ID A0A2T5M4K7_9EURO Unreviewed; 929 AA.
AC A0A2T5M4K7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=P175DRAFT_0530576 {ECO:0000313|EMBL:PTU23462.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU23462.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU23462.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU23462.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
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:PTU23462.1}.
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DR EMBL; MSFN02000002; PTU23462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5M4K7; -.
DR VEuPathDB; FungiDB:P175DRAFT_0530576; -.
DR OrthoDB; 1058547at2759; -.
DR Proteomes; UP000244073; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 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 110..132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 322..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 688..709
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 715..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 751..770
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 821..844
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 856..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 70..137
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 909..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 100989 MW; 657A26852BCAE227 CRC64;
MEANQLNIVE TKTALISGVQ DEKIVPLMED EDYEQEEHID SLIQDLESTD GDDIVYNVRK
SIEGSIKRAS AGRGPPIITS LETGLTDDQA SILRKRHGPN RMKEAKENMF LKFLSYFVGP
VQFVMEAAAI LAAGLKDWVD FGVICALLLL NASVGFIQEY QAGSIVDELK KTLALKATVL
RNGTLIEIDA TEVVPGDILK IDEGTIVCAD GRVETLNSLQ VDQSSITGES LAVDKRKDDV
CFASSVVKRG DGYLLITATG DKTLVGETAA LVNASSSNIG HFTEVLNRIG AVLLILVILT
LIIVWVSSFY RSNHTLTILE FTLAITMIGV PVGLPAVVTT TMAVGAAYLA KKQAIVQRLS
AIESLAGVEI LCSDKTGTLT KNKLSLSEPY TVAGVDPDDL MLTACLAASR KKKGMDAIDR
AFFKALPDYP RAKSALTQYR VREFCPFDPV SKKVTAVVLS PQGQEIICVK GAPLVVLNTV
LKEQQVPEHV DIEYKNKVSE FAVRGFRSLG VARKRGDGPW EILGIVPCSD PPRHDTAKTI
SEAKTLGLSI KMLTGDAVGI ARETSRQLGL GTNVYNAERL GLGGGGTMPG SEVYDFVEAA
DGFAEVFPQH KYNVVEILQQ RGYLVAMTGD GVNDAPSLKK ADTGIAVEGA SDAARSAADI
VFLAPGLSAI IDALKTSRQI FHRMYAYVIY RIALSLHLEI FLGLWIAIMN ESLNLQLVVF
IAIFADIATL AIAYDNAPYS KTPVKWNLPK LWGLSVVLGI VLAVGTWVAL TTMLNEGEHG
GIVQNFGKRD EVLFLEISLT ENWLIFITRA NGPFWSSCPS WQLLAAIVVV DLVATFFCIF
GWFVGGQTSV VAVFRIWVFS FGVFCIMGGI YYLLQGSTAF DDIMHGRSPR RREGTRRSLE
DFLVVLQRVS SQHEKSSLSP ENGQAGRRG
//
