NAA35_SCHPO
ID NAA35_SCHPO Reviewed; 708 AA.
AC Q9USY3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=N-alpha-acetyltransferase 35, NatC auxiliary subunit;
DE AltName: Full=N-terminal acetyltransferase C complex subunit mak10;
DE Short=NatC complex subunit mak10;
GN Name=mak10; Synonyms=naa35; ORFNames=SPBC1861.03;
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: Component of the NatC N-terminal acetyltransferase.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the MAK10 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52739.1; -; Genomic_DNA.
DR PIR; T39742; T39742.
DR RefSeq; NP_596720.1; NM_001022645.2.
DR PDB; 7L1K; EM; 3.16 A; B=1-708.
DR PDBsum; 7L1K; -.
DR AlphaFoldDB; Q9USY3; -.
DR SMR; Q9USY3; -.
DR BioGRID; 276244; 52.
DR STRING; 4896.SPBC1861.03.1; -.
DR MaxQB; Q9USY3; -.
DR PaxDb; Q9USY3; -.
DR EnsemblFungi; SPBC1861.03.1; SPBC1861.03.1:pep; SPBC1861.03.
DR GeneID; 2539689; -.
DR KEGG; spo:SPBC1861.03; -.
DR PomBase; SPBC1861.03; mak10.
DR VEuPathDB; FungiDB:SPBC1861.03; -.
DR eggNOG; KOG2343; Eukaryota.
DR HOGENOM; CLU_011757_0_0_1; -.
DR InParanoid; Q9USY3; -.
DR OMA; NTCRYRQ; -.
DR PhylomeDB; Q9USY3; -.
DR PRO; PR:Q9USY3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031417; C:NatC complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IEA:InterPro.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; ISO:PomBase.
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; Nucleus; Reference proteome.
FT CHAIN 1..708
FT /note="N-alpha-acetyltransferase 35, NatC auxiliary
FT subunit"
FT /id="PRO_0000316239"
FT TURN 42..47
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 112..116
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 154..158
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 218..223
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 417..436
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 453..461
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 462..466
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 482..502
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 511..532
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 543..560
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 585..595
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 610..621
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 625..647
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 673..678
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 681..686
FT /evidence="ECO:0007829|PDB:7L1K"
SQ SEQUENCE 708 AA; 80456 MW; 05C89FC570F39C4F CRC64;
MSVKESLSLL NSMQGNVKIG NVEPAKGNEG YVDNAGYVDC TKSYFEATKS LKEEQLVCDP
KFTLLDSISA FEIMEPKMDS GIDYQPLRVD FSRDLSYLEI LALMDLIVSA EKEWHYGSPL
SESLLCSAHV FSICKSPISQ VGDSGFSSGS GRNTTDIVLF PFVLAVIKCC DIVHREFLMG
NLYDEEDISS FSYHMSFLQN YPIEKLNYLL QSSIEYLASE VIKFSAELRQ IIEGILNRIQ
LRIGILRVYE RSDIKTTIDA LHLIKNLVPE IQNTVSVVDS SIKESILKQY WDFRVQAQLV
ATAPVRNIPP TGIEHSYQRI LYFADDMLLI LNSHTLASSL AVYQFCLDFT RLNRTPEPYV
RSSLQALITA NNAVNLRDQP TSYMLECIRE FSGLPSNFYN PNTRTVIEKN SISSAYGPLV
ESLIAHSTNI MVDLVRICSH NPCRFRRNLI NLLPEITVAH FEAEALDLKF VAKSLPSNGP
FSSFIYHVKL NAIEHILLSS FEQKLHQPYQ WPHFFAVLDH VFSIHQTHLE LHGKDRNTPP
MAKTFVTYLH RILNAIKETY SGYLLLTVLC MRLNIIKTPS FTLDEKIQES YYMAHYRPLI
NLRQPKPLLR SEADCIIKNL QNFSTDDLII KSNEKFTAAK NSLINVIKSG FEQNEFINPY
FLQTNYLKNL LCCCITNLVS LAILSKDHSA NLKIVEIPGN PLPSLSRT
