ID M3WKP5_FELCA Unreviewed; 602 AA.
AC M3WKP5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSFCAP00000013380.3};
GN Name=ESCO2 {ECO:0000313|Ensembl:ENSFCAP00000013380.3,
GN ECO:0000313|VGNC:VGNC:61960};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000013380.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013380.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013380.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000013380.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013380.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000013380.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013380.3};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000256|ARBA:ARBA00000636};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000256|ARBA:ARBA00005816}.
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DR EMBL; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006930803.1; XM_006930741.2.
DR AlphaFoldDB; M3WKP5; -.
DR STRING; 9685.ENSFCAP00000013380; -.
DR PaxDb; 9685-ENSFCAP00000013380; -.
DR Ensembl; ENSFCAT00000014430.6; ENSFCAP00000013380.3; ENSFCAG00000014426.6.
DR GeneID; 101093351; -.
DR KEGG; fca:101093351; -.
DR CTD; 157570; -.
DR VGNC; VGNC:61960; ESCO2.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; M3WKP5; -.
DR OMA; HIQYHHR; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000014426; Expressed in embryonic head and 8 other cell types or tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR PANTHER; PTHR45884:SF3; N-ACETYLTRANSFERASE ESCO2; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 378..417
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 530..598
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
SQ SEQUENCE 602 AA; 68251 MW; 2018557F358685D0 CRC64;
MSAFTPRKKK QRSLSCDNLL SDIPSKKLIL DFAENVFPSP DQKYISQSSD NNEEKVLCSQ
QGHFISSPLK TTEKSRLASA NQGSPFKSAV STVSFYNKDQ WYLNPLERKL IKESRSICLK
TNNEDKSFPI VTVCSKKINK KPQKCLTSKY QPKHKCIKPV SKNSKKSKQN RVAYKPVVEK
ENNYYSAQNN LNAPRVLSQK VKPQVTLQGG AAFFVRKKSC LRKLSSENKP LLELTQKNPS
EVIEDSDVET VRKRKGFEKR QVPKCLLLEK EPNVELLCAR SKNGEKSIKD SSGGVVSSRE
CKPNENKCFP SEDSLSENKA VSPDSVVYPI FSVSSVNTKR SLVEQSSVGS IISANLLKQI
NTQKSTNTRD TNKETKDQLI IDAGQKHFGA TMCKSCGMIY TASNPEDEMQ HVQHHHRFLE
GIKYTGWKKE RIVAQFWDGK ILLVLPHDPS YAIRKVEDVQ ELVDNELGFH QVVPRCPNKT
KTLLFISDEK RVVGCLIAEP IKQAFRVLSE PTGPSSKECH RAWQCSDVPE PAVCGISRIW
VFRLKRRKRI ARRLVDTLRN CFMFGCFLKT DEIAFSDPTP DGKLFATKYC NTPNFLVYNF
NS
//
