ID A0A2S5B8E3_9BASI Unreviewed; 493 AA.
AC A0A2S5B8E3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative Phospholipid-translocating ATPase {ECO:0000313|EMBL:POY73046.1};
DE EC=3.6.3.1 {ECO:0000313|EMBL:POY73046.1};
GN ORFNames=BMF94_3884 {ECO:0000313|EMBL:POY73046.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY73046.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY73046.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY73046.1,
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 -!- 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:POY73046.1}.
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DR EMBL; PJQD01000042; POY73046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B8E3; -.
DR STRING; 741276.A0A2S5B8E3; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR032631; P-type_ATPase_N.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:POY73046.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..206
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 52598 MW; AF80CE0DE28C4601 CRC64;
MRNGGGGGKS GYGYAGSEAG TAQSVTDGGG DAHSEADSLL GGIEPDPNSR GTRRSGRTAR
GRRGEAAIPV GLGGRGESDG DFDAGWTNGL EAEEEEIGLL ASGRLDRDRP PTTGGPSPPG
KPTRTPSSFK RFFALSAPPS SQPRTIVLNE PPSKRKKAPH PPNIVKNQKY NLATFLPLVL
YEQFKFFYNL YFLLVALSQF VPALRIGFLA TYIVPLAFVL AVTIGKEAYD DYVRYLRDRS
ANSAKYSVLT SAAAPSPHSH HASSSNSSPA PLRPTPSADL RVGDLVHLDK NDRVPADVLL
LRTSDPSGTC FVRTDQLDGE TDWKLRVAVE KTQALATDAD LLQVGGEAYA DPPTKDIHTF
VGNITLRSWP TPAASGDDAA SQSQDGPIAA SNGDVVEPLT AENMLWANTV LAAGSAVGVV
VYTGRETRAV MNTSQPGTKV GLLDHEINRL AKILCAVTFV LSVVLVALNG FRGHWWVYVF
RFLILFSSII PIS
//
