ID A0A150GU09_GONPE Unreviewed; 559 AA.
AC A0A150GU09;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GPECTOR_7g1262 {ECO:0000313|EMBL:KXZ53366.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ53366.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000256|ARBA:ARBA00005816}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ53366.1}.
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DR EMBL; LSYV01000008; KXZ53366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GU09; -.
DR STRING; 33097.A0A150GU09; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
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:SF2; N-ACETYLTRANSFERASE ECO; 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:UP000075714};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 47..85
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 459..505
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 13..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 55780 MW; 44F343D8F12A0767 CRC64;
MAGRDAFAML MRGARQARCD SRAPEDKPRP AAARTPAPPG GSTHGTQLHL DLGQRDFSFA
SCPGCGMLYG KGLPSEERLH EQFHNAHLAA FRFQGWSSER VVLRDGPRSR LLLVLPTDPR
AQWRKVSELC GRLERLLGVP EGHLLAERPP FKVFLWVSAE PATGAPGPGP RPGSSGGGGG
GSKGGRVVGV LVAQLQERAR RATLSPQPPQ PLRGRLRPPH TREGAAPPPA PAKRAIAAGP
AAATGTVAVA ATQAPGRVRG VPAGSVPAEG RLRGCQPNLG DALAPAGCST PAAATSSALQ
YGLCEPDAAE LGAVARGAGE EGLGDAAGAS AAPCAVESAG DSGGSGGGGA GGGEGGGGRC
LPEVKRRRCS DDGGDGLVNG GAGCKTSRAE GHTTAATARS PRHHAAVVGG APGVPQQQHA
DGGGREACHD GSPRPTPAPA PAPAPASTAA AALPASSARV VVGVRGLWVE PGSRRRGVAR
RMLDAARALM VPGLLAERQQ TAFSALAAAA TAGDDDGGAA FAAFASSYLG ADSGSGSDRS
CSGNGGGVGG SVQVLLYDN
//
