NAA35_YEAST
ID NAA35_YEAST Reviewed; 733 AA.
AC Q02197; D3DLJ7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=N-alpha-acetyltransferase 35, NatC auxiliary subunit;
DE AltName: Full=Glucose repressible protein MAK10;
DE AltName: Full=L-A virus GAG protein N-acetyltransferase subunit MAK10;
DE AltName: Full=Maintenance of killer protein 10;
DE AltName: Full=N-terminal acetyltransferase C complex subunit MAK10;
DE Short=NatC complex subunit MAK10;
GN Name=MAK10; Synonyms=NAA35; OrderedLocusNames=YEL053C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1398065; DOI=10.1093/genetics/132.1.87;
RA Lee Y.-J., Wickner R.B.;
RT "MAK10, a glucose-repressible gene necessary for replication of a dsRNA
RT virus of Saccharomyces cerevisiae, has T cell receptor alpha-subunit
RT motifs.";
RL Genetics 132:87-96(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE NATC COMPLEX, AND FUNCTION OF THE NATC COMPLEX.
RX PubMed=11274203; DOI=10.1074/jbc.m011440200;
RA Polevoda B., Sherman F.;
RT "NatC Nalpha-terminal acetyltransferase of yeast contains three subunits,
RT Mak3p, Mak10p, and Mak31p.";
RL J. Biol. Chem. 276:20154-20159(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Component of the NatC N-terminal acetyltransferase, which
CC catalyzes acetylation of the N-terminus Met of L-A virus Gag protein.
CC MAK10 has a role in the propagation of L-A and M viruses, perhaps in
CC the viral assembly. It is apparently directly needed for optimum
CC respiration. {ECO:0000269|PubMed:11274203}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC complex, which is composed of MAK3, MAK10 and MAK31.
CC {ECO:0000269|PubMed:11274203}.
CC -!- INTERACTION:
CC Q02197; Q03503: MAK3; NbExp=3; IntAct=EBI-10924, EBI-10388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Glucose-repressed.
CC -!- MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MAK10 family. {ECO:0000305}.
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DR EMBL; M94533; AAA34749.1; -; Genomic_RNA.
DR EMBL; U18779; AAB64989.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07601.1; -; Genomic_DNA.
DR PIR; S31288; S31288.
DR RefSeq; NP_010861.3; NM_001178868.3.
DR PDB; 6YGA; X-ray; 2.40 A; B=1-733.
DR PDB; 6YGB; X-ray; 2.45 A; B=1-733.
DR PDB; 6YGC; X-ray; 2.99 A; B=1-733.
DR PDB; 6YGD; X-ray; 2.75 A; B=1-733.
DR PDBsum; 6YGA; -.
DR PDBsum; 6YGB; -.
DR PDBsum; 6YGC; -.
DR PDBsum; 6YGD; -.
DR AlphaFoldDB; Q02197; -.
DR SMR; Q02197; -.
DR BioGRID; 36676; 76.
DR ComplexPortal; CPX-781; NatC N-alpha-acetyltransferase complex.
DR DIP; DIP-1428N; -.
DR IntAct; Q02197; 4.
DR MINT; Q02197; -.
DR STRING; 4932.YEL053C; -.
DR MaxQB; Q02197; -.
DR PaxDb; Q02197; -.
DR PRIDE; Q02197; -.
DR EnsemblFungi; YEL053C_mRNA; YEL053C; YEL053C.
DR GeneID; 856657; -.
DR KEGG; sce:YEL053C; -.
DR SGD; S000000779; MAK10.
DR VEuPathDB; FungiDB:YEL053C; -.
DR eggNOG; KOG2343; Eukaryota.
DR GeneTree; ENSGT00390000002445; -.
DR HOGENOM; CLU_022669_1_0_1; -.
DR InParanoid; Q02197; -.
DR OMA; NTCRYRQ; -.
DR BioCyc; YEAST:G3O-30171-MON; -.
DR PRO; PR:Q02197; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; Q02197; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031417; C:NatC complex; IDA:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IEA:InterPro.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:SGD.
DR InterPro; IPR007244; Naa35/Mak10.
DR PANTHER; PTHR21373; PTHR21373; 1.
DR Pfam; PF04112; Mak10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..733
FT /note="N-alpha-acetyltransferase 35, NatC auxiliary
FT subunit"
FT /id="PRO_0000084553"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 83..102
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 145..165
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6YGD"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6YGB"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6YGB"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 384..400
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 404..427
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 431..454
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 463..504
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 509..524
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 526..562
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 579..586
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 594..597
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 617..651
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 666..699
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:6YGD"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 722..727
FT /evidence="ECO:0007829|PDB:6YGA"
SQ SEQUENCE 733 AA; 84302 MW; 11148C1FC6BB0931 CRC64;
MEVDSILGSL SITDDFDQLV DVTSLFDELC SKLKPEAIVK DPRFDLFEGT HSLEVNNSKL
DSSLIELTAE EIEFDVNVAY DPPLASVAAI ADRLLRCVIS WLNDYQTLPT TVLSCRYTES
LLSSLVKGTT AGSSWCTGNI LYDKVLGSCI LGVCYLTKFV QKLLSAGIVF EEEDLNFNNM
GFNTFDNLPG QDVVINSLTE SLQILEAYSD DSLHLTMLKH ILKIIICLVH LEDHLTDYST
KTSHLDELIE NANSVNGIFP QLQLSPPKGA FSTYIQKHRS NQFPPRKITK LPTDYSGFIT
LANDVKTILL VDKAESALET YQFAKFFNKL EQRHVIARIL FPLFFIRDDR TVLGKFSYTQ
FYLLHVKEFS AQTPSEFESS IGNELIQESS NMLLEWYQNC SQNTCRYRQG FNRQLILWDS
LQAQFESVNS QVYCSWTYFM KLSSMIEFSL KGFDLDIYKP FEAYSMFWYV YYLSHHLETF
LKDSQNDIES NINAIHSMNK KLKKLKAGEK KDQLRLKYRF AMDNEMEQLQ ATKQFLNYLL
KEINITKSLC LIEVFQFAIL KSFGLIDNKN STPSKFSNER LIHNLRFKPF NSIGVPELPE
YEVFQQTLKD FVIEEKGAAF DIKLERATNF IETEVRNVVS SIDEIMQGIK GGDNNGVLVT
GTRLVQELSL EYYCKLKHTS KALSVNSKVI VNTLKKNIKN KDSHEYKVEL VHTTEGWNYF
PIQTLRIKQD RYK
