ID A0A3Q1GBM5_9TELE Unreviewed; 526 AA.
AC A0A3Q1GBM5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Treacle protein-like {ECO:0000313|Ensembl:ENSAPOP00000015345.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000015345.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000015345.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1GBM5; -.
DR Ensembl; ENSAPOT00000033199.1; ENSAPOP00000015345.1; ENSAPOG00000018337.1.
DR GeneTree; ENSGT00940000157762; -.
DR Proteomes; UP000257200; 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: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:UP000257200};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 290..325
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 444..512
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 57424 MW; 533EC8AB0DB496B5 CRC64;
MDAISGSIER ADSALEEETA RQVINEVKAD KSVRNIEEGA ESNEVIVFVC GQPDDSDIVI
QTAEEQIKTV NQSVAELHEN QIVYEPISSP ESNDGREICA AAAAERHDGI SILDIQNSES
QQVEENASNF SQNADDGASV DPQLDNEGEI CVTGSQEVVE MEVETASVPE SSVPAQLEQN
NAAVDVKQVA VISSSDDVSA PDGRSEDVAE KSERNGFPEC VSATEFSEQV QEGAGVQEVA
DVRVTTTTAA AEAEMPDSAS EEYVILEPVP ESEIHFDIVT QAAAESGLSD AGQKHFGAVA
CSVCGMLYSA ANPEDESQHL LFHNQFISAV KYVGWKKERI LGEYPDGKII LVLPDDPKYA
LKKVEEIREM VDNDLGFQQV ETKCPSQTKT FLFISNDKKV AGCLIAEHIQ EGYRVIEEPA
PEGSEGEKVM FERQRAWCCS TTPEPAICGI SRIWVVSMMR RLGIASRMIE CLRNNFIYGS
YLSKDEIAFS DPTPDGKLFA THYFGTSQFL VYNFVSGTRS SQPKTV
//
