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Database: UniProt
Entry: A0A439D6Q9_9PEZI
LinkDB: A0A439D6Q9_9PEZI
Original site: A0A439D6Q9_9PEZI 
ID   A0A439D6Q9_9PEZI        Unreviewed;      1067 AA.
AC   A0A439D6Q9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   ORFNames=EKO27_g5040 {ECO:0000313|EMBL:RWA10080.1};
OS   Xylaria grammica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA10080.1, ECO:0000313|Proteomes:UP000286045};
RN   [1] {ECO:0000313|EMBL:RWA10080.1, ECO:0000313|Proteomes:UP000286045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHI A82 {ECO:0000313|EMBL:RWA10080.1,
RC   ECO:0000313|Proteomes:UP000286045};
RA   Buettner E., Kellner H.;
RT   "Draft genome sequence of Xylaria grammica IHI A82.";
RL   Submitted (DEC-2018) 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:RWA10080.1}.
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DR   EMBL; RYZI01000128; RWA10080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A439D6Q9; -.
DR   STRING; 363999.A0A439D6Q9; -.
DR   Proteomes; UP000286045; 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   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; 2.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
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; 2.
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; 2.
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:UP000286045};
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        166..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        191..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        397..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        439..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        838..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        872..890
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        938..958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        984..1008
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          120..190
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  117392 MW;  02744ABEB0C58DAA CRC64;
     MSFLASRRPH NTAADDVEAN AAARHNEPEI TTAEHAVTTG AGGGGNEQEE HVTFGEHRLK
     PPPKSSDLGE FEALDRYITT FEAERRASLV STVRSVKKRK WWQFWQSDKA APKVQAQPAA
     VVGQPPDSWL ETDIHHGITS AAVEERRKRF GWNELTSEKE NTLSKIFGYF TGPILYVMEL
     AALLAAGLQD WIDFGVILGI LALNAFVGFY QEKQAADVVA SLKGDIAMKA MVIRDGREQQ
     ILARELVPGD IVIIQEGQTV PGDAQLICDY NRTQDFDQYR ELKNEDKFNE EGGEANDKKE
     KEKVGDDNGK GEKGQDEDDE GSEGSIHYGD SLVACDQSAI TGESLAVDKY MGDTIYYTTG
     CKRGKAYAII LTSAKHSFVG RTAELVQGAR DQGHFKAVMN SIGTSLLVLV MFWILAAWIG
     GFYHNLRIAQ PHVQNLLHYT LVLLIIGVPV GLPVVTTTTL AVGAAYLAKQ KAIVQKLTAI
     ESLAGVNVLC SDKTGTLTAN KLSLREPYVA EGQDVNWMMA VAALASSHNV ASLDPIDKVT
     ITTLKKYPKA REILRQGWKT DKFTPFDPVS KRITSYCRLG EDRYICAKGA PRAILALADV
     DKETSRNYNA KAKEFAQRGF RSLGVAYKKN DEPWVLQGLL SMFDPPREDT AQTIIEAVHL
     GVPVKMLTGD AIAIAKETCK MLGLGTKVYN SEKLIHSGLT GTVQHDLVQR ADGFAEVFPE
     HKYQVVEMLQ QRGSLTAMTG DGVNDAPSLK KADCGIAVEG SSEAAQAAAD IVFLAPGLST
     IILSIKTARQ CLDSTLTPGQ IFQRMKSYVQ YRIALCLHLE IYLTTSMIIL NETIRPDLIV
     FIALFADLAT VAVAYDNAHV EPRPVEWQLK KIWVISVILG ALLAAGTWII RGTMFLRSGG
     IIENFGSIQE VLFLEVALTE NWLIFVTRGG QTWPSWQLVG AIFGVDVLAT LFCLFGWLSG
     SGGGVMRTTP PDQFHNSGNG WTDIVTVVVV WAYSIGVVIF IAIVYLALNS FQWVKDLGRQ
     DRNKKDSYIE NIIGHINKLA LEHEPDPKTG HDKYYIVEKA TTEEEDL
//
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