NDUF7_SCHPO
ID NDUF7_SCHPO Reviewed; 467 AA.
AC O14138; Q9UTB7;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein arginine methyltransferase NDUFAF7 homolog, 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 homolog;
DE AltName: Full=Protein midA homolog;
GN ORFNames=SPAC25A8.03c, SPAC3C7.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Arginine methyltransferase involved in the assembly or
CC stability of mitochondrial NADH:ubiquinone oxidoreductase complex
CC (complex I). {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:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB16745.1; -; Genomic_DNA.
DR RefSeq; NP_593616.2; NM_001019047.2.
DR AlphaFoldDB; O14138; -.
DR STRING; 4896.SPAC25A8.03c.1; -.
DR PaxDb; O14138; -.
DR EnsemblFungi; SPAC25A8.03c.1; SPAC25A8.03c.1:pep; SPAC25A8.03c.
DR GeneID; 2543202; -.
DR KEGG; spo:SPAC25A8.03c; -.
DR PomBase; SPAC25A8.03c; -.
DR VEuPathDB; FungiDB:SPAC25A8.03c; -.
DR eggNOG; ENOG502QRKD; Eukaryota.
DR HOGENOM; CLU_585470_0_0_1; -.
DR InParanoid; O14138; -.
DR PhylomeDB; O14138; -.
DR PRO; PR:O14138; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..467
FT /note="Protein arginine methyltransferase NDUFAF7 homolog,
FT mitochondrial"
FT /id="PRO_0000116736"
SQ SEQUENCE 467 AA; 54568 MW; FAC7AB545004ED2C CRC64;
MLNLYMWKLS RSQVYQASLL FGSRVISALA FTNTGLVLHG PRRWYTTDNG FLLHRDSKVS
LADYIHESTF DPSKGYYSRL WTGSTNNLSH SVHVLRKEGH KCSKEFDPFL HGIPIPQKAL
NIYEKQRSLF SESISNYLVL QYKLRYFPVF DLKIYDFHSG TGIIALDILD YLYKNHLEVY
GRTTYNIVLH NSWQASWFKS MLTSVRYAKH GDHIDIYVSD PLTWNHTDTN PCFVLALQVI
SSFGHDLFRQ SNGAMMMERC WLGPEHFLNE FFTLNTHQKV SSLNYHLAFQ QARINVQQGF
SDSRAKRYFS GVKQVFWSFF STQKLTYYPT KAIRFFERLS KQFPHHSLLL MDVCHVDKSL
PGINAPSVLS MENDFSTKKM SSNIGHVFQN ETVKYVFPTP LYLVSDILQL ATHNRSFICS
LPHFLRRWSN EHGRKFFVPV EPSSKNLKVP YSFNNYYVVS SMPTYYY
