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Database: UniProt
Entry: G3BA00_CANTC
LinkDB: G3BA00_CANTC
Original site: G3BA00_CANTC 
ID   G3BA00_CANTC            Unreviewed;       179 AA.
AC   G3BA00;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha {ECO:0000256|ARBA:ARBA00014437};
DE   AltName: Full=Alpha-NAC {ECO:0000256|ARBA:ARBA00030300};
GN   ORFNames=CANTEDRAFT_114829 {ECO:0000313|EMBL:EGV62495.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV62495.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(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. {ECO:0000256|ARBA:ARBA00025035}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family.
CC       {ECO:0000256|ARBA:ARBA00009882}.
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DR   EMBL; GL996527; EGV62495.1; -; Genomic_DNA.
DR   RefSeq; XP_006688665.1; XM_006688602.1.
DR   AlphaFoldDB; G3BA00; -.
DR   STRING; 590646.G3BA00; -.
DR   GeneID; 18247601; -.
DR   KEGG; cten:CANTEDRAFT_114829; -.
DR   eggNOG; KOG2239; Eukaryota.
DR   HOGENOM; CLU_057806_2_0_1; -.
DR   OrthoDB; 26509at2759; -.
DR   Proteomes; UP000000707; 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/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   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          16..80
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000259|PROSITE:PS51151"
FT   REGION          79..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   179 AA;  19828 MW;  CC3171F2B3AFF4F5 CRC64;
     MSIEEIPQGA DIQVISKNEK KARDAIKKFN LKQIKGISRV TFKQRGNLIY AIDTPEVYKS
     VSGTYIVFGE AKVDDINQRF ADQAAAGEDD HEGHDHSHEG HDHSHEDKSP ESITADLEKA
     SLGGATVEEE DDDEEVDDTG LDPKDIEIII EQTKVSRAKA VKALRKHDGD MVNAIMEFA
//
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