ID A0A9W4MTG4_PENOL Unreviewed; 1026 AA.
AC A0A9W4MTG4;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=POLS_LOCUS5726 {ECO:0000313|EMBL:CAG8138463.1};
OS Penicillium olsonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=99116 {ECO:0000313|EMBL:CAG8138463.1, ECO:0000313|Proteomes:UP001153618};
RN [1] {ECO:0000313|EMBL:CAG8138463.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) 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=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|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004127}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {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:CAG8138463.1}.
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DR EMBL; CAJVOS010000029; CAG8138463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W4MTG4; -.
DR OrthoDB; 3352408at2759; -.
DR Proteomes; UP001153618; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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: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 FunFam; 2.70.150.10:FF:000028; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000193; Plasma membrane calcium-transporting ATPase 2; 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 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 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:UP001153618};
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 127..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 326..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 363..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 885..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 950..970
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 982..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 37..143
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 111889 MW; 1F4F2384011C82DD CRC64;
MRTTRSKPTE QSSSNGSAFA LDPDTLGELV VSKNLREVQD LGVRGWEDAL QTDVRSGLSL
NEAHLDSVVV STSAASTEKV TTPEDPAAGP EHDSFVGRRR YFGDNRLPTK PPPSFISLMW
AAYNDHVLFL LTGAAIISLA LGLYQTFGTK HSADNPPVEW VEGVSILVAI VVITLAGAAN
DYQKEFKFQK LNKKQQDRSV WVLRSSRTHE VAISDVVVGD IVHINPGDIV PADGILISGH
QVKLDESSAT GESDPVDKHS LETTHDGSQQ VDPFILSHTK VVEGVGAYLV LATGTRSSYG
KVLLSLDTDP GFTPLQVRLS VLAKNIARFG ALAALVLFVI LFIKFCVSLR NSTESASEKG
QAFLNVFILS LTVVVIAVPE GLPLAVTLAL SFATTRMMRD NNLVRQLRAC ETMGQATDIC
SDKTGTLTQN KMTVVSCFFG SESLTGRKES IDADSEHPSH VAAELSSLSA TLTSDLKQSI
VINSTAIESQ EGAGRQFLGS QTEAALLRFA QDHLGLGHLD FERSNVEVVD LLPFDASRKY
MITIIKLPNG SYRAYIKGAP EGILRKCIAI QSQQGEQTQE RAATDHAIEG IRSRISEYAS
RSLRTIAVCF RDLEVLPLRQ DGESVGFEQV MQALTFQGIF GLQDPLRSDA WSAVDTSHKA
GLTVRMVTGD NHLTARAIAR ECGIINNSDD IVMEGDEFRT LDETQQKDIV LNLKVLARSR
PDDKRILVQR LKDLGRVVAV TGDGTNDAPA LAAADIGFSM GISGTEIARE ASSIVLMDDT
FSSIVKAIMW GRAVGDAVKK FLQFQITITF TSVGLAFVSA VADSSQESVL TPVQLMWVNL
FQDTLAALAL ATDPPPRRIL NRKPEPISTP LITPTMWKMI IGQSIYQMVV TLVLYFAGSS
IFSYHGAHQT SQLQTAVFNT YVWMQIFNMY NNRQIERSFN LVEGLHRNWL FIAITSIMMG
AQILIMFVGG RAFSITTLTG DQWAYSVVLG AISIPVGFLL QAVPDVIVAK PMAGMGSLWD
RLRRRS
//
