ID A0A165FBW3_XYLHT Unreviewed; 207 AA.
AC A0A165FBW3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha {ECO:0000256|ARBA:ARBA00014437};
DE AltName: Full=Alpha-NAC {ECO:0000256|ARBA:ARBA00030300};
GN ORFNames=L228DRAFT_222925 {ECO:0000313|EMBL:KZF20799.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF20799.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF20799.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF20799.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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; KV407462; KZF20799.1; -; Genomic_DNA.
DR RefSeq; XP_018186354.1; XM_018330311.1.
DR AlphaFoldDB; A0A165FBW3; -.
DR STRING; 1328760.A0A165FBW3; -.
DR GeneID; 28895448; -.
DR InParanoid; A0A165FBW3; -.
DR OMA; QTKCTRE; -.
DR OrthoDB; 26509at2759; -.
DR Proteomes; UP000076632; 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:UP000076632};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 49..114
FT /note="NAC-A/B"
FT /evidence="ECO:0000259|PROSITE:PS51151"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22022 MW; A53687D022399FF1 CRC64;
MSNSRIEELP DEPTKNVEVE DASSSSDSEV EAGEGEANIP AGASVAVHSR NEKKARKAIA
KLGLKHVPGI TRVTLRRPKN ILFVINQPDV YKSPSSNTYI IFGEAKIEDL NSAAQASAAQ
QLAAAEANAN ADPHAGHDHG DKGKAVEAGD VKKDEEEDDG EEVDETGLEA KDIELVMAQA
SVSRKKAVKA LKENDNDIVN SIMALSI
//
