ID A0A2N6NH31_BEABA Unreviewed; 998 AA.
AC A0A2N6NH31;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=Ca-P60A {ECO:0000313|EMBL:PMB66603.1};
GN ORFNames=BB8028_0001g15240 {ECO:0000313|EMBL:PQK09454.1}, BM221_007596
GN {ECO:0000313|EMBL:PMB66603.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66603.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB66603.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66603.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
RN [2] {ECO:0000313|EMBL:PQK09454.1, ECO:0000313|Proteomes:UP000237441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 8028 {ECO:0000313|EMBL:PQK09454.1,
RC ECO:0000313|Proteomes:UP000237441};
RA Valero Jimenez C.A., Zwaan B.J., Van Kan J.A., Takken W., Debets A.J.,
RA Schoustra S.E., Koenraadt C.J.;
RT "Comparative genomics of the entomopathogenic fungus Beauveria bassiana.";
RL Submitted (JUL-2016) 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|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}.
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:PMB66603.1}.
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DR EMBL; MRVG01000008; PMB66603.1; -; Genomic_DNA.
DR EMBL; JRHA01000001; PQK09454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NH31; -.
DR EnsemblFungi; BB8028_0001g15240.1; BB8028_0001g15240.1; BB8028_0001g15240.
DR OMA; PLWNNMM; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR Proteomes; UP000237441; 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; cd02083; P-type_ATPase_SERCA; 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; 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 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:UP000235728};
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..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 290..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 750..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 823..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 918..939
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 998 AA; 107887 MW; DEA15890D06CB3DE CRC64;
MDSAFATPVK QVLANFNVND HDGLTDKQVD ELRSKYGRNS IPEDPPTPLW ELILEQFKDQ
LVLILLGSAA VSFVLALFED EGGWSAFVDP AVILTILILN AVVGVSQESS AEKAIAALQE
YSANEANVIR NGGHVSRVKA DDLVPGDIIS VSVGNRIPAD CRVIAIESNS FSVDQAILTG
ESESVGKDAA AVIKDDKAVL QDQVNMLFSG TTVVVGRARA VVALTGSNTA IGDIHESITA
QISEPTPLKQ KLNDFGDNLA KVITVICILV WLINIPNFND PSHGSWTKGA IYYLKIAVSL
GVAAIPEGLA VVITTCLALG TRKMAAKNAV VRSLPSVETL GSCSVICSDK TGTLTTNQMS
VNKIVYLTDA GKDLVELDVE GTTFSPKGDI RSNGKVVNNL TEKSSTIQQM AEVGALCNNA
HLAYDEKTGQ YSSVGEPTEG ALRVLVEKLG PVAPAGTDVH EALHYASTNF EEALPVLSTF
EFSRDRKSMS VIVADGKKKK LLVKGAPESI IDRCTQATVG ADGKRVPLTS KISEVLMKEV
VDYGNRGMRI IALASIDDVS KNRLASTAKT TEQYAELEQD MTFLGLIGML DPPRPEVPKS
VNQCKAAGIR IIVITGDNRN TAESICRQIG VFGENEDLTG KSYTGREFDN LSPGEQLEAA
KRASLFSRVE PGHKSRLVDL LQSLGEVVAM TGDGVNDAPA LKKADIGVAM GSGTDVAKLA
ADMVLADSNF ATIEVAIEEG RSIYNNTQQF IRYLISSNIG EVVSIFLTAA LGMPEALIPV
QLLWVNLVTD GLPATALSFN PPDHDIMNRQ PRKRDEKLIG GWLFFRYLII GTYVGLATVA
GYAWWFMYYP AGPQISFSQL SRFHHCSTEF PEIGCQMFSN DMAKAGSTVS LSILVTIEMF
NAMNALSSSE SLLTLPLWKN MMLVYAIALS MALHFALLYT PVLQTLFAIL PLNWVEWKAV
IIISAPVILL DEVLKFIERQ YFMQKITPVA KKEAKKNL
//
