ID A0A2V1AXK8_9ASCO Unreviewed; 178 AA.
AC A0A2V1AXK8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha {ECO:0000256|ARBA:ARBA00014437};
DE AltName: Full=Alpha-NAC {ECO:0000256|ARBA:ARBA00030300};
GN ORFNames=CXQ85_005160 {ECO:0000313|EMBL:PVH22588.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH22588.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH22588.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH22588.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVH22588.1}.
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DR EMBL; PKFO01000008; PVH22588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AXK8; -.
DR STRING; 45357.A0A2V1AXK8; -.
DR EnsemblFungi; CXQ85_005160-t46_1; CXQ85_005160-t46_1-p1; CXQ85_005160.
DR VEuPathDB; FungiDB:CXQ85_005160; -.
DR OrthoDB; 26509at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070300; F:phosphatidic acid binding; IEA:EnsemblFungi.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; IEA:EnsemblFungi.
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 Reference proteome {ECO:0000313|Proteomes:UP000244309};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 16..80
FT /note="NAC-A/B"
FT /evidence="ECO:0000259|PROSITE:PS51151"
FT REGION 79..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 19423 MW; 62912AA169DC8186 CRC64;
MSVEEIPQGA EVSIISKNEK KARETIKKFN LKQIKGISRV TFKQKGNLIY AIDEPDVYKS
AAGTYVVFGE AKVDDMNQRI ADAQAQQQAA ADSAATEGEG KDDVTTDKSP EAITADLEKA
SLNSAKPDEV DENDLNEEGL ESSDIDIIVE QTHVSRARAI AALRKHKNDM VNAIMELS
//
