ID A0A1J9PVK9_9EURO Unreviewed; 929 AA.
AC A0A1J9PVK9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=ACJ73_09438 {ECO:0000313|EMBL:OJD11915.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD11915.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD11915.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD11915.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) 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:OJD11915.1}.
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DR EMBL; LGTZ01002665; OJD11915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PVK9; -.
DR STRING; 1658174.A0A1J9PVK9; -.
DR VEuPathDB; FungiDB:ACJ73_09438; -.
DR OrthoDB; 1058547at2759; -.
DR Proteomes; UP000242791; 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:SF26; PLASMA MEMBRANE ATPASE 1-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 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:UP000242791};
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 121..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 335..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 728..747
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 768..786
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 836..857
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 863..887
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 78..149
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 100327 MW; 626DD59DE70B0E65 CRC64;
MSDPTASGPQ GHGIPPNHLG TNVPSGEFSE KATEPVPNEK KPPVPEDDDE DEDMDALIEE
LESQDGHIDV EDEDDGEPGS ARPVPEELLN TDTRQGLTDA EVTARRKKYG LNQMKEEKEN
LVLKFLSYFV GPIQFVMEAA AILAAGLEDW VDFGVICGLL LLNACVGFVQ EFQAGSIVDE
LKKTLALKAV VLRNGRLTEI EAPEVVPGDI LQVEEGTIIP ADGRIVTEEA FLQVDQSAIT
GESLAVDKHK GDTCYASSAV KRGEAFMVIT STGDNTFVGR AAALVNAAAA GTGHFTEVLN
GIGTVLLILV ILTLLVVWVS SFYRSNDIVT ILEFTLAITI IGVPVGLPAV VTTTMAVGAA
YLAKKKAIVQ KLSAIESLAG VEILCSDKTG TLTKNKLSLA EPYCVAGVDP EDLMLTACLA
ASRKKKGIDA IDKAFLKSLR YYPRAKSVLT QYKVLEFHPF DPVSKKVSAV VVSPQGERIT
CVKGAPLFVL KTVEEDHPIP EEVDNAYKNK VAEFATRGFR SLGVARKRGE GSWEILGIMP
CSDPPRHDTA KTINEAKTLG LSIKMLTGDA VGIARETSRQ LGLGTNVYNA ERLGLGGGGT
MPGSEVYDFV EAADGFAEVF PQHKYNVVEI LQQRGYLVAM TGDGVNDAPS LKKADTGIAV
EGASDAARSA ADIVFLAPGL SAIIDALKTS RQIFHRMYAY VVYRIALSLH LEIFLGLWIA
ILNTSLNLEL VVFIAIFADI ATLAIAYDNA PFSKTPVKWN LPKLWGMSVL LGIVLAIGTW
ITLTTMLVGS ENGGIVQNFG VRDEVLFLQI SLTENWLIFI TRANGPFWSS IPSWQLAGAI
LVVDIVATFF TLFGWFVGGQ TSIVAVVRVW IFSFGCFCVL GGLYYLLQGS TGFDNMMHGK
SPKKNQKQRS LEDFVVSLQR VSTQHEKSS
//
