ID A0A2T9Y382_9FUNG Unreviewed; 911 AA.
AC A0A2T9Y382;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=BB559_006403 {ECO:0000313|EMBL:PVU86805.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU86805.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU86805.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU86805.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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:PVU86805.1}.
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DR EMBL; MBFT01000842; PVU86805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9Y382; -.
DR STRING; 61424.A0A2T9Y382; -.
DR Proteomes; UP000245699; 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 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:UP000245699};
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 62..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 652..673
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 710..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 792..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 825..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 17..89
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 911 AA; 101193 MW; D7C7F462EE518422 CRC64;
MSYDSRETFN NEKEIVFDNS IPPELECLLY TNPTYGLTAY EHAERLEKFG RNEIKERKRN
PFIHFFSFFT GSIAYLIEIA LILTGITRDW VNFGIILLLL FVNAFVGWFE ESKAESTVEA
LKNTLAIKTK VWRSGNLIDV DSSTLVPGDI IIVRLGDIVP ADAVLLGIGV DGSRTEVDLM
LDQAGLTGES LPVVKTKGDT IYSSSIVKQG QMAAVVVKTG TSTFIGRAAN LIAITNEQGH
FQKIIGTIGN FLVWTTVTMV LIIFTFLVLK RRNLNGGIIS KKDILDTLED VVVLTVAAIP
VGLPTVLSVT MTVGSKQLAK KHVIVKRLAA VEEMASISVL CSDKTGTLTL NELTFDKPFL
KKDFNEEELL FFSYLAAEPG TTDPIELAVR TAATTKVPML KNLSSHNVPG YKVVSFLPFN
PSTKMTQATI KNLKAQESFR VAKGAPQVII NLCGGDEEAT DAVNEFAYRG LRALGVAINY
FDVEDKWILV GMISLLDPPR PDSAETIARC EELGISVKMI TGDQQVIAKE VARRLGMQRT
ILDASMIVNP LESEETITER CIAADGFAHV IPEHKFRVVE LLQNKGILVA MTGDGVNDAP
ALKKANVGIA VHGCTDAARA AADIVLLEPG LSTIIDGILT SRAIFQRMRS YALYRITSTV
HFLLFFFIIT LWLSWQMSSF LLILIAVLND AATIVIAFDN SEVSQKPDKW RIGQLITLSV
ILGVCLCLLT FGVFFVARDI YGIPAYSKLM PMIEILDNRM QSIIYLNISS APHFQIFSTR
LSGFFFENLP SLSFFSIIMA TQLIATIICS VGIEGMVQKI GFKWGLSLLA ISFVYFMILD
VIKVYIMRYW SFELVTNLWP TKSNRRKLQR KKEKEATKTR VSRNVSKVRN VVRVISMIPV
LKNHMAKRRI H
//
