ID A0A3Q2DHB6_CYPVA Unreviewed; 629 AA.
AC A0A3Q2DHB6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSCVAP00000018502.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000018502.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000018502.1}
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; A0A3Q2DHB6; -.
DR Ensembl; ENSCVAT00000027462.1; ENSCVAP00000018502.1; ENSCVAG00000021780.1.
DR GeneTree; ENSGT00940000158598; -.
DR OMA; PTDWMDS; -.
DR Proteomes; UP000265020; 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:UP000265020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 399..438
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 558..625
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 69436 MW; 36BC2BD637B0911B CRC64;
MKEQASPVKR RSPRKRLLSP HVEKQAGQES PHKPAGSPRR SPRKSPSMVT SSFYGKQKTI
YLNPLERKAV KESLPSLPPV ITSPPPSAQK TEKKMKKTVK RGNKSRNAIT GSGKRGKKST
KGSPASKKAV EPSKRNTSSL AVKPTSTSSS NVPANNNPVE AKKGITLSFA SLKPKPKIFV
GAAFFGTGKK PTSMYKRPAP KSSARPAPVK SRSQTGPPQQ NAKTPKQQVD PRVASQLQEP
GKQMDVKEIQ DGTKQRTKFD PTDWMDVNDG ESETVKPSSS PELMAETHGV TKQVKIVLSR
TPSPKSTALF FDNQDELQTD GGSEQSKINP TESSTTPSKA SGAVYPIFGS SSKRLSAALR
PPVSCSTPSV SSGASPLPAS SAVKERQTRR KKEKLDHDQL IIDAGQKQFG ATTCSSCGMV
YSADNPEDNF QHTQFHQQFL DSIRYVGWKK ERVVAEFWDG KIILVLPDDP KYAVRKAEEV
RRIADNELGF QQVTLSRPTQ AKTFLFINTD RLVVGCLIAE PIRLAYRVLE QPDHKKDMTK
DDFMERHRAW CCSTTPEQAL CGISRIWVFS LARRQGIATR MLDTVRSTFM FGSYLSKDEI
AFSDPTPDGK LFATKYCNTP TFLIYNFIA
//
