ID A0A059B7H5_EUCGR Unreviewed; 986 AA.
AC A0A059B7H5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_H04358 {ECO:0000313|EMBL:KCW61620.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW61620.1};
RN [1] {ECO:0000313|EMBL:KCW61620.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW61620.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
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:ARBA00000363};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124}.
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DR EMBL; KK198760; KCW61620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059B7H5; -.
DR EnsemblPlants; KCW61620; KCW61620; EUGRSUZ_H04358.
DR Gramene; KCW61620; KCW61620; EUGRSUZ_H04358.
DR eggNOG; KOG0204; Eukaryota.
DR InParanoid; A0A059B7H5; -.
DR OMA; MWIAFND; -.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
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; 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; 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:SF509; 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; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
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:ARBA00022568};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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:ARBA00022568}.
FT TRANSMEM 145..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..985
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..162
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT NON_TER 986
FT /evidence="ECO:0000313|EMBL:KCW61620.1"
SQ SEQUENCE 986 AA; 108446 MW; 9ED6A7940C3C42B1 CRC64;
MSSLRLRKPS EEAATDAVLN RGDGPTIIIH RRRWRLAFLV IYFTRALESL SKQNSDNPRE
GDCPSLPDVG PKILSNLVRE KSFESLAQIG GVKRLASILM TNLENGLSGD ETDLMRRTNI
FGANKYNKPP AKSFLSFVLD AFKDMIIIIL IACAVLSLAF GIKQHGLKEG WYDGGSIIIA
IFLVVIVSAV SNYKQGKQFR ELSKESSNIR VEVVRDGRRQ PISIFDIVVG DVVYLKIGDQ
VPTDGLFVDG HSLRVDESSM TGESDHIEVN RENPFLLSGT KVIDGYGRMM VASVGMNTAW
GKMMSSVSRD LDEETPLQAR LNKLTSLIGK VGVSVAVLVL LVSMIRYFTG HTQDDAGNRE
FTSGKTKLED VMDAVVRIVA AAVTIVVVAI PEGLPLAVTL TLAYSMKRMM GDNAMVRKLS
ACETMGSATM ICTDKTGTLT LNEMRVTELC MGKEHVSVDA SKEIATGIVE VLLQGIGLNT
TGTVHMRPSE SVPEILGSPT EKAILSWGVS KLGMTMDELK QEWEIVQVEA FNSEKKRSGV
AVRRRGEQVV HIHWKGAAEM ILAMCSDYYS QSGTVNVMTD EARSDFGTAI KNMADKSLRC
IAFAYKKFDG SLAQFHGKLE EDGLTLLGIV GIKDPCRPGV RRAVVSCRSA GVNIKMITGD
NMHTARAIAL ECGIFNPEED LEHEAIVEGV QFRNYSPEQR VAAIEKIRVM ARSSPFDKLL
MVQCLKQKGH VVAVTGDGTN DAPALKEADI GLSMGIQGTE VAKESSDIVI LDDNFASVVT
VLRWGRCVYN NIQKFIQFQL TVNVAALVIN FVAAVSSGNV PLTAVQLLWV NLIMDTLGAL
ALATEQPTND LMLKPPVGRT EPLISRVMWR NLISQALYQV IILLTLQFKG SSIFGVDKKV
RDTIIFNCFV LCQVFNEFNA RKLEEKNVFK GIHKNKLFLG IVGMTIILQV VMVEFLKRFA
NTERLDWGQW GACIGLAALS WPICWL
//
