NDUF7_DICDI
ID NDUF7_DICDI Reviewed; 484 AA.
AC Q54S83;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Mitochondrial dysfunction gene A {ECO:0000303|PubMed:16507593};
DE AltName: Full=NADH dehydrogenase [ubiquinone] complex I, assembly factor 7 homolog;
DE Flags: Precursor;
GN Name=midA {ECO:0000303|PubMed:16507593}; ORFNames=DDB_G0282615;
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16507593; DOI=10.1242/jcs.02819;
RA Torija P., Vicente J.J., Rodrigues T.B., Robles A., Cerdan S., Sastre L.,
RA Calvo R.M., Escalante R.;
RT "Functional genomics in Dictyostelium: midA, a new conserved protein, is
RT required for mitochondrial function and development.";
RL J. Cell Sci. 119:1154-1164(2006).
RN [3]
RP FUNCTION, INTERACTION WITH NDUFS2, SUBUNIT, AND MUTAGENESIS OF GLY-170.
RX PubMed=20406883; DOI=10.1242/jcs.066076;
RA Carilla-Latorre S., Gallardo M.E., Annesley S.J., Calvo-Garrido J.,
RA Grana O., Accari S.L., Smith P.K., Valencia A., Garesse R., Fisher P.R.,
RA Escalante R.;
RT "MidA is a putative methyltransferase that is required for mitochondrial
RT complex I function.";
RL J. Cell Sci. 123:1674-1683(2010).
CC -!- FUNCTION: Involved in the assembly or stability of mitochondrial
CC NADH:ubiquinone oxidoreductase complex (complex I) (PubMed:16507593,
CC PubMed:20406883). Acts as an arginine methyltransferase and probably
CC acts by mediating arginine methylation of ndufs2 (By similarity).
CC {ECO:0000250|UniProtKB:Q7L592, ECO:0000269|PubMed:16507593,
CC ECO:0000269|PubMed:20406883}.
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: Homodimer (PubMed:20406883). Interacts with ndufs2
CC (PubMed:20406883). {ECO:0000269|PubMed:20406883}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16507593}.
CC -!- DEVELOPMENTAL STAGE: High level of expression at the vegetative stage
CC and the first hours of development. {ECO:0000269|PubMed:16507593}.
CC -!- DISRUPTION PHENOTYPE: Cells show pleiotropic defects. Cell size, growth
CC rate, phagocytosis and macropinocytosis are affected. During
CC development, cells show an enhanced tendency to remain at the slug
CC stage, and spore viability are compromised.
CC {ECO:0000269|PubMed:16507593}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66167.1; -; Genomic_DNA.
DR RefSeq; XP_640156.1; XM_635064.1.
DR PDB; 5ZTZ; X-ray; 2.80 A; A/B/C=76-484.
DR PDB; 5ZU0; X-ray; 2.76 A; A/B/C=76-484.
DR PDB; 5ZZW; X-ray; 2.60 A; A/B/C=76-484.
DR PDBsum; 5ZTZ; -.
DR PDBsum; 5ZU0; -.
DR PDBsum; 5ZZW; -.
DR AlphaFoldDB; Q54S83; -.
DR SMR; Q54S83; -.
DR STRING; 44689.DDB0232140; -.
DR PaxDb; Q54S83; -.
DR EnsemblProtists; EAL66167; EAL66167; DDB_G0282615.
DR GeneID; 8623694; -.
DR KEGG; ddi:DDB_G0282615; -.
DR dictyBase; DDB_G0282615; midA.
DR eggNOG; KOG2901; Eukaryota.
DR HOGENOM; CLU_024840_3_2_1; -.
DR InParanoid; Q54S83; -.
DR OMA; YYHPQRN; -.
DR PhylomeDB; Q54S83; -.
DR Reactome; R-DDI-6799198; Complex I biogenesis.
DR PRO; PR:Q54S83; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006536; P:glutamate metabolic process; IMP:dictyBase.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:dictyBase.
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:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:dictyBase.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..484
FT /note="Protein arginine methyltransferase NDUFAF7 homolog,
FT mitochondrial"
FT /id="PRO_0000356854"
FT MUTAGEN 170
FT /note="G->V: Fails to complement the null phenotype."
FT /evidence="ECO:0000269|PubMed:20406883"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 345..356
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:5ZZW"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:5ZZW"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:5ZZW"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:5ZZW"
SQ SEQUENCE 484 AA; 55025 MW; 9EE62084AC1FFF2C CRC64;
MFRSITQRVI RNNCYKQSTK SITSSTSFIN NSLSYTTTSN ENDIKDKNEE HDHRAKGKGR
ELLLSFDKSG LAQFPKQVFK NRKYPITDFE KYLQDITKVR GPMSIDTFIK EVLTNPKYGY
YMNKDVFGKG GDFITAPEVS QLFGEMIGIW CVATWEAMGK PKKLQIVEMG PGRGTLMKDI
LRSTKVFKEF YDSISVHLVE ASPANKKTQK QNLLYFKDKA INFDHKTIGE TPNGIKVTWV
GKLEEVPTDI PTLFLAQEFF DALPIHVFRF SREKNDWCEV LVDEDITEHG EYYLRFVQSK
GPTLMTTAVK HLLPEFGLDG YQVELGLAGL AISQQIANRI DKSGGAALII DYGYDKIVKS
SLQAIRDHEF VDILDKPGTA DLSVWVDFQT IRKTVKLLKN KSTAIGPVDQ GIFLKEMGIE
HRLAQIGRKL DSNEKFEELV MGYKKLVDPK EMGTNYKVIT ICDKNITPIG FSTSKTYDDE
DLMI
