ID A0A2S5B247_9BASI Unreviewed; 553 AA.
AC A0A2S5B247;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BMF94_6171 {ECO:0000313|EMBL:POY70761.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY70761.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY70761.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY70761.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
CC -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC {ECO:0000256|ARBA:ARBA00010322}.
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:POY70761.1}.
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DR EMBL; PJQD01000097; POY70761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B247; -.
DR OrthoDB; 1617at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR005654; ATPase_AFG1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF040713; ZapE; 1.
DR PANTHER; PTHR12169:SF6; AFG1-LIKE ATPASE; 1.
DR PANTHER; PTHR12169; ATPASE N2B; 1.
DR Pfam; PF03969; AFG1_ATPase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144}.
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 61292 MW; 7CBECA83392F6B93 CRC64;
MLPARTARQL AHSSRQRAAQ ALAGASRVPL PPLAAALHSS TPAPTRPTRP QRTPQPGWKR
TASSPNANKV GTKPRHFHST PPSGPAQAYD HQVATGLISN DDHQRSIVAI LQRMHDELDH
YQPPPIGPLP PPVKPSAWTR LMRSRLFADM SDELHQANTA VIPLPPPPPG LPNGLYLYGS
VGCGKSFLMD LFYANLPEKY REPGAEGNST SFGSKRVHFH QFMMEVHKKG HKIKMEQGGG
QDWIVIAARE IAEETRVLCF DEFQVTDIAD AMILRRLMEA LHAHGVVCVM TSNRAPDELY
KNGIQREQFM PCIELIKSSF TVHCLDSDID YRKRPRELSR VYFHPLTPQH ESEFNKLFEA
ACAGIDPSDN VMSGRELAVW GRPVKIPLST SHVAQFTFQD LCGAPHSAAD YLEITKTFGT
IFLRDVPQLG LDTKDQARRF ILFIDAAYEA RTKLFVLSDP PIASVFSDER RPTGEITPHM
RAMMDDLGLS AETVGSSSIF TGDEEVFAFA RAVSRITEMS SKQWAQLPSV KNDQGEGLTA
DQIHESGEKV ATA
//
