ID A0A2S7QH72_9HELO Unreviewed; 1125 AA.
AC A0A2S7QH72;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=CJF30_00000617 {ECO:0000313|EMBL:PQE25881.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE25881.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE25881.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE25881.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361146}; Multi-
CC pass membrane protein {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}.
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:PQE25881.1}.
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DR EMBL; NJPT01000014; PQE25881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7QH72; -.
DR STRING; 2070414.A0A2S7QH72; -.
DR Proteomes; UP000238072; Unassembled WGS sequence.
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 CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 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: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; 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 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|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|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000238072};
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 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 251..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 771..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 881..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 728..903
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 329..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 122964 MW; 6142A27ED00BF689 CRC64;
MWITYNDKVL ILLSIAAAIS LAVGLYQTFG TKHDPEHPPI EWVEGVAIIV AIVVVVVVGS
LNDYQKERQF VKLNKKKEDR DVNVIRSGKT MEISVFDVLV GDVMHLEPGD MIPVDGIFIE
GHNVICNESQ ATGESDLIRK RPADDVFAAI KNHDSLRKMD PFILSGAQVN EGVGTFLVTA
TGVNSMYGKT LVSLREDPES TPLQSKLNTL AEYIAKLGGA AGLLLFIVLF IEFLVRLPHN
HHTPTEKGQE FLSIFIVTVT IIVVAVPEGL PLAVTLALAF ATTHNNLVRH LKACEVMGNA
TTICSDKTGT LTQNKMLVVA GTVGTSSRFG GTVETSGDDD VSKGKQPQRE GENITANEVV
STFDPSVKEL IKQSVVLNST AFEGEVDGEQ TFVGSKTETA LLLFAREHLG TGPLAEERSN
VTITQLIPFD SGRKCMGVVV QLDNGKYRLY VKGASEILLE KCSNIIRDPT KDVSSVPMTD
ENRQTLTSLI DNYASRSLRT IALIYRDFDK WPVKGARLVE GEKDQVVFED IFKNMVLLGI
VGIQDPLRDG VPEAVRTCQN AGVVVRMVTG DNMVTAKAIA TECGIYTPGG IVMEGPAFRN
LSAAKKEQII PRLQVLARSS PKDKEDLVKA LKQLGETVAV TGDGTNDAPA LKKADVGFSM
GIAGTEVAKE ASAIILMDDN FNSIVKAMMW GRAVNDAVKK FLQFQLTVNI TAVLLTFITA
VSSSKEESVL TAVQLLWVNL IMDTMAALAL ATDPPTPSIL NRKPDPKSAP LITMTMWKMI
IGQAIYQLVI TLLVYFGSKS ILSYTSDREM EQLPALVFNT FVWMQIFNQW NNRRLDNKFN
ILEGVSKNWF FIGINVVMVG GQVLIMFVGG DAFNIKRRLN AAQWAYSIVL GFLSIPVGAS
IRLIPDELLI SLIPSYLKNR PKAPEVTISD EEEHFRFPKP LADVKEELSF LKKVKGGRLN
NLKFAIQQTR DQIMPRSRSG SRSRSNSIPH TPGGDSQRED SFGAAPHPTP ESRKRGRSTR
SRSNSALGAT TVMAGIIAGS VAGWSPIERN YNESDGMGFT RSRGRSELEQ SNEVEIHPDT
KPDDPVITED PAHLSAPPSQ IPEITPIPAS EVPTLSIPTP RKSSK
//
