ID NACA_PHANO Reviewed; 211 AA.
AC Q0UKB5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE Short=NAC-alpha;
DE AltName: Full=Alpha-NAC;
GN Name=EGD2; ORFNames=SNOG_07799;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445335; EAT85265.1; -; Genomic_DNA.
DR RefSeq; XP_001798126.1; XM_001798074.1.
DR AlphaFoldDB; Q0UKB5; -.
DR SMR; Q0UKB5; -.
DR STRING; 321614.Q0UKB5; -.
DR EnsemblFungi; SNOT_07799; SNOT_07799; SNOG_07799.
DR GeneID; 5975019; -.
DR KEGG; pno:SNOG_07799; -.
DR VEuPathDB; FungiDB:JI435_077990; -.
DR eggNOG; KOG2239; Eukaryota.
DR HOGENOM; CLU_057806_2_0_1; -.
DR InParanoid; Q0UKB5; -.
DR OMA; QTKCTRE; -.
DR OrthoDB; 26509at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd22054; NAC_NACA; 1.
DR CDD; cd14358; UBA_NAC_euk; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 2.20.70.30; Nascent polypeptide-associated complex domain; 1.
DR InterPro; IPR016641; EGD2/NACA0like.
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:SF4; GH09281P-RELATED; 1.
DR PANTHER; PTHR21713; NASCENT POLYPEPTIDE ASSOCIATED COMPLEX ALPHA SUBUNIT-RELATED; 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..211
FT /note="Nascent polypeptide-associated complex subunit
FT alpha"
FT /id="PRO_0000273494"
FT DOMAIN 48..113
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 172..211
FT /note="UBA"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23324 MW; 830A6C9AF1A649C5 CRC64;
MSNPRIEELP DEPEKKNVQI EEDESSDESE GEEGEANIPA GASVAVHSRN EKKARKAIAK
LGLKHIDGIT RVTLRRPKNI LFVINQPDVY KSPSSNTWII FGEAKIEDLN SQAQASAAQQ
LAQAEAASHD HSGHDHDHDH KGKGKAVEDK KDDEEDEEEE EEDDEEVDDS GLEAKDIELV
MQQASVSRKK AVKALKENDN DIVNSIMALS I
//
