ID A0A9P5BFJ2_9HYPO Unreviewed; 1242 AA.
AC A0A9P5BFJ2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=FAGAP_3399 {ECO:0000313|EMBL:KAF4500373.1};
OS Fusarium agapanthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1803897 {ECO:0000313|EMBL:KAF4500373.1, ECO:0000313|Proteomes:UP000737391};
RN [1] {ECO:0000313|EMBL:KAF4500373.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 31653 {ECO:0000313|EMBL:KAF4500373.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (JAN-2020) 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 -!- 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 ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU361146}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|ARBA:ARBA00038148, 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:KAF4500373.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LUFC02000198; KAF4500373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P5BFJ2; -.
DR OrthoDB; 3352408at2759; -.
DR Proteomes; UP000737391; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005774; C:vacuolar 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: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 CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR FunFam; 1.20.1110.10:FF:000002; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000039; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000028; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000018; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000001; Phospholipid-transporting ATPase IC; 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; 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; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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; 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 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:UP000737391};
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};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 194..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 438..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 967..993
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1005..1022
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1042..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1073..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 162..205
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 264..379
FT /note="P-type ATPase A"
FT /evidence="ECO:0000259|Pfam:PF00122"
FT DOMAIN 924..1095
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 135673 MW; AE5E4F5992B9229F CRC64;
MDSSTPRRPR APTITVDTAA VDSSDPVPTA KSRTESWSSS PSTKVGTDHE QMSREVEALR
KGDQAEILKP DPGEEDLFHV EDNPFAFSPG QLAKLINPKN LAAFVALGGL PGLQKGLRTD
AKAGLSVDEG KLAGVVSFEE ATSSKVENTT HSDAHASGTD AFPDRKRVYG ANRLPEPKSK
SFFELAWIAL QDRVLILLCI AAVVSLALGL YQTFGGSHED GGAKVEWVEG VAIIVAITIV
VVVGAANDWQ KERQFQKLNQ KKEDRIVKIT RSGKPQNISI HDVLVGDVML LEPGDVIPVD
GVFIEGHNLS CDESSATGES DLMKKVPAEQ VLHALLHEQA PKLKKLDPFI ISGAKVLDGV
GTFLVTAVGE QSSHGKTMMS LRDDPGLTPL QAKLNLLAGY IAKLGSAAGL LLFFVLLIEF
LARLPNNRES GEQKGQDFLQ ILITSITVIV VAVPEGLPLA VTLSLAFATK KMTRENNLVR
HLQSCETMGN ATVICSDKTG TLTENIMTVV AGSLGIRGLF SFGDSSFEKE SAGAEKRETI
ALAQFATKLD PEYKELLKTA ITVNTTAFEL DEEGKQGFVG TKTETALLDW ARRYLGLGPL
AIERANHPIT RLFPFNSQRK CMGAVVQIPG PTKDKPKYRL YIKGASEIVL GECTAILGDP
TTAPTTEALS DDGKEELRSI IFNYATNSLR TLGLAYRDFE NWPPVLTLRP EDDNADIDLT
DLVHNLTWMG VVGIQDPVRK GVPEAVNDCG IASVNVKMVT GDNVETARAI ALKCGILTES
TINEPNAVMQ GSDFRKLSES DRTAVVKKLR VLARSSPEDK RILVKTLRSL GEIVAVTGDG
TNDAPALKAA DVGFSMGVTG TEVAKEASDI ILMDDNFSSI VVALGWGRAI NDSVKKFLQF
QLTVNITAVG VTFISAVSDD EQKSVFNAVQ LLWVNLIMDT FAALALATDP PTGSLLHRKP
EARTTPLITI TMWKMIIGQS IYQLIVCFVL WFGRDAILGY DERKVRSLIF NIFVFMQIFK
LINSRRIDNK LNIFEGLHRN HLFMLMMTIM AAGQIIIIFF GGDAFVVTRL NGVQWGISLV
LGFFSIPIGV LIRLFPDEWF HAFVKVLAKL WPSWIRFSRK KKDTSEEDGT EPFPKEKLEG
YDMDTALLGI RDDLEFLKRV RGGRMTALSD AMARSREKML RRKRSESRPR SKLRSRRGSS
RSSNRPPISP MMSVVGMPGI VAASVAGLQP GQCASNENLE AR
//
