ID   A0A3B3T757_9TELE        Unreviewed;       661 AA.
AC   A0A3B3T757;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-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:ENSPKIP00000038126.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000038126.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000038126.1}
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; A0A3B3T757; -.
DR   STRING; 1676925.ENSPKIP00000038126; -.
DR   Ensembl; ENSPKIT00000019115.1; ENSPKIP00000038126.1; ENSPKIG00000016038.1.
DR   GeneTree; ENSGT00940000158598; -.
DR   OrthoDB; 22809at2759; -.
DR   Proteomes; UP000261540; 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:1990523; P:bone regeneration; IEA:Ensembl.
DR   GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0007062; P:sister chromatid cohesion; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          431..470
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          589..657
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  73278 MW;  586B4D02F0065654 CRC64;
     MLPYGTARKR KHSSTGSAST RVKRQVVGRG TPPRRRSPLL PQSPVGETVI GHGQNKQNYH
     SHKIMASPRR MGSSPLAPRI LYGDSPPKGS PKIASPVKPA MGTRSFYSKK KALYLTPLER
     KLISETKPAI SQTNASLTSP LRSVTTQRTK TVPKVTKRIS ARGQKNNIRG YMSSPGMGRS
     SNVQADLPVE STTSLPPIIF GSLKAKVKPK LIVGAAFFIS GKRAITMHKK AMLKHSKLQL
     TAKVEKRPVP LPAEEQGKDP RGGFKAATNV PEMKPQELPP KVTTKRVSFG DPMKFTGIVK
     ENLEMFEPGT SEVQSTVTQL QKHRITKEVK IVLSRTVTPT SSESSLSDMS TPDTSTEMAS
     DTVFDLSNVT SACSKSVSVS PSVYPIFGSR RPQKKRSISS PMNCSTPSAL SASIRQRTTK
     KKHLERQSFD QLIIDAGQKQ FGATTCSSCG MIYSADSLED NFQHTQFHQR FLDSIKFVGW
     KKERVVAEFW DGKIVLVLPD DPKYAVRKAE DIRQLADNEL GFQQISLSSP TQAKTYLFVN
     NERMIVGCLI VEHIKQAFRV IDQLGHTEDV TKRDFMDHHR AWCCSTTPVK AICGVSRIWV
     FSLTRQQGIA TRLVDSARKS FIYGIHLDKE EVAFSDPTPD GKLFATKYCG TPEFLVYNFI
     C
//