ID A0A443HVA0_BYSSP Unreviewed; 1435 AA.
AC A0A443HVA0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=C8Q69DRAFT_263252 {ECO:0000313|EMBL:RWQ95691.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ95691.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ95691.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ95691.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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:RWQ95691.1}.
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DR EMBL; RCNU01000005; RWQ95691.1; -; Genomic_DNA.
DR STRING; 264951.A0A443HVA0; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000283841; 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; 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; 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 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 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|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:UP000283841};
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 306..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 509..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 548..575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1000..1021
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1070..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1148..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1181..1202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1321..1342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 272..317
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 1027..1202
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 155502 MW; EA1E1D39083B9F1A CRC64;
MSDRKENGDG ARQNNNPFRR ARAPTITIDT SAVNLATDSP SQGQGGAAPA RPQPSLRIST
SNVETDTGTL LPSNDVSPTD QRSMRSFEGR ERESRPTSPH NVSSPTFKGP DVHSNFLAVP
GSRSRGNSIE SEGTTHSGSS FGSDTYVQSS PVDNSRTNST VMNDEDALLP DPGTEGDFEV
EDNKFAFSPG QLNKLLNPKS LSAFHAIGGL AGLERGLRSD RRSGLSLDET YLDGTVSFEE
ATGRDVQQQT PKVASNTPLA DSNQGASGQG GDAFADRKRV FGDNRLPEKK AKSFLELAWI
AYNDKVLILL TIAAVISLAL GIYQSVTAKN GEPGVEWVEG VAIIVAILIV VIVGAVNDWQ
KERQFVKLNK KKEDRHVKVI RSGKTVEISV FDVLVGDVVH LEPGDLVPVD GIFIEGHNLK
CDESSATGES DMLRKHSADD VYRAIENHEN LSKMDPFIVS GAKVSEGVGT FLVTSTGVNS
SYGKTMMSLQ DEGQTTPLQS KLNVLAEHIA KLGLASGLLL FVVLFIKFLV ELKNIDGADA
KGQAFLQIFI VAVTIIVVAV PEGLPLAVTL ALAFATTRML KDNNLVRLLR ACETMGNATT
ICSDKTGTLT QNKMSVVAGT LGTSSRFGDK KKPQNSSTEV ETSNNGGDDS SNVSPSEFVA
TLSPSVKDML LQSIVQNSTA FEGDEDGVPT FVGSKTETAL LNFARDFLGM GALSEARSNS
QMVQMVPFDS GRKCMAVVIK QQDGRYRMFV KGASEILISK STRIISDPTK EPADTPLTDQ
MRSSLNDIVA NYASRSLRTI GLLYRDFDQW PPRGAPTLEE DRKLAQFDAI FKDMVFLGVV
GIQDPLRPGV ADSVHQCQKA GVFVRMVTGD NILTAKAIAQ ECGIFTPGGV AMEGPKFRKL
SSHQMNQVIP RLQVLARSSP EDKRILVARL KKLGETVAVT GDGTNDAPAL KTADVGFSMG
IAGTEVAKEA SDIILMDDNF TSIVKAIAWG RTVNDAVKKF LQFQITVNVT AVVLTFVSAV
ASGDESSVLT AVQLLWVNLI MDTFAALALA TDPPSPYVLD RRPEPKSSSL ISLTMWKMII
GQSIYQLVVT LVLNFAGNRI FGYKTSEEQA ALETVVFNTF VWMQIFNQYN CRRLDNHFNI
FEGIHRNVWF IGIQAIIIAG QVMIIFVGGR AFSVKRLNGP QWGVSLVLGA ISVPVAVIIR
LIPDSLIQRL VPHFLSRKKP PQLFVSDEES RFEWNPALEE IRDQLSFLKT VRGGRLRHLK
HKLQHPETLL PRSRSGSRSR EESAPATPVS EEAPPSTSAS PPPATPESRS RNRTRSRSNS
AFGPAAAMAG IVAGSIAGWS PIERGHGDND SLKFSRNGNG RDDQAAIEVH PDTHPDDPVI
TDYAVSSTTP PSQNPDLVPS FDFVPSDSTS TRGRRSTSRR SRSNTLRSQS QQSQN
//
