ID A0A0L0G9X5_9EUKA Unreviewed; 1053 AA.
AC A0A0L0G9X5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=SARC_02115 {ECO:0000313|EMBL:KNC85704.1};
OS Sphaeroforma arctica JP610.
OC Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC85704.1, ECO:0000313|Proteomes:UP000054560};
RN [1] {ECO:0000313|EMBL:KNC85704.1, ECO:0000313|Proteomes:UP000054560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP610 {ECO:0000313|EMBL:KNC85704.1,
RC ECO:0000313|Proteomes:UP000054560};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Sphaeroforma arctica JP610.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362083}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ241688; KNC85704.1; -; Genomic_DNA.
DR RefSeq; XP_014159606.1; XM_014304131.1.
DR AlphaFoldDB; A0A0L0G9X5; -.
DR STRING; 667725.A0A0L0G9X5; -.
DR EnsemblProtists; KNC85704; KNC85704; SARC_02115.
DR GeneID; 25902619; -.
DR eggNOG; KOG0205; Eukaryota.
DR OrthoDB; 46741at2759; -.
DR Proteomes; UP000054560; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054560};
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 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 366..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 756..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 796..818
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 910..932
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 99..171
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 114429 MW; 42A3E3426AE5E030 CRC64;
MANETPDAGS DSAITDTNVV NGLTTASNTT EPTDARDEAI VDEPVSAAAE ELHPEPKTTA
GEELTIKKDP SIHDLPNCEP PKPTSVDVPM ATGDGGDNDY KNLTQEAALR KLESSKDGLT
TKEYEQRLQQ YGPNALPTVE KNKLWEFFKF LWNPLSWAME VAAILSIILL DYVDFVLIII
LLLLNAAIGY KEEAAAGDAI SALAASLAPK AKVYRDGAIV TIEAINLVPG DVILVRLGDV
IPADIKLLGE DHQEPCQIDQ AALTGESLPV KRFVGECAYS GSTVKQGETR GLVYATGANS
FFGKAAALIN GTENPGHLQQ VMTTIGATCI ITIIFWAVIE LGVQFGHYDH GCSLGSQGSC
PTLSNLLVII VGGIPIAMPT VLSVTLALGA SALAKHGAIV SRLTAIEEMA GMDMLCSDKT
GTLTLNQLSV DKPNLKAQES AGFTQGDICL YGALGAKIEN EEPIDLCCHE AYDGKDTLWD
NYTCIKYVPF NPNDKRTIAT IKPKDGSEIF RCTKGAPQVI LKMAHNYEEI KNQFEDTILE
YAGRGYRALG VGKSMGEDSE KWEFVGLIPI FDPPRHDTKD TIEKCIELGI GVKMITGDQL
PIGIETARQL GMGTNMYTTE VLNEGHGEHK LIKGALTLDD LIEQADGFAE VFPEHKYEIV
ARLQKMGHIT AMTGDGVNDA PALKKADIGI AVADATDAAR AASDIVLTES GLGVIIHAII
EARKIFGRMK SYAKYTIAMT FRICFTFGLL TTIYNWYFPT ILIVLLAIFN DGAMISLSKD
RVSPNHNPDA WFLKKLFIAG LIYGLYLTLS SWVLFYVASH TNFFEGGSAL NLSPSLYYTD
SSNYCLTQTD ATTGAIITAG TQAYTLCVTE VTWERQSRLR ALMYSQVSIS GMALIFITRT
SKISWMDRPG MSILAAFIFS QVVSSLIAGF GFDGYERPDP SQLCVYCEDY TAAAPIPGDN
ESRFNASLLG CGIWVLISWI WCIIWYVPMD LIKMVLQYVM DEEKPVFFVQ KDVVNPHFQG
SISRASSLGR PRNGASVSTG NPRASRVVRG SVM
//
