ID   A0A2K6SYK5_SAIBB        Unreviewed;       511 AA.
AC   A0A2K6SYK5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSSBOP00000012473.1};
GN   Name=ESCO2 {ECO:0000313|Ensembl:ENSSBOP00000012473.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000012473.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000012473.1}
RP   IDENTIFICATION.
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   AlphaFoldDB; A0A2K6SYK5; -.
DR   STRING; 39432.ENSSBOP00000012473; -.
DR   Ensembl; ENSSBOT00000029264.1; ENSSBOP00000012473.1; ENSSBOG00000023036.1.
DR   GeneTree; ENSGT00940000158598; -.
DR   OMA; HIQYHHR; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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: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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   TRANSMEM        445..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          304..339
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          467..507
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
SQ   SEQUENCE   511 AA;  58428 MW;  9160790C330648CC CRC64;
     MAALTSRKRK QDFLNCDSLL LFTENLFPSP NKNDTNEENL LSSQQGPFVL SAFKTSEINR
     RPSANQGSPF KSAVSTVSFY NQNKWYLNPL ERKLIKESRS TYLKNHVEDK SFPIVTEKMQ
     GKPVCPKKNN KKPQKSLTAK YQPRYRHIKP VSRNPKNSKQ NRVVCKPVGE KENNCYSAEN
     NPNAPRVLSQ KIKPQVTLQG GAAFFVSRKK SSLRKWSSEN EPSMGLTGKN KSELIEDSDV
     ETVSEKKALE TRQVPKCLFL EEKLNIELLN VSSKNQEKLI KVKKAKYVVL KMSTVYPIFN
     ASSDAGQKHF GATVCKSCGM IYTASNPEDE MQHVQHHHRF LEGIKYVGWK KERVVAEFWD
     GKIVLVLPRD PSFAIKKVED VQELVDNELG FQQVVPKCPN KIKTFLFISD EKRVVGCLIA
     EPIKQVRSLS AFKIAIINDI LPTEIYLTMW IIEVIFNIWN FALYKQNRNC FMFGCFLSTD
     EIAFSDPTPD GKLFATKYCN TPNFLVYNFN S
//