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Database: UniProt
Entry: A0A0A2VYK8_BEABA
LinkDB: A0A0A2VYK8_BEABA
Original site: A0A0A2VYK8_BEABA 
ID   A0A0A2VYK8_BEABA        Unreviewed;       630 AA.
AC   A0A0A2VYK8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=ABC transporter ATP-binding protein uup {ECO:0000313|EMBL:KGQ11472.1};
GN   ORFNames=BBAD15_g2833 {ECO:0000313|EMBL:KGQ11472.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11472.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ11472.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11472.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:KGQ11472.1}.
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DR   EMBL; ANFO01000216; KGQ11472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VYK8; -.
DR   STRING; 1245745.A0A0A2VYK8; -.
DR   HOGENOM; CLU_000604_36_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:EnsemblFungi.
DR   GO; GO:0071232; P:cellular response to histidine; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0006448; P:regulation of translational elongation; IEA:EnsemblFungi.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   HAMAP; MF_00848; Uup; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032524; ABC_tran_C.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR043686; Uup.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR   PANTHER; PTHR42855:SF1; ABC TRANSPORTER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF16326; ABC_tran_CTD; 1.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KGQ11472.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN          1..248
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          315..533
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   COILED          558..619
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   630 AA;  71229 MW;  35B798F76CC55DA6 CRC64;
     MHGAWLSFSD APLLDNTELH IEENERVCLV GRNGAGKSTL MKILNREIPL DDGRMVYEQD
     LIVARLQQDP PRNVAGTVYD FVAEGVEEQA EYLKAYHDIS HKVMSDPSEK NLNEMARIQE
     ILDHQGLWQL DSRINEVLEQ LGLEADTELS ALSGGWLRKA ALGRALVSSP RVLLLDEPTN
     HLDIETIDWL EGFLKEFQGS IIFISHDRSF IRNMATRIVD LDRGKLVSYP GDYDQYLLAK
     EEALRVEELQ NAEFDRKLAQ EEVWIRQGIK ARRTRNEGRV RALKAMRRER GERREVMGSA
     KMQVEEASRS GKIVFEMEDV NYQVAGKTLV RDFSAQVLRG DKIALVGPNG CGKTTLLKLM
     LSQLQADSGR VHCGTKLEVA YFDQHRAELD PDRTVMDNLA EGKQEVMVNG KPRHVLGYLQ
     DFLFHPKRAM TPVRALSGGE RNRLLLARLF LKPSNLLILD EPTNDLDVET LELLEELIDG
     YQGTVMLVSH DRQFVDNTVT ECWIFEGQGK IGRYVGGYHD AKGQQGSAQP LRQASAAKSE
     KAEAQKAEPV KRANSKLSYN LQRELEQLPQ RLEQLEADLG ALQAKVADAD FFNQPHDVTQ
     KVLAEMAAAE QALEEAFERW EYLEALKNGS
//
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