NACA_ASPTN
ID NACA_ASPTN Reviewed; 202 AA.
AC P0C2C7; Q0CGW2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE Short=NAC-alpha;
DE AltName: Full=Alpha-NAC;
GN Name=egd2; ORFNames=ATEG_07080.1;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU32464.1; Type=Erroneous gene model prediction; Note=The predicted gene ATEG_07080 has been split into 2 genes: ATEG_07080.1 and ATEG_07080.2.; Evidence={ECO:0000305};
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DR EMBL; CH476603; EAU32464.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001209766.1; XM_001209766.1.
DR AlphaFoldDB; P0C2C7; -.
DR SMR; P0C2C7; -.
DR STRING; 341663.P0C2C7; -.
DR GeneID; 4319385; -.
DR eggNOG; KOG2239; Eukaryota.
DR eggNOG; KOG3366; Eukaryota.
DR OrthoDB; 1097026at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
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; 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..202
FT /note="Nascent polypeptide-associated complex subunit
FT alpha"
FT /id="PRO_0000273482"
FT DOMAIN 46..111
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 163..202
FT /note="UBA"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..165
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 126..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 21912 MW; 367FDF0B1AA8F110 CRC64;
MADPRVEELP DEEVPKTNVE DAGSDSESEA GEEPTIPGGA AVAVHSRNEK KARKAIGKLG
LKLVPGITRV TFRRPKNILF VINQPEVYRS PSSNTWIIFG EAKIEDLNAQ AQASAAQQLA
AQEAAQEHAG HEHEDILGKA KEPEAEKKEA EEDDGEEVDE SGLEAKDIEL VMAQANVSRK
KAVKALREND NDIVNSIMAL SI