ID A0A1Y1Y3G6_9FUNG Unreviewed; 897 AA.
AC A0A1Y1Y3G6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=K493DRAFT_316535 {ECO:0000313|EMBL:ORX92533.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX92533.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX92533.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX92533.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC ion pump. The proton gradient it generates drives the active transport
CC of nutrients by H(+)-symport. The resulting external acidification
CC and/or internal alkinization may mediate growth responses.
CC {ECO:0000256|ARBA:ARBA00003417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC Evidence={ECO:0000256|RuleBase:RU362083};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC ECO:0000256|RuleBase:RU362083}.
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:ORX92533.1}.
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DR EMBL; MCFE01000271; ORX92533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1Y3G6; -.
DR STRING; 1314790.A0A1Y1Y3G6; -.
DR InParanoid; A0A1Y1Y3G6; -.
DR OrthoDB; 1058547at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW Ion transport {ECO:0000256|RuleBase:RU362083};
KW Magnesium {ECO:0000256|RuleBase:RU362083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362083};
KW Reference proteome {ECO:0000313|Proteomes:UP000193498};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362083};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 282..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 676..695
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 707..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 774..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 804..827
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 18..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 897 AA; 98467 MW; FCAE7B4CAD6BC5E0 CRC64;
MPVEEEKNKV ELEDHKHQEM AEEIPPELEA LLHTDPAKGL TSAEVAQRLE QFGRNELSEK
KKNPFLKFLG YFTGAIAYLI EIAWILSGVV QDWANFGIIG ALLFINAAIG FIEESKAENA
LDALKNTLAL KTRVWRDGEL NEIDVVDLVP GDVIVLRLGD IVPADCRLLG IGVHGEPVEG
NLQIDQSALT GESLPVSKGK GATAYSSSIV KQGQQMGVVT KTGEHTFIGR AATLMSNTNE
QGHFQKIINR IGNFLVLVTI LLVVIIFIVL MVKDKGHNVL DILRQVLVLT VAAIPVGLPT
VMSVTMAVGA KQLAKKEVIV KRLTAVEEMA SVSVLCSDKT GTLTLNELTF DEPWLCKGYT
SDDILMYSYM AAEQGANDPI EYAVRTAARA QLDTLQSLGE KETKIPGFKT TSFLPFNPVT
KLTQATILNE ETGEVFKVAK GAPQVIIKLV GGNDDAIHAV NSLARRGLRA LGVARTINGD
IEQWELIGMI SLLDPPRPDS AATIARCHEM GVSVKMITGD QLIIAKEVAQ RLGMQRAILE
AQKLVEADVP EEEIVRRCVK ADGFAQVVPE HKYRVVELLQ EQGLLVGMTG DGVNDAPALK
KANVGIAVHG CTDAARSASD IVLLAPGLST IVDGITTSRA IFQRMRSYAL YRITSTIHFL
LFFFFVTIIF QWQLDAILLI FIAVLNDAAT LVISVDNAQI SAKPDKWRIG QLITMSFTLA
VFLTGASFAH FFIARDVFNV TNDELGTIMY LHISSCPHFV IFSTRLSGFF WENLPSWTFT
IAILGTQVFA MLISVFGVPG LTTAIGWGWG CSVIAISLGY FVVLDFVKVF MFRIWSFELT
AKLWPTPTRR RKLSARKIEK ELNTRVTSNI EKVRTAVRAI HAINLLQNGN TSEKTTH
//
