKE
VLTNPAKGYY VHHDMLGEKG DFITSPEISQ IFGELLGVWF VSEWMASGKS TAFQLVELGP
GRGTLTADIL RVFSQLGSVL KTCDISIHLV EVSQKLSEIQ ALTLTEETVP LERDAESLVY
MKGVTKSGIP ISWYRDLKDV PTGYSFYLAH EFFDVLPVHK FQKTPHGWRE VFVDIDPQSP
DKLRFVLAPC ATPAEAFIQR DERREHVEVC PDAGVVIQEL SQRIASTGGA ALIADYGHDG
TKTDTLRGFY EHQLHDVLTA PGTADLTADV DFSYLRRMAQ GRVASLGPVE QRTFLKNMGI
DVRLKVLLDK AGDPSLQQQL LRGYDMLMNP QKMGERFHFF ALLPHQRLHV GSQGGKACQS
EAPSTSVPGF DELVWH