ID A0A0L0N075_TOLOC Unreviewed; 1019 AA.
AC A0A0L0N075;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=TOPH_08128 {ECO:0000313|EMBL:KND87175.1};
OS Tolypocladium ophioglossoides (strain CBS 100239) (Elaphocordyceps
OS ophioglossoides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=1163406 {ECO:0000313|EMBL:KND87175.1, ECO:0000313|Proteomes:UP000036947};
RN [1] {ECO:0000313|EMBL:KND87175.1, ECO:0000313|Proteomes:UP000036947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100239 {ECO:0000313|EMBL:KND87175.1,
RC ECO:0000313|Proteomes:UP000036947};
RX PubMed=26215153; DOI=10.1186/s12864-015-1777-9;
RA Quandt C.A., Bushley K.E., Spatafora J.W.;
RT "The genome of the truffle-parasite Tolypocladium ophioglossoides and the
RT evolution of antifungal peptaibiotics.";
RL BMC Genomics 16:553-553(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate;
CC Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00035079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate;
CC Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00034989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC Evidence={ECO:0000256|ARBA:ARBA00034989};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IID subfamily. {ECO:0000256|ARBA:ARBA00035017}.
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:KND87175.1}.
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DR EMBL; LFRF01000040; KND87175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0N075; -.
DR STRING; 1163406.A0A0L0N075; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000036947; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030001; P:metal ion transport; IEA:UniProt.
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; IPR006414; P-type_ATPase_IID.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01523; ATPase-IID_K-Na; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF12; SODIUM ION P-TYPE ATPASE (EUROFUNG); 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 PRINTS; PR00120; HATPASE.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036947};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..119
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 109536 MW; CCED0C4BD5895A24 CRC64;
MGRAVVSTNG AEHANSASDS TAVASPDYQP PIAEPPEVAI EKPSQPHTLP AEHVAQRLGT
HPQHGLSERE AAARLARDGP NAIRGAKGPS LWEIFLQQVA NALTVVLIAV AGLSFGINDY
TEGGVVIAVI VLNIVVGLIQ DYHAEQTIQS LYALSTPRCQ VVRNGRRTTI KAETLVKGDL
VTLVTGDVVP ADLRLVQGHN ISTDEAHLTG ESKTINKKPG AVFDDPDMPV GDRTNIAFSG
SSVTRGRATG IVISTGMETE VGQIAEMLRG KKQDNQGDGA VTRVLFSVYR SLRNILGLEG
TPLQVTLSKF ALLWFALAIL LAIVVFSVSL WRVDEDILLY GICVGVAVIP ESLLAVLTVT
MAVATKAMVK GHVIVRQMPS LEAVGGVTNI CSDKTGTLTQ GRMITRKVWL REGLTGAVEG
TADPYDPSSG TVSWSGSLAE SCFEAFLNTL VLCNNSTVTD GNNETETDSS SGTTAFEPAE
WKAVGEPTEI ALRVFAMRFG KHKTPLDTLV AEHPFDSSCK LMSVVYGGPM DPQHVVHTKG
AVEVMLPILA ESDELKQAIH EKAEELAADG LRVLCVADKA IAGDEHVQDR AKVECNLRFL
GLAGLHDPPR PETASAVAQC RQAGIAVHMV TGDHIKTATA IAYEVGILSR DTPLAPNAVM
SAADFANLSD DQVDALDSLP LVIARCSPLT KVRVIQALHR RKAFCIMTGD GVNDSPALKQ
ADVGIAMGDR RSDVAKQASD MVLTDDNFAS IVTGIQEGRR LADNIQKFLL HLLTSNLAQV
ILLLIGLAFT DDEGIPVFPL SPLEILWANL VTSSPLALGL GLEEVQPDIL QRPPRSLHSG
VFTFELVRDQ LIYGTFMGSL CLGAFTLVAY AASGRGYHAL THGCNDGTSN ACQDVFRARA
TTFATLSFLL LVTAWEVKHF HRSLFAMDER WPGPLSVFRT VYHNRFLFWA VVAGFLATFP
IIYIPYLNNV VFKHQGLSWE WGVVFGCVVL YIALVEAWKA VKRRFGLGID GHRGAGGDV
//
