ID   NACB1_YEAS7             Reviewed;         157 AA.
AC   A6ZWL1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Nascent polypeptide-associated complex subunit beta-1;
DE            Short=NAC-beta-1;
DE   AltName: Full=BTF3 homolog EGD1;
DE   AltName: Full=Beta-1-NAC;
DE   AltName: Full=GAL4 DNA-binding enhancer protein 1;
GN   Name=EGD1; ORFNames=SCY_5688;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Component of the nascent polypeptide-associated complex
CC       (NAC), a dynamic component of the ribosomal exit tunnel, protecting the
CC       emerging polypeptides from interaction with other cytoplasmic proteins
CC       to ensure appropriate nascent protein targeting. The NAC complex also
CC       promotes mitochondrial protein import by enhancing productive ribosome
CC       interactions with the outer mitochondrial membrane and blocks the
CC       inappropriate interaction of ribosomes translating non-secretory
CC       nascent polypeptides with translocation sites in the membrane of the
CC       endoplasmic reticulum. EGD1 may act as a transcription factor that
CC       exert a negative effect on the expression of several genes that are
CC       transcribed by RNA polymerase II. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       consisting of EGD2 and either EGD1 or BTT1. NAC associates with
CC       ribosomes via EGD1 or BTT1, and with the CCR4-NOT complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Predominantly cytoplasmic, may also transiently localize to the
CC       nucleus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFW02000135; EDN61103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZWL1; -.
DR   SMR; A6ZWL1; -.
DR   PRIDE; A6ZWL1; -.
DR   EnsemblFungi; EDN61103; EDN61103; SCY_5688.
DR   HOGENOM; CLU_098726_2_2_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.70.30; -; 1.
DR   InterPro; IPR039370; BTF3.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR10351; PTHR10351; 1.
DR   Pfam; PF01849; NAC; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Phosphoprotein; Protein transport; Repressor;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN           1..157
FT                   /note="Nascent polypeptide-associated complex subunit beta-
FT                   1"
FT                   /id="PRO_0000310168"
FT   DOMAIN          38..103
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          19..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02642"
SQ   SEQUENCE   157 AA;  17020 MW;  7C278A3DC79BF95B CRC64;
     MPIDQEKLAK LQKLSANNKV GGTRRKLNKK AGSSAGANKD DTKLQSQLAK LHAVTIDNVA
     EANFFKDDGK VMHFNKVGVQ VAAQHNTSVF YGLPQEKNLQ DLFPGIISQL GPEAIQALSQ
     LAAQMEKHEA KAPADAEKKD EAIPELVEGQ TFDADVE