ID   NACA_ASPCL              Reviewed;         204 AA.
AC   A1CMF8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=egd2; ORFNames=ACLA_096790;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027058; EAW08745.1; -; Genomic_DNA.
DR   RefSeq; XP_001270171.1; XM_001270170.1.
DR   AlphaFoldDB; A1CMF8; -.
DR   SMR; A1CMF8; -.
DR   STRING; 5057.CADACLAP00008965; -.
DR   EnsemblFungi; EAW08745; EAW08745; ACLA_096790.
DR   GeneID; 4702542; -.
DR   KEGG; act:ACLA_096790; -.
DR   VEuPathDB; FungiDB:ACLA_096790; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   HOGENOM; CLU_057806_2_0_1; -.
DR   OMA; LVMCQAN; -.
DR   OrthoDB; 1331328at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042788; C:polysomal ribosome; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..204
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000282680"
FT   DOMAIN          46..111
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   DOMAIN          165..204
FT                   /note="UBA"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..165
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22032 MW;  846C3A8D96C9F2FD CRC64;
     MADPRVEELP DEEVPKTNVE DAGSDSESEA GEESSIPSGA AVTIHSRNEK KARKAIGKLG
     LKHVPGITRV TLRRPKNILF VINQPDVYRS PTSNTWIIFG EAKIEDLNSQ AQASAAQQLA
     AAEAAAGEHA GHDHDHDHGK GKAPETEAKK EEEEDDGEEV DETGLEAKDI ELVMAQANVS
     RKKAVKALRE NDNDIVNSIM ALSI