GenomeNet

Database: UniProt
Entry: F0XAB5_GROCL
LinkDB: F0XAB5_GROCL
Original site: F0XAB5_GROCL 
ID   F0XAB5_GROCL            Unreviewed;       245 AA.
AC   F0XAB5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE            EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
GN   ORFNames=CMQ_3495 {ECO:0000313|EMBL:EFX05426.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX05426.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) +
CC         N-terminal N(alpha)-acetyl-L-seryl-[histone H2A];
CC         Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00000345};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596,
CC         Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC         ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00001388};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008870}.
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; GL629735; EFX05426.1; -; Genomic_DNA.
DR   RefSeq; XP_014174908.1; XM_014319433.1.
DR   AlphaFoldDB; F0XAB5; -.
DR   STRING; 655863.F0XAB5; -.
DR   GeneID; 25976601; -.
DR   eggNOG; KOG2488; Eukaryota.
DR   HOGENOM; CLU_051699_2_1_1; -.
DR   InParanoid; F0XAB5; -.
DR   OrthoDB; 2047206at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043998; F:histone H2A acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039949; NAA40.
DR   PANTHER; PTHR20531; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   PANTHER; PTHR20531:SF1; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFX05426.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        174..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          94..244
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          115..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   245 AA;  27895 MW;  D921AB303419D6CF CRC64;
     MAVKKRRRAA TSPIERANQK NDEDFIASYL APGAPLAVPW TARWTHPQTG AAYDVSLARS
     GCVGEAALET CFALIEETSR KDYDGSQQKW QPADKRREMR EADLRYILVQ EVRGEEAEEK
     EGETKERKGG QKEKDQSHQR IRGFTSLMPA YEEGQPVVYC YEIHLKPELQ GTGLAGLLLG
     FLYTIAYNLP LIAKVMLTCF LSNERALRFY RKQHFVVDPI APEIRQLRGK TVVPDYTIMS
     KAVRR
//
DBGET integrated database retrieval system