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Database: UniProt
Entry: A0A2V5HLD7_ASPV1
LinkDB: A0A2V5HLD7_ASPV1
Original site: A0A2V5HLD7_ASPV1 
ID   A0A2V5HLD7_ASPV1        Unreviewed;      1004 AA.
AC   A0A2V5HLD7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   28-JAN-2026, entry version 32.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=BO99DRAFT_203192 {ECO:0000313|EMBL:PYI23372.1};
OS   Aspergillus violaceofuscus (strain CBS 115571).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450538 {ECO:0000313|EMBL:PYI23372.1, ECO:0000313|Proteomes:UP000249829};
RN   [1] {ECO:0000313|EMBL:PYI23372.1, ECO:0000313|Proteomes:UP000249829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115571 {ECO:0000313|EMBL:PYI23372.1,
RC   ECO:0000313|Proteomes:UP000249829};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-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=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|ARBA:ARBA00038148, ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; KZ825106; PYI23372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5HLD7; -.
DR   STRING; 1450538.A0A2V5HLD7; -.
DR   OMA; PLWNNMM; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02083; P-type_ATPase_SERCA; 1.
DR   FunFam; 3.40.50.1000:FF:000005; Calcium-transporting ATPase 1; 1.
DR   FunFam; 3.40.1110.10:FF:000021; calcium-transporting ATPase, endoplasmic reticulum-type; 1.
DR   FunFam; 1.20.1110.10:FF:000037; Calcium-transporting ATPase, putative; 1.
DR   FunFam; 2.70.150.10:FF:000014; Calcium-transporting ATPase, putative; 1.
DR   FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 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; 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   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; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
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:UP000249829};
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        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        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        288..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        754..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        787..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        827..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        890..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        927..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        958..978
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   1004 AA;  108829 MW;  97957D1AD19F75B5 CRC64;
     MEQSYLSSPA EVLDHFSVTE SFGLSQDQVI KARQRHGPNA LAEEPPTPLW QLVAEQFKDQ
     LVLILLGSAA VSFILALFEE GDDWSAFVDP VVILTILILN AVVGVTQESN AEKAIAALQE
     YSANEATVVR DGKTQRVKAE DLVPGDIVHV AVGDRVPADC RLLAIHSNSF RVDQAILTGE
     SESVAKDARI IQDKQAVKQD QVNMLFSGTT VVNGHATAIV VLTGGSTAIG DIHESITSQI
     SEPTPLKQKL DDFGDMLAKV ITVICVLVWI INIEHFNDPS HGGWTKGAIY YLKIAVSLGV
     AAIPEGLAVV ITTCLALGTR KMAQKNAVVR SLPSVETLGS CSVICSDKTG TLTTNQMSAE
     KIAYLNETGH GVEEIDVEGT TFAPEGKISL QGKELQNVAV TSSTIRQMTE VMARCNSATL
     AHDAKTGAFS CIGEPTEGAL RVLVEKIGTE DSAINAELLP LPATQRLHAA SAHYETRLSL
     KATYEFSRDR KSMSVLVDTG KEQKLLVKGA PESILERCSH VLLGTNGKRV SLTKDHLNCL
     SEELIGYGNR GLRVIALASV DTDGTNPLMH NAKSTDDYAQ LEQNMTLLGF VAMLDPPRVE
     VAASIRKCKE AGIRVIVITG DNRNTAESVC RQIGVFSEDE DLKGKSFTGR EFDSLSYNEK
     LDAVKTASLF SRTEPSHKSK LVDLLQSLGH VVAMTGDGVN DAPALKKSDI GVAMGTGTDV
     AKLAADMVLA DDNFATITVA VEEGRSIYSN TQQFIRYLIS SNIGEVVSIF LTAALGMPEA
     LIPVQLLWVN LVTDGLPATA LSFNPPDHDV MRRAPRKRDE PLVGGWLLFR YMVIGTYVGA
     ATVFGYVWWF VYNPEGPQIS FWQLSHFHKC SSQFPEVGCE MFTNDMSRSA STVSLSILVV
     IEMLNAMNAL SSSESLFTFG LSNNPMLVYA IILSMSLHFA ILYVPFLQGL FSILPLGWME
     WQAVLAISAP VIFIDEALKV MERRLYNNVP AVAPVELNGK PKRA
//
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