(data stored in ACNUC7421 zone)

SWISSPROT: ECO1_ASHGO

ID   ECO1_ASHGO              Reviewed;         266 AA.
AC   Q757N6;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=N-acetyltransferase ECO1;
DE            EC=2.3.1.-;
DE   AltName: Full=Establishment of cohesion protein 1;
GN   Name=ECO1; OrderedLocusNames=AEL024C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 164.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Probable acetyltransferase required for the establishment of
CC       sister chromatid cohesion and couple the processes of cohesion and DNA
CC       replication to ensure that only sister chromatids become paired
CC       together. In contrast to the structural cohesins, the deposition and
CC       establishment factors are required only during S phase. Acts by
CC       acetylating the cohesin complex component SMC3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC       {ECO:0000305}.
DR   EMBL; AE016818; AAS52661.2; -; Genomic_DNA.
DR   RefSeq; NP_984837.2; NM_210191.2.
DR   SMR; Q757N6; -.
DR   STRING; 33169.AAS52661; -.
DR   EnsemblFungi; AAS52661; AAS52661; AGOS_AEL024C.
DR   GeneID; 4621035; -.
DR   KEGG; ago:AGOS_AEL024C; -.
DR   HOGENOM; HOG000093358; -.
DR   InParanoid; Q757N6; -.
DR   KO; K11268; -.
DR   OMA; ISRIWVC; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; IEA:EnsemblFungi.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR   GO; GO:0034421; P:post-translational protein acetylation; IBA:GO_Central.
DR   GO; GO:0006275; P:regulation of DNA replication; IBA:GO_Central.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:EnsemblFungi.
DR   GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0032200; P:telomere organization; IEA:EnsemblFungi.
DR   GO; GO:0070058; P:tRNA gene clustering; IEA:EnsemblFungi.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR033257; Eco1/CTF7.
DR   InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR   Pfam; PF13880; Acetyltransf_13; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757N6.
DR   SWISS-2DPAGE; Q757N6.
KW   Acyltransferase; Cell cycle; Metal-binding; Nucleus; Reference proteome;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..266
FT                   /note="N-acetyltransferase ECO1"
FT                   /id="PRO_0000074545"
FT   DOMAIN          108..266
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ZN_FING         31..55
FT                   /note="CCHH-type"
SQ   SEQUENCE   266 AA;  29944 MW;  F32B203E1146FD28 CRC64;
     MAGVKKNRSP RKPTKLLQSR LKFAHSSATL KKCTECQMSY IIDSPADCAE HKKYHDLHLY
     GKKWLASWGT AIQDTCSSQY ITPPSTSGGN ASGNGAKADR EDYIVYITPG KTAEVKAMME
     IMYIVNNELT APHDENDFWS EEGTSSMGRA FVYIKDGRAV GAITVEYLKE DDSRGRWMRV
     STRELVPEVV PRVRLGISRI WVCRKQRGQG IATRLLECVR KYAILGNEVA RWEMAWSQPS
     ESGGKLATRY NSVRHKSGEL LIPCYI
//

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