ID A0A2Y9DW45_TRIMA Unreviewed; 614 AA.
AC A0A2Y9DW45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=N-acetyltransferase ESCO2 {ECO:0000313|RefSeq:XP_004382239.1};
GN Name=LOC101356057 {ECO:0000313|RefSeq:XP_004382239.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004382239.1};
RN [1] {ECO:0000313|RefSeq:XP_004382239.1}
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_004382239.1; XM_004382182.2.
DR STRING; 127582.A0A2Y9DW45; -.
DR GeneID; 101356057; -.
DR KEGG; tmu:101356057; -.
DR InParanoid; A0A2Y9DW45; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:UP000248480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 387..426
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 542..610
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 238..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 69446 MW; E94C685A3358BC3D CRC64;
MAAFTPRKRK QHSLNCDSLL SDIPSKKLIL DFTENIFLPP NKKHILQSSD KNEENMHCFQ
QDDFISSSLN TSTFPTNKKN RSSSADQGSP FKSAVSTVSF YNKDKWYLNP LERKLIKESR
ATCLKTNNED KSFPSMMEKM QGKPVCSKKM NKKQQKSLTA KCQPSYKCIK PVSRNSKNSK
QNRVAYKPIV GKENSCYSAE NNLNAPRVLS QKIKLQVTLQ GGAAFFVSRK KSSLRKSSLE
NKSLLGSTGE NKSEVTEDSD GETVRERKTF ETSQVPKCLL QELNMELLGA RSKNEKLMKD
SSGGIVSSGG YQLDENKHFA LEDTLSENKA ASPESVVYPI FSVSSVNTKR SVAEEQSPMG
SVISTNFLKQ TSTQKSARDT NKEIKDQFII DAGQKHFGAT MCKSCGMIYT ASNPEDELQH
VQHHQRFLEG IKYAGWKKER VVAEFWDGKI VLVLPHDPNY AIRKVEDVQE LVDNELGFHQ
VIPRRPDKTK TFLFISDEKK VVGCLIAEPI KQAFRVLSEP TGPESARSKE CHRAWQCSNV
PQPAICGISR IWVFRLKRRK RIARRLVDTL RNCFMFGCFL STXXXXXXXP TPDGKLFASK
YCNTPNFLVY NFNS
//