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NACA_SCLS1
ID   NACA_SCLS1              Reviewed;         214 AA.
AC   A7EIZ1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE            Short=NAC-alpha;
DE   AltName: Full=Alpha-NAC;
GN   Name=egd2; ORFNames=SS1G_05284;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476626; EDO02807.1; -; Genomic_DNA.
DR   RefSeq; XP_001593856.1; XM_001593806.1.
DR   AlphaFoldDB; A7EIZ1; -.
DR   SMR; A7EIZ1; -.
DR   STRING; 665079.A7EIZ1; -.
DR   PRIDE; A7EIZ1; -.
DR   EnsemblFungi; EDO02807; EDO02807; SS1G_05284.
DR   GeneID; 5490020; -.
DR   KEGG; ssl:SS1G_05284; -.
DR   VEuPathDB; FungiDB:sscle_08g065550; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   HOGENOM; CLU_057806_2_0_1; -.
DR   InParanoid; A7EIZ1; -.
DR   OMA; LVMCQAN; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
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   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..214
FT                   /note="Nascent polypeptide-associated complex subunit
FT                   alpha"
FT                   /id="PRO_0000310162"
FT   DOMAIN          52..117
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   DOMAIN          175..214
FT                   /note="UBA"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..175
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  23114 MW;  DDF7F4D84F0CCBFA CRC64;
     MSNPRIEELP DNEEPTKQQV TAEDEGSDSS DSEGEGEVES GIPAGAGAVV HSRNEKKARK
     SIAKLGLTRV PGITRVTLRR PKNILFVINN PEVYKSPTSN TYIVFGEAKI EDLNSQAQAS
     AAAQLAAQES HDHAGHDHSG HDHSHDHGKG KAVDTGDEKK EEEEDDTEEV DATGLEDKDI
     ELVMTQASVS RNKAVKALKE NDNDIVNSIM ALSI
 
 
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