ID W6MQD7_9ASCO Unreviewed; 186 AA.
AC W6MQD7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha {ECO:0000256|ARBA:ARBA00014437};
DE AltName: Full=Alpha-NAC {ECO:0000256|ARBA:ARBA00030300};
GN ORFNames=KUCA_T00004950001 {ECO:0000313|EMBL:CDK28964.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28964.1};
RN [1] {ECO:0000313|EMBL:CDK28964.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28964.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28964.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28964.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) 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; HG793130; CDK28964.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MQD7; -.
DR STRING; 1382522.W6MQD7; -.
DR HOGENOM; CLU_057806_2_1_1; -.
DR OrthoDB; 26509at2759; -.
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 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..88
FT /note="NAC-A/B"
FT /evidence="ECO:0000259|PROSITE:PS51151"
FT REGION 95..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 186 AA; 19737 MW; D00D04EFB7EE02EF CRC64;
MSAEDKIVEV SDEQIPEGSE VSVISKDEKK ARALISKLGL KEVPGISRVT FRRRGEIVAI
ENPSVYKSPA GSYVVFGEAK VEDLAKRYEE AAAAEAAAAA AGGAPKDADS ITADLQASAL
EREHNHDHAG HDHSHDDEDD GEVDLTGLVA EDVDIVVDQA HCSKSKAAKA LREHSGDVIN
AIMSLV
//
