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NDUF5_DICDI
ID   NDUF5_DICDI             Reviewed;         436 AA.
AC   Q54JW0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Arginine-hydroxylase NDUFAF5, mitochondrial;
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:Q5TEU4};
DE   AltName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 5 {ECO:0000250|UniProtKB:Q5TEU4};
DE   AltName: Full=Putative methyltransferase NDUFAF5 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ndufaf5 {ECO:0000303|PubMed:23536703}; ORFNames=DDB_G0287769;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   GLY-86; LEU-165 AND LEU-235.
RX   PubMed=23536703; DOI=10.1091/mbc.e12-11-0796;
RA   Carilla-Latorre S., Annesley S.J., Munoz-Braceras S., Fisher P.R.,
RA   Escalante R.;
RT   "Ndufaf5 deficiency in the Dictyostelium model: new roles in autophagy and
RT   development.";
RL   Mol. Biol. Cell 24:1519-1528(2013).
CC   -!- FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone
CC       oxidoreductase complex (complex I, MT-ND1) at early stages
CC       (PubMed:23536703). Probably acts as an arginine hydroxylase (By
CC       similarity). May also have methyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q5TEU4, ECO:0000269|PubMed:23536703}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23536703}.
CC   -!- DISRUPTION PHENOTYPE: Defects in development due to mitochondrial
CC       NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) deficiency
CC       (PubMed:23536703). Increased autophagy (PubMed:23536703).
CC       {ECO:0000269|PubMed:23536703}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000104; EAL63531.1; -; Genomic_DNA.
DR   RefSeq; XP_637042.1; XM_631950.1.
DR   AlphaFoldDB; Q54JW0; -.
DR   SMR; Q54JW0; -.
DR   STRING; 44689.DDB0187624; -.
DR   PaxDb; Q54JW0; -.
DR   EnsemblProtists; EAL63531; EAL63531; DDB_G0287769.
DR   GeneID; 8626296; -.
DR   KEGG; ddi:DDB_G0287769; -.
DR   dictyBase; DDB_G0287769; ndufaf5.
DR   eggNOG; KOG2940; Eukaryota.
DR   HOGENOM; CLU_046586_0_0_1; -.
DR   InParanoid; Q54JW0; -.
DR   OMA; QNMGENN; -.
DR   PhylomeDB; Q54JW0; -.
DR   PRO; PR:Q54JW0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:dictyBase.
DR   GO; GO:0010507; P:negative regulation of autophagy; IMP:dictyBase.
DR   GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..436
FT                   /note="Arginine-hydroxylase NDUFAF5, mitochondrial"
FT                   /id="PRO_0000356856"
FT   REGION          365..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         86
FT                   /note="G->V: Unable to complement a ndufaf5 mutant strain."
FT                   /evidence="ECO:0000269|PubMed:23536703"
FT   MUTAGEN         165
FT                   /note="L->F: Unable to complement a ndufaf5 mutant strain."
FT                   /evidence="ECO:0000269|PubMed:23536703"
FT   MUTAGEN         235
FT                   /note="L->P: Unable to complement a ndufaf5 mutant strain."
FT                   /evidence="ECO:0000269|PubMed:23536703"
SQ   SEQUENCE   436 AA;  50194 MW;  21C4C38D2297863A CRC64;
     MLRTTFRKGF NLKCFSKDWN QTRQYSNYTK MTIFDTNVKT IQKNNTVTNV DDPKHYDYLM
     NEVADRLADR ILDIKDIKCG NVLDFGSRNG ALFKYIQEKG AKIDKYYMVE SSKELLYRDD
     NNVSQENEDD NNNNKVKPTK ILVNSLEDKI EGIEDQSLDL IISNLSLHWV NDLPGVFGGL
     KRLLKPNGVF LASLFGEDTL MELKDSLYLA EIEREGGFSP HVSPFTKISD IGNILSKNRY
     TLPTVDTEKI TINYDNMFVL MRDLQNMGEN NAILKRRNYT SKDTFLAASA IYKHLYGNED
     NNSIPATFQI IYLIGWAPHE SQQKPLQRGS AKKHFSEISG TSSFGYKFDN DSSIPSILTN
     ENNSVTLSQQ QQQQGIEPQQ SNDDSINEPF PKTDDFVIKR LDYHGNFHFE KQQQQQQQQD
     QNKESSDEIN KNKDDK
 
 
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