ID   ERF1Z_BRAOB             Reviewed;         435 AA.
AC   D2K760;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1-3 {ECO:0000305};
DE            Short=BoeRF1-3 {ECO:0000303|PubMed:21175633};
DE            Short=Eukaryotic release factor 1-3 {ECO:0000303|PubMed:21175633};
GN   Name=ERF1-3 {ECO:0000305};
OS   Brassica oleracea var. botrytis (Cauliflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=21175633; DOI=10.1111/j.1469-8137.2010.03578.x;
RA   Zhou X., Sun T.H., Wang N., Ling H.Q., Lu S., Li L.;
RT   "The cauliflower Orange gene enhances petiole elongation by suppressing
RT   expression of eukaryotic release factor 1.";
RL   New Phytol. 190:89-100(2011).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA
CC       (By similarity). Modulates plant growth and development
CC       (PubMed:21175633). {ECO:0000250|UniProtKB:Q39097,
CC       ECO:0000269|PubMed:21175633}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q39097}.
CC   -!- MISCELLANEOUS: Plants silencing ERF1-3 show increased elongation of the
CC       leaf petiole. {ECO:0000269|PubMed:21175633}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; GU183404; ACZ71035.1; -; mRNA.
DR   AlphaFoldDB; D2K760; -.
DR   SMR; D2K760; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   Gene3D; 3.30.960.10; -; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR024049; eRF1_1_sf.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR   PANTHER; PTHR10113; PTHR10113; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF55481; SSF55481; 1.
DR   TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Growth regulation; Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPV8"
FT   CHAIN           2..435
FT                   /note="Eukaryotic peptide chain release factor subunit 1-3"
FT                   /id="PRO_0000438019"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPV8"
SQ   SEQUENCE   435 AA;  48818 MW;  F4E2C3BF8EC82695 CRC64;
     MADQESDKSI EIWKSFKLIK GLESARGNGT SMISLIMPPR DQVARVTKML ADEYGTASNI
     KSRVNRQSVL SAITSAQQRL KLYNKVPPNG LVLYTGTIVT DDGKEKKVTI DFEPFKPINA
     SLYLCDNKFH TEPLNELLES DDKFGFIVMD GNGTLFGTLS GNTREVLHKF TVDLPKKHGR
     GGQSALRFAR LRMEKRHNYV RKTAELATQF YINPATSQPN VSGLILAGSA DFKTELSQSE
     LFDPRLQAKI LNVVDVSYGG ENGFNQAIEL SAEILSNVKF IQEKKLIGKY FEEISQDTGK
     YVFGVDDTLK ALDMGAVETL IVWENLDINR YELKNGATGE TVIKHLGKEQ ENDQSNFHDA
     ESNAELEIVE KMPLLEWFAN EYKRFGCTLE FVTNKSQEGS QFCRGFGGIG GLLRYQLDMR
     TFDELSDGEV YEDSD