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Database: UniProt
Entry: A0A1U8CWV5_MESAU
LinkDB: A0A1U8CWV5_MESAU
Original site: A0A1U8CWV5_MESAU 
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
//
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