ID A0A5J5EK55_9PEZI Unreviewed; 949 AA.
AC A0A5J5EK55;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Calcium-transporting ATPase 2 {ECO:0000256|ARBA:ARBA00067965};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE Flags: Fragment;
GN ORFNames=FN846DRAFT_785074 {ECO:0000313|EMBL:KAA8895457.1};
OS Sphaerosporella brunnea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Sphaerosporella.
OX NCBI_TaxID=1250544 {ECO:0000313|EMBL:KAA8895457.1, ECO:0000313|Proteomes:UP000326924};
RN [1] {ECO:0000313|EMBL:KAA8895457.1, ECO:0000313|Proteomes:UP000326924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb_GMNB300 {ECO:0000313|EMBL:KAA8895457.1,
RC ECO:0000313|Proteomes:UP000326924};
RG DOE Joint Genome Institute;
RA Benucci G.M., Marozzi G., Antonielli L., Sanchez S., Marco P., Wang X.,
RA Falini L.B., Barry K., Haridas S., Lipzen A., Labutti K., Grigoriev I.V.,
RA Murat C., Martin F., Albertini E., Donnini D., Bonito G.;
RT "Draft genome of the ectomycorrhizal ascomycete Sphaerosporella brunnea.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. Transports the calcium to
CC the vacuole and participates in the control of the cytosolic free
CC calcium. {ECO:0000256|ARBA:ARBA00059328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00048694};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004127}.
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:KAA8895457.1}.
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DR EMBL; VXIS01000263; KAA8895457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5EK55; -.
DR FunCoup; A0A5J5EK55; 462.
DR InParanoid; A0A5J5EK55; -.
DR OrthoDB; 3352408at2759; -.
DR Proteomes; UP000326924; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:TreeGrafter.
DR FunFam; 1.20.1110.10:FF:000039; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000031; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000018; Calcium-transporting ATPase; 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; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000326924};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 575..751
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 827..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAA8895457.1"
SQ SEQUENCE 949 AA; 103440 MW; DDC8E89A1D678169 CRC64;
HPNPHKLDPF ILSGAKVLEG VGTFLVTSVG VHSSFGKTMM ALREDSTATP LQMKLNDLAE
AIAKLGGAAA LLLFVVLLIR FLVNLRGNTA PPSEKGQSFM RILITAITVV VVAVPEGLPL
AVTLALAFAT TRMLKDNNLV RVLQACETMG NATTVCSDKT GTLTQNRMTV VAGTIGTTQR
FGDKRALKGD AAQSGDAEKD AQDLTIRDFV GSLPKDLKDI LLQSIVQNST AFEGEEDGVP
TFIGSKTETA MLTFARDYLG MSSVSEERAN AQVAQMVPFD SGRKCMGAVI RMPNGQFRLY
VKGASEIVLS KCTRIVTLEG PEAQLSEEIE KSINQTITGY AERSLRTIGM LYRDFPSWPP
AGARLSKDDS TQAHFDDVFN EMTWLGIVGI QDPLRPGVHE AVTQCQKAGV FVRMVTGDNV
TTAKAIAADC GIYTPGGVVM EGPKFRQLPP AEMDRIIPRL QVLARSSPED KRTLVRRLKE
LGETVAVTGD GTNDGPALKM ADVGFSMGIA GTEVAKEASA IILMDDNFSS IVKALMWGRA
VNDAVKKFLQ FQLTVNITAV LLTFVSAVAS TDETSVLSAV QLLWVNLIMD TFAALALATD
PPSPSILNRK PDPKSAPLIT INMWKMILGQ AVYQLVVTFT LNFAGRHILG YQDTPGENLQ
LKALIFNTFV WMQIFNQYNN RRLDNKFNIF EGVTRNWFFI AINLVMIGGQ VMIIFVGGQA
FSVTKLNGIQ WAISIILGAI SLPVAVIIRL IPDEMLEKIA PSFMLRKRDT TPVYVSADDR
FEWNRGIEEI RQELSFLKTV RGGRLNQLRF RPHDLSETVK ENFSHMFRSG SRSELQPSPT
GEDNQPPQTA VSHRRRRSRS NSTIAATIIM PSIVAGSVGG WSPVEKTPSP LREGSGNLPF
SSRSDLESQP GVTVHPDTAQ TDPVLPKQPP AENSVPSQQP GLTPESQHK
//
