ID   NACB_MAGO7              Reviewed;         172 AA.
AC   A4RC23; G4NJ88; Q2KG77;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Nascent polypeptide-associated complex subunit beta;
DE            Short=NAC-beta;
DE   AltName: Full=Beta-NAC;
GN   Name=EGD1; ORFNames=MGCH7_ch7g458, MGG_02713;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RA   Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T.K.,
RA   Dean R.A.;
RT   "The sequence of Magnaporthe grisea chromosome 7.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAQ71051.1; Type=Erroneous gene model prediction; Evidence={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; CM000230; EAQ71051.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM001237; EHA46304.1; -; Genomic_DNA.
DR   RefSeq; XP_003721047.1; XM_003720999.1.
DR   AlphaFoldDB; A4RC23; -.
DR   SMR; A4RC23; -.
DR   STRING; 318829.MGG_02713T0; -.
DR   EnsemblFungi; MGG_02713T0; MGG_02713T0; MGG_02713.
DR   GeneID; 2682313; -.
DR   KEGG; mgr:MGG_02713; -.
DR   VEuPathDB; FungiDB:MGG_02713; -.
DR   eggNOG; KOG2240; Eukaryota.
DR   HOGENOM; CLU_098726_2_1_1; -.
DR   InParanoid; A4RC23; -.
DR   OMA; KVHKNSM; -.
DR   OrthoDB; 1435264at2759; -.
DR   Proteomes; UP000009058; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; ISS:PAMGO_MGG.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; ISS:PAMGO_MGG.
DR   GO; GO:0005634; C:nucleus; ISS:PAMGO_MGG.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:PAMGO_MGG.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; ISS:PAMGO_MGG.
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..172
FT                   /note="Nascent polypeptide-associated complex subunit beta"
FT                   /id="PRO_0000294530"
FT   DOMAIN          54..119
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          36..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   172 AA;  18887 MW;  B131A2E4D63A8336 CRC64;
     MADVQERLKK LGASARIGYV LVNFFFSQAS IGSRWKTGKG TPRRKMKRAP ARSGGDDKKL
     QQTLKKLNVQ PIQAIEEVNM FKSDGNVIHF AAPKVHAAVP ANTFAIYGNG EDKELTELVP
     GILNQLGPDS LASLRKLAES YQNMQKADGD KEADDDDIPD LVAGENFEDK VE