ID   NACB_PICST              Reviewed;         154 AA.
AC   A3GHR2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Nascent polypeptide-associated complex subunit beta;
DE            Short=NAC-beta;
DE   AltName: Full=Beta-NAC;
GN   Name=EGD1; ORFNames=PICST_75534;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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 EGD1. NAC associates with ribosomes via EGD1 (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}.
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DR   EMBL; AAVQ01000002; EAZ63097.1; -; Genomic_DNA.
DR   RefSeq; XP_001387120.1; XM_001387083.1.
DR   AlphaFoldDB; A3GHR2; -.
DR   SMR; A3GHR2; -.
DR   STRING; 4924.XP_001387120.1; -.
DR   EnsemblFungi; EAZ63097; EAZ63097; PICST_75534.
DR   GeneID; 4851811; -.
DR   KEGG; pic:PICST_75534; -.
DR   eggNOG; KOG2240; Eukaryota.
DR   HOGENOM; CLU_098726_2_2_1; -.
DR   InParanoid; A3GHR2; -.
DR   OMA; KVHKNSM; -.
DR   OrthoDB; 1435264at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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; Protein transport; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN           1..154
FT                   /note="Nascent polypeptide-associated complex subunit beta"
FT                   /id="PRO_0000285134"
FT   DOMAIN          33..98
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          125..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  16591 MW;  F182C903DF6F4762 CRC64;
     MPVDPEKLAK LQKAAAKKVG GSRVKAKKVV KTEQDDTKLI EALGKLKATK IENVEEANFF
     REDGKVLHFN RVGVQGAAAS NTFAFTGYPQ EKNVTQLIPQ ILPQLGAENL EILRQLAEQL
     QAGKAPTELN AGAPAGGDEG IPDLIDGEKF DEVE