ID M1VI70_CYAM1 Unreviewed; 1005 AA.
AC M1VI70;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=CYME_CMT241C {ECO:0000313|EMBL:BAM83222.1};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM83222.1, ECO:0000313|Proteomes:UP000007014};
RN [1] {ECO:0000313|EMBL:BAM83222.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM83222.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=15071595; DOI=10.1038/nature02398;
RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA Kuroiwa T.;
RT "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT merolae 10D.";
RL Nature 428:653-657(2004).
RN [2] {ECO:0000313|EMBL:BAM83222.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM83222.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT "A 100%-complete sequence reveals unusually simple genomic features in the
RT hot-spring red alga Cyanidioschyzon merolae.";
RL BMC Biol. 5:28-28(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
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|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. {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; AP006502; BAM83222.1; -; Genomic_DNA.
DR RefSeq; XP_005539258.1; XM_005539201.1.
DR AlphaFoldDB; M1VI70; -.
DR STRING; 280699.M1VI70; -.
DR EnsemblPlants; CMT241CT; CMT241CT; CMT241C.
DR GeneID; 16997976; -.
DR Gramene; CMT241CT; CMT241CT; CMT241C.
DR KEGG; cme:CYME_CMT241C; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_2_1; -.
DR OMA; YDPMEKA; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000007014; Chromosome 20.
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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 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; PR00121; NAKATPASE.
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 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|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000007014};
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}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 292..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 762..783
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 933..956
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1005 AA; 111126 MW; 284462DDB85C797E CRC64;
MEDAFCRTAE EVLEAFQVRK DYGLTEEQVA LYAQRYGRNV TAREESAPLW QLVVKQFQDQ
LVLILLGAAG ISFILALFED DEDRVTAFFE PLVIVLILAA NATVGVIQET NAEKAIEALR
EYEPDDATVL RCGELRRVRS EELVPGDIIE VSVGMRVPAD CRIIELASTV LYADQSVLTG
ESISVSKSPE AITDTQCMIQ DKTCLLFAGC TIVRGKARCV VTQVGERTEI GKVRRNIAET
KAVMTPLKRR LDEFGSLLSK IILLICVLVW LINIRNFWNP EHGGFLRGAV YYFKIAVALA
VAAIPEGLPA VVTTCLALGT KRMARKNAIV RSLPSVETLG CTSVICSDKT GTITTNRMCV
TRVLLVSDVL PAGDGKLLDL EVTGHGDFSP FGNVVYNGSV LESPLKSLPP LAELSIAATF
CNDASITFNM KGRQYDKIGE GTEAALITLV EKLRTPDEHY NAEISHMPLV QRATATRAYW
NRLFERVATL EFTRDRKSMS VFCRRLSDES LHMFVKGAPE RILENSDYVC IGNGMRIPIT
PVLRRQLLDA VASLSSGVHA LRTLAIATRD HPPALETVDM RDTQSFARYE SNLTFIGLVG
MIDPPREEVR AAIETCALAG IRVIVITGDN KATAEAICRQ VGIFDDYEDL SGKSYTGREF
ELLPEDARRQ VVRRARLFAR VEPLCKQRIV TLLQERGEVV AVTGDGVNDA PALKAADIGI
SMGTGTAVAK GAADMVLGDD NFATIVAAVE EGRAIYENMR QFIRYLISSN IGEVWCVFLT
AVLHTPEALA PVQLLWVNLV TDGLPATALS FNRPAKNIMQ QPPRPSNEHI VNGWLLFRYL
VIGTYVGVAT IAGLIWWYMF YAGGPQLSWS ELRLHRQCQS GNDLGTGLAI SCDIFRSRHP
STVSLSILVT IEMLNALNSL AENESITIVG PWTNPFLVLA ICLSLALHAI ILYVPFFNRV
FATAPLDFQE WVAVLWLSLP VVWLDEGLKY FSRLQKRRQT IKKMR
//
