ID   NACA_ASHGO              Reviewed;         168 AA.
AC   Q756T5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=EGD2; OrderedLocusNames=AER168C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. EGD2 may also be involved in transcription
CC       regulation (By similarity). {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-alpha family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52850.1; -; Genomic_DNA.
DR   RefSeq; NP_985026.1; NM_210380.1.
DR   AlphaFoldDB; Q756T5; -.
DR   SMR; Q756T5; -.
DR   STRING; 33169.AAS52850; -.
DR   EnsemblFungi; AAS52850; AAS52850; AGOS_AER168C.
DR   GeneID; 4621233; -.
DR   KEGG; ago:AGOS_AER168C; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   HOGENOM; CLU_057806_2_1_1; -.
DR   InParanoid; Q756T5; -.
DR   OMA; LVMCQAN; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070300; F:phosphatidic acid binding; IEA:EnsemblFungi.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   Gene3D; 2.20.70.30; -; 1.
DR   InterPro; IPR016641; EGD2/NACA.
DR   InterPro; IPR044034; NAC-like_UBA.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR21713; PTHR21713; 1.
DR   Pfam; PF19026; HYPK_UBA; 1.
DR   Pfam; PF01849; NAC; 1.
DR   PIRSF; PIRSF015901; NAC_alpha; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..168
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000273479"
FT   DOMAIN          14..78
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   DOMAIN          129..168
FT                   /note="UBA"
FT   REGION          83..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  18217 MW;  FC75CDFD3CDB3486 CRC64;
     MSEIPENSKV SIYSKNEKKA RELIQKFSMK PMPGITRVTF RKKNNQIFAI DNPDVYKTQG
     GNYVVFGEPK VDDFTRRLAR AQQQAASAAK DPQSIQADMA AAAAAPAAPA APAAAPEEDE
     AGQVDESGLD GQDIELVMQQ ANVSRNKAVK ALREHNSDIV NAIMSLSK