ARD1_SCHPO
ID ARD1_SCHPO Reviewed; 177 AA.
AC Q9UTI3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=N-terminal acetyltransferase A complex catalytic subunit ard1;
DE Short=NatA complex subunit ARD1;
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P07347};
GN Name=ard1; ORFNames=SPAC15E1.08;
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: Catalytic component of the NatA N-terminal acetyltransferase,
CC which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly
CC and Met-Ala. N-acetylation plays a role in normal eukaryotic
CC translation and processing, protect against proteolytic degradation and
CC protein turnover. {ECO:0000250|UniProtKB:P07347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P07347};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC complex, which is composed of at least ard1 and nat1.
CC {ECO:0000250|UniProtKB:P07347}.
CC -!- INTERACTION:
CC Q9UTI3; O74985: nat1; NbExp=4; IntAct=EBI-16067117, EBI-16067095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB52427.1; -; Genomic_DNA.
DR PIR; T37723; T37723.
DR RefSeq; NP_594309.1; NM_001019732.2.
DR PDB; 4KVM; X-ray; 2.60 A; E/F/G/H=1-156.
DR PDB; 4KVO; X-ray; 3.15 A; E/F/G/H=1-156.
DR PDB; 4KVX; X-ray; 2.00 A; A/B=1-156.
DR PDBsum; 4KVM; -.
DR PDBsum; 4KVO; -.
DR PDBsum; 4KVX; -.
DR AlphaFoldDB; Q9UTI3; -.
DR SMR; Q9UTI3; -.
DR BioGRID; 279215; 3.
DR DIP; DIP-60549N; -.
DR IntAct; Q9UTI3; 1.
DR STRING; 4896.SPAC15E1.08.1; -.
DR iPTMnet; Q9UTI3; -.
DR MaxQB; Q9UTI3; -.
DR PaxDb; Q9UTI3; -.
DR PRIDE; Q9UTI3; -.
DR EnsemblFungi; SPAC15E1.08.1; SPAC15E1.08.1:pep; SPAC15E1.08.
DR GeneID; 2542765; -.
DR KEGG; spo:SPAC15E1.08; -.
DR PomBase; SPAC15E1.08; -.
DR VEuPathDB; FungiDB:SPAC15E1.08; -.
DR eggNOG; KOG3235; Eukaryota.
DR HOGENOM; CLU_013985_7_2_1; -.
DR InParanoid; Q9UTI3; -.
DR OMA; MSMQNAN; -.
DR PhylomeDB; Q9UTI3; -.
DR BRENDA; 2.3.1.255; 5613.
DR PRO; PR:Q9UTI3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031415; C:NatA complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IDA:PomBase.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IDA:PomBase.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IC:PomBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..177
FT /note="N-terminal acetyltransferase A complex catalytic
FT subunit ard1"
FT /id="PRO_0000310300"
FT DOMAIN 1..153
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:4KVX"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:4KVX"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4KVX"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4KVX"
SQ SEQUENCE 177 AA; 20305 MW; ABE46773A259B82B CRC64;
MDIRPARISD LTGMQNCNLH NLPENYQLKY YLYHAISWPM LSYVATDPKG RVVGYVLAKM
EEEPKDGIPH GHITSVSVMR SYRHLGLAKR LMVQSQRAMV EVYGAKYMSL HVRKSNRAAI
HLYRDTLQFD VQGIESKYYA DGEDAYAMHK DFSTLKFDTP ETNDELAKTV QSLALNN
