ID A0A1U8CWV5_MESAU Unreviewed; 835 AA.
AC A0A1U8CWV5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=N-acetyltransferase ESCO1 {ECO:0000313|RefSeq:XP_012980313.1, ECO:0000313|RefSeq:XP_021090778.1};
GN Name=Esco1 {ECO:0000313|RefSeq:XP_012980313.1,
GN ECO:0000313|RefSeq:XP_021090778.1, ECO:0000313|RefSeq:XP_021090782.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012980313.1};
RN [1] {ECO:0000313|RefSeq:XP_012980313.1, ECO:0000313|RefSeq:XP_021090778.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_012980313.1; XM_013124859.2.
DR RefSeq; XP_021090778.1; XM_021235119.1.
DR RefSeq; XP_021090782.1; XM_021235123.1.
DR STRING; 10036.ENSMAUP00000020882; -.
DR GeneID; 101839884; -.
DR KEGG; maua:101839884; -.
DR CTD; 114799; -.
DR eggNOG; KOG3014; Eukaryota.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:SF1; N-ACETYLTRANSFERASE ESCO1; 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:UP000189706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 599..638
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 758..826
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 28..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 93763 MW; 7692EA27D2378CD5 CRC64;
MSIQEKSKEN SSKVIKEIED ENLELEIQGS QNSLIKRPGS KEAEKVLVRS SSKSKINQPE
LGTRMSTRSA TAVDKSATKS INKNTVTVKG QSQESAKKKR LCQEKLALGT FRGNDQFTRR
SQRLQQLTEC SVRSLRSRGI PTQTQAVKQN LQPARREQCN SPHSKSNKVT VNQKHVKRKV
LEVKSDCKED SDSVTNEVVN SPKEKKRKVQ HQTAPTCRSQ CIQGSEKCFQ KTNRKEESKP
VPVTSEIRKS KAAVSVVSKK NEPRKAAHTQ ANNSTTPAQI PQPLVPEQSI DHELEQAGKS
KRGSILQLCE EIAGEIESDT VEVKKEPSHM ENVEEKPAEV KSEGTDGERQ ILHQKEANQD
VQCNRFFPSR KTKPVKCILN GINNSTKRNS TWTKIKLSKF NSVQQHKLDS QVSPKLGLLP
TGFSPPVLEM PHSVSQSTFL EMKPHSNVTC QRDKMKGIKS EEDKINNIAI EINKATKRAP
GNCHLDNHIK HSPDSPLDNQ MKHSCESAPD KNFSLCSGST VEKNSLEDIA AASTLPSQAK
IDGDRKLPGS APKHLHSVLS SEASINSKHR ALPPNHSHLE ITIPKALKLK DSEKVDDKQL
VIDAGHKRFG AVSCNICGML YTASNPEDET QHLLFHNQFI SAVKYVGWKK ERILAEYPDG
RIIMVLPEDP KYALKKVDEI REMVDNDLGF QQAPLMCYSR TKTLLFISND KKVVGCLIAE
HIQWGYRVIE EKLPVVRSEE EKVRFERQKA WCCSTLPEPA ICGISRIWVF SMMRRKKIAS
RMIECLRSNF IYGSYLSKEE IAFSDPTPDG KLFATQYCGT GQFLVYNFIN GQNTT
//