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NDUF7_DROME
ID   NDUF7_DROME             Reviewed;         437 AA.
AC   Q9VGR2; Q6NLJ4; Q8MYZ3; Q95S80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=CG17726;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-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). {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAM29473.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014297; AAF54614.1; -; Genomic_DNA.
DR   EMBL; AY060921; AAL28469.1; ALT_INIT; mRNA.
DR   EMBL; AY113468; AAM29473.1; ALT_SEQ; mRNA.
DR   EMBL; BT012337; AAS77462.1; -; mRNA.
DR   RefSeq; NP_650054.2; NM_141797.4.
DR   AlphaFoldDB; Q9VGR2; -.
DR   SMR; Q9VGR2; -.
DR   BioGRID; 66483; 2.
DR   IntAct; Q9VGR2; 2.
DR   STRING; 7227.FBpp0081828; -.
DR   PaxDb; Q9VGR2; -.
DR   PRIDE; Q9VGR2; -.
DR   DNASU; 41349; -.
DR   EnsemblMetazoa; FBtr0082352; FBpp0081828; FBgn0037880.
DR   GeneID; 41349; -.
DR   KEGG; dme:Dmel_CG17726; -.
DR   UCSC; CG17726-RA; d. melanogaster.
DR   FlyBase; FBgn0037880; CG17726.
DR   VEuPathDB; VectorBase:FBgn0037880; -.
DR   eggNOG; KOG2901; Eukaryota.
DR   GeneTree; ENSGT00390000001588; -.
DR   HOGENOM; CLU_024840_3_1_1; -.
DR   InParanoid; Q9VGR2; -.
DR   OMA; YYHPQRN; -.
DR   OrthoDB; 491869at2759; -.
DR   PhylomeDB; Q9VGR2; -.
DR   Reactome; R-DME-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 41349; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 41349; -.
DR   PRO; PR:Q9VGR2; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037880; Expressed in secondary oocyte and 19 other tissues.
DR   ExpressionAtlas; Q9VGR2; baseline and differential.
DR   Genevisible; Q9VGR2; DM.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; 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.
FT   CHAIN           1..437
FT                   /note="Protein arginine methyltransferase NDUFAF7 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000315679"
FT   REGION          21..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        275
FT                   /note="L -> P (in Ref. 4; AAS77462)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="T -> P (in Ref. 4; AAS77462)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="K -> E (in Ref. 4; AAS77462)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="S -> R (in Ref. 4; AAS77462)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   437 AA;  49068 MW;  0CBBB79AB1638CEB CRC64;
     MLREALRIGN RRWYSYKSVR RPNLGATGTP KMEPPKEQPE ASSKAESGHG SLAKQLRAKI
     LSTGPIPVAE YMREVLTNPQ AGYYMNRDVF GREGDFITSP EISQIFGELV GIWLVSEWRK
     MGSPSPFQLV ELGPGRGTLA RDVLKVLTKF KQDAEFSMHM VEVSPFLSKA QAQRFCYSHQ
     TLPEDAQLPH YQEGTTASGT KAFWHRRLED VPQGFSLVLA HEFFDALPVH KLQLVDGKWQ
     EVLIDVASSD GAQEASFRYV LSRSQTPVSS LYRPLPGETR SCLEHSLETE RQVGLLAERI
     ERDGGIALIM DYGHFGEKTD TFRAFKQHKL HDPLVEPGSA DLTADVDFKL VRHIAETRGN
     VHCCGPVEQG LFLQRMQGEA RLEQLLAHAL PENQEIIRSG YEMLTDPAQM GTRFKFLAMF
     PGVLAAHLDK YPVVGFS
 
 
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