ID   NACB_AJECN              Reviewed;         158 AA.
AC   A6R5Z3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Nascent polypeptide-associated complex subunit beta;
DE            Short=NAC-beta;
DE   AltName: Full=Beta-NAC;
GN   Name=EGD1; ORFNames=HCAG_05051;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476659; EDN08552.1; -; Genomic_DNA.
DR   RefSeq; XP_001539584.1; XM_001539534.1.
DR   AlphaFoldDB; A6R5Z3; -.
DR   SMR; A6R5Z3; -.
DR   STRING; 339724.A6R5Z3; -.
DR   PRIDE; A6R5Z3; -.
DR   EnsemblFungi; EDN08552; EDN08552; HCAG_05051.
DR   GeneID; 5446034; -.
DR   KEGG; aje:HCAG_05051; -.
DR   VEuPathDB; FungiDB:HCAG_05051; -.
DR   HOGENOM; CLU_098726_2_0_1; -.
DR   OMA; HFKNPRV; -.
DR   OrthoDB; 1435264at2759; -.
DR   Proteomes; UP000009297; 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; Protein transport; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN           1..158
FT                   /note="Nascent polypeptide-associated complex subunit beta"
FT                   /id="PRO_0000310165"
FT   DOMAIN          34..99
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..148
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   158 AA;  17391 MW;  35E8021A69C15418 CRC64;
     MDQAKLARLQ QSVRIGKGKG TPRRKTKKVH KSSGTDDKKL QTSLKKLNVQ PIQAIEEVNM
     FKEDGNVIHF AAPKVHASVP SNTFAIYGNG EDKELTELVP GILNQLGPDS LASLRKLAES
     YQSMQKGEGG EDAKKDDDDD DDEIPDLVEG ENFESKVE