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Database: UniProt
Entry: W2RMV9_9EURO
LinkDB: W2RMV9_9EURO
Original site: W2RMV9_9EURO 
ID   W2RMV9_9EURO            Unreviewed;      1070 AA.
AC   W2RMV9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE            EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN   ORFNames=HMPREF1541_07464 {ECO:0000313|EMBL:ETN37841.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN37841.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN37841.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN37841.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KB822723; ETN37841.1; -; Genomic_DNA.
DR   RefSeq; XP_008720010.1; XM_008721788.1.
DR   AlphaFoldDB; W2RMV9; -.
DR   STRING; 1220924.W2RMV9; -.
DR   GeneID; 19974803; -.
DR   VEuPathDB; FungiDB:HMPREF1541_07464; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_0_1; -.
DR   InParanoid; W2RMV9; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000030752; 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:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02086; P-type_ATPase_Na_ENA; 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; 2.
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:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 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   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   Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT   TRANSMEM        70..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        788..809
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        825..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..893
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        913..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        964..984
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        996..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..90
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1051..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  117627 MW;  49CA7D3D4264BE65 CRC64;
     MDNHVSGQSN KPMSKPAHAL DCDTLVRELG ADAQTGFSKS QASQRLNEFG RNELEDGPGV
     QPIKILIRQV ANAMMLVLIM AMVVSFAIKS WIEGGVVAAV IALNIIVGFL QEYQAEKTMD
     SLRSLSSPTA NVVRDGSTIN IPTAELVVGD LVELKVGDTV PADLRIVESI NLETDEALLT
     GESLPVAKEE EAVFDPDTGP GDRLNVAYSS STVTKGRARG IVYATGMYTE IGSIAQSLRQ
     KDSRRRPVKR RDDGTASPLH LAQAWTLTVA DFIGNFLGLN VGTPLQRKLS RLAILLFGIA
     VVCAIIVLAA NEFSNRAEVI IYAVATGLSM IPASLIVVLT ITMAVGTKHM VQRNVIVRNL
     KSLEALGAVT DICSDKTGTL TQGKMVAKKV WIPNRGTYSV GISNNPFDPT ASSLAHSVEV
     PTKGLSESET LTDDESTSAS SLLENNEDLE AFLAVAGLCN IARVHKNNDG EWTALGDPTE
     IALQVFASRF DRNRHGLVDG EGAKYKQVSE YPFDSDVKKM SVIFEDRQTQ AQMIYTKGAV
     ERVLESCDSV IWEDGQTVGF SDSLKDKTLK VMEALAFQGL RVLALASRDY NPRDGRRASR
     DGPPTREDIE CNLTFRGLIG LYDPPRPESA DAVKRCHRAG IKVHMLTGDH PGTASAIAKQ
     VHILPDMNKV SATIAQSMVM TAKEFDKLTD EELDRLPVLP LVIARCAPNT KVRMIEALRR
     RDAFMAMTGD GVNDSPSLKI ADVGIAMGMA GSDVAKDAAD IVLTDDNFAS ILNAIEEGRR
     MFDNIQKFIL HLLAENIAQA CTLLIGLAFK DSTGLSVFPL APVQIMWIIM ITSGMPDMGL
     GLEIAAPDIL ERPPMPLKVG VFTREVCFDM LAYGLWMSAL CLSSFLLVLY GFGDGNLGEG
     CNTSYSEQCD TVFRARATTF VSLTWFALFL AWEMVNTRRS FFRMQPKSKK YLTQWMYDVW
     RNPFLFWAII AGFVTIFPTL YIPVLNHDVF KHTGISWEWG IVFVEATLFF AGIETWKWGK
     RIFFRRRARK MGQTSDDLEK RAYGDFFDAS ESDRDVDVPT KDEKYPSRAS
//
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