ID A0A2V5HYZ3_9EURO Unreviewed; 363 AA.
AC A0A2V5HYZ3;
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=BP00DRAFT_437957 {ECO:0000313|EMBL:PYI29031.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI29031.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI29031.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI29031.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC consisting of EGD2 and EGD1. NAC associates with ribosomes via EGD1.
CC {ECO:0000256|ARBA:ARBA00025826}.
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; KZ825537; PYI29031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HYZ3; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd22054; NAC_NACA; 1.
DR CDD; cd14358; UBA_NAC_euk; 1.
DR Gene3D; 6.10.280.70; -; 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; IPR008689; ATP_synth_F0_dsu_mt.
DR InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
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; PF05873; Mt_ATP-synt_D; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR SUPFAM; SSF161065; ATP synthase D chain-like; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 46..111
FT /note="NAC-A/B"
FT /evidence="ECO:0000259|PROSITE:PS51151"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 290..317
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 40217 MW; DFCCB55B05AA8A54 CRC64;
MADPRVEELP DEEVPKTQVE DAGSDSESEA GDEPTIPGGA AVTIHSRNEK KARKAIGKLG
LKHVPGITRV TLRRPKNILF VINQPDVYRS PTSNTWIIFG EAKIEDLNSQ AQASAAQQLA
EAAANEHAGH DHEHDHAQAK APEAEAKKEE EEDDGEEVDE SGLEAKDIEL VMAQANVSRK
KAVKALREND NDIRSAALKI DWTKLTSSLG LRGQTAASLQ AFKKRNDDAR RKVQVLSEQP
QTVDFAHYRK VLKNQAIVDQ LESHFKSFKP ATYDVNRQLK AIDAFEAQAV QSAEETKGKV
EVELRNLQKT LENIETARPF EDLTVDEVAA AQPEIDEKTS SLVQKGRWMP AGYKERFGEM
SVV
//