ID NACA_COCIM Reviewed; 205 AA. AC Q1DHR3; J3K086; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 03-MAY-2023, 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=CIMG_10150; OS Coccidioides immitis (strain RS) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=246410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS; 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). RN [2] RP GENOME REANNOTATION. RC STRAIN=RS; RX PubMed=20516208; DOI=10.1101/gr.103911.109; RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J., RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D., RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A., RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J., RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R., RA Taylor J.W., Rounsley S.D.; RT "Population genomic sequencing of Coccidioides fungi reveals recent RT hybridization and transposon control."; RL Genome Res. 20:938-946(2010). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG704915; EAS27545.3; -; Genomic_DNA. DR RefSeq; XP_001239128.1; XM_001239127.2. DR AlphaFoldDB; Q1DHR3; -. DR SMR; Q1DHR3; -. DR STRING; 246410.Q1DHR3; -. DR GeneID; 4558192; -. DR KEGG; cim:CIMG_10150; -. DR VEuPathDB; FungiDB:CIMG_10150; -. DR InParanoid; Q1DHR3; -. DR OMA; QTKCTRE; -. DR OrthoDB; 26509at2759; -. DR Proteomes; UP000001261; 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 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/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: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..205 FT /note="Nascent polypeptide-associated complex subunit FT alpha" FT /id="PRO_0000273486" FT DOMAIN 48..113 FT /note="NAC-A/B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507" FT DOMAIN 166..205 FT /note="UBA" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..169 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 130..150 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 151..165 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 205 AA; 22081 MW; 05F26F97F7F05DD4 CRC64; MANPRVEELP DEEVPKTTVE DAGESSESEA EAAEEPTIPG GAAITVHSRN EKKARKAIGK LGLKHVPGIT RVTLRRPKNI LFVINQPDVY RSPSSNTWII FGEAKIEDLN SQAQASAAQQ LSAAEAAGNG EHAGHEHIDL GKGKAPETEK KEEEEEEEGE VDETGLEAKD IELVMAQANV SRSKAIKALK ENDNDIVNSI MALSV //