UniProt: A0A2Z6LQY8

Database: UniProt
Entry: A0A2Z6LQY8_TRISU

LinkDB:  A0A2Z6LQY8_TRISU 
Original site:  A0A2Z6LQY8_TRISU

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (13)   
   Pfam (5)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   A0A2Z6LQY8_TRISU        Unreviewed;      1037 AA.
AC   A0A2Z6LQY8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 31.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=TSUD_79390 {ECO:0000313|EMBL:GAU19116.1};
OS   Trifolium subterraneum (Subterranean clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=3900 {ECO:0000313|EMBL:GAU19116.1, ECO:0000313|Proteomes:UP000242715};
RN   [1] {ECO:0000313|Proteomes:UP000242715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Daliak {ECO:0000313|Proteomes:UP000242715};
RX   PubMed=28928752; DOI=10.3389/fpls.2017.01463;
RA   Kaur P., Appels R., Bayer P.E., Keeble-Gagnere G., Wang J., Hirakawa H.,
RA   Shirasawa K., Vercoe P., Stefanova K., Durmic Z., Nichols P., Revell C.,
RA   Isobe S.N., Edwards D., Erskine W.;
RT   "Climate Clever Clovers: New Paradigm to Reduce the Environmental Footprint
RT   of Ruminants by Breeding Low Methanogenic Forages Utilizing Haplotype
RT   Variation.";
RL   Front. Plant Sci. 8:1463-1463(2017).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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         ECO:0000256|RuleBase:RU361146};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; DF973194; GAU19116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6LQY8; -.
DR   OrthoDB; 3352408at2759; -.
DR   Proteomes; UP000242715; Unassembled WGS sequence.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   FunFam; 1.20.1110.10:FF:000039; Calcium-transporting ATPase; 1.
DR   FunFam; 1.20.5.170:FF:000026; Calcium-transporting ATPase; 1.
DR   FunFam; 2.70.150.10:FF:000006; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000011; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000011; Calcium-transporting ATPase; 1.
DR   Gene3D; 1.20.5.170; -; 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; 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; IPR059000; ATPase_P-type_domA.
DR   InterPro; IPR024750; Ca_ATPase_N_dom.
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; 3.
DR   PANTHER; PTHR24093:SF462; CALCIUM-TRANSPORTING ATPASE 11, PLASMA MEMBRANE-TYPE-RELATED; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF12515; CaATP_NAI; 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   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242715};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        159..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        352..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        394..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        818..838
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        912..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        958..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        989..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          109..187
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1037 AA;  113613 MW;  DD7212397621AFE4 CRC64;
     MEWNLLKDFE LEPKNRSVEA LRRWRSAVTL VKNRRRRFRM VADLDKRSEA EQIKQGIKEK
     IRIALYVQKA ALQFIDAGNR VEYKLSQEAI EAGFDIHPNE IASIVRSQDY KNLSNNGGVE
     AVARKLSVST DEGVSEASVD CRQQIFGANR YTEKPSRSFL MFVWDALQDL TLTILMVCAV
     VSIGIGLATE GWPKGTYDGV GIILSIFLVV IVTAVSDYKQ SLQFLDLDKE KKKIFVHVTR
     DGKRKKISIY DIVVGDIVHL STGDQVPADG IYISGYSLLI DESSLSGESE PVFITEKHPF
     LLSGTKVQDG QGKMLVTTVG MRTEWGKLME TLNEGGEDET PLQVKLNGVA TIIGKIGLAF
     AIVTFLVLTI RFLVEKVLHG EFSNWSSNDA TKLLDFFAIA VTIIVVAVPE GLPLAVTLSL
     AFAMKKLMND MALVRHLSAC ETMGSASCIC TDKTGTLTTN HMVVNKIWIC EKTTQLKGNE
     SADELKTNIN EGVLSILSQA IFQNTSAEVV KDKNGKNTIL GSPTESALLE FGLLLGSDFD
     ARNRSKAYKI LKLEPFNSVR KKMSVLIGLP DGRVQAFCKG ASEIILNMCD KIIDCNGEVI
     DLPADRASNV SDVINSFASE ALRTLCLAVK DINETQGEPN IPDSGYTLIA LVGIKDPVRP
     GVKEAVQTCI AAGITVRMVT GDNINTAKAI AKECGILTDD GVAIEGPTFR ELSDGQMKDI
     IPRIQVMARS LPLDKHKLVT NLRNMFGEIV AVTGDGTNDA PALHESDIGL AMGIAGTEVA
     KEKADVIIMD DNFATIVNVV KWGRAVYINI QKFVQFQLTV NVVALIINFV SACITGSAPL
     TAVQLLWVNL IMDTLGALAL ATEPPNDGLL KRPPVGRGAS FITKTMWRNI IGQSIYQLIV
     LAILNFDGKR LLGIYGSDAT EVLNTLIFNS FVFCQVFNEI NSRDMEKINI FKGMFDSWIF
     LMIIFATIAF QVVIVEFLGA FASTVPLNWQ FWLLSVLIGA ISMPIAVILK CIPVETKNTS
     NQNHDGYEAL PSGPELA
//

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