ID J6EJK3_SACK1 Unreviewed; 174 AA.
AC J6EJK3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha {ECO:0000256|ARBA:ARBA00014437};
DE AltName: Full=Alpha-NAC {ECO:0000256|ARBA:ARBA00030300};
GN Name=YHR193C {ECO:0000313|EMBL:EJT43437.1};
GN Synonyms=SKDI08G2380 {ECO:0000313|EMBL:CAI4064157.1};
GN ORFNames=SKDI_08G2380 {ECO:0000313|EMBL:CAI4064157.1}, SKUD_168906
GN {ECO:0000313|EMBL:EJT43437.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT43437.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT43437.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT43437.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT43437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43437.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT43437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43437.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4064157.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4064157.1};
RA Byrne P K.;
RL Submitted (OCT-2022) 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. {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; OX365903; CAI4064157.1; -; Genomic_DNA.
DR EMBL; AACI03000802; EJT43437.1; -; Genomic_DNA.
DR AlphaFoldDB; J6EJK3; -.
DR STRING; 226230.J6EJK3; -.
DR HOGENOM; CLU_057806_2_1_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 8.
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; cd14278; UBA_NAC_like; 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 InterPro; IPR009060; UBA-like_sf.
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 SUPFAM; SSF46934; UBA-like; 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:UP000002753};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 14..78
FT /note="NAC-A/B"
FT /evidence="ECO:0000259|PROSITE:PS51151"
FT REGION 85..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 174 AA; 18684 MW; 763D4C5834DDAEA0 CRC64;
MSAIPENASV TVLNKNEKKA RDLIGKLGLK QIPGIIRVTF RKKDNQIYAI EKPEVFRSAG
GNYVVFGEAK VDNFTQKLAA AQQQAQASGI MPSNEDVATK SPEDIQADMK AAAEGSVNAA
TEEDDEEGEV DAGDLNKDDV ELVVQQTNVS KNQAIKALKA HNGDLVNAIM SLSK
//
