ID W7MEM1_GIBM7 Unreviewed; 1094 AA.
AC W7MEM1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN ORFNames=FVEG_09346 {ECO:0000313|EMBL:EWG50008.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG50008.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG50008.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000256|ARBA:ARBA00037422}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; DS022253; EWG50008.1; -; Genomic_DNA.
DR RefSeq; XP_018756199.1; XM_018898334.1.
DR AlphaFoldDB; W7MEM1; -.
DR EnsemblFungi; FVEG_09346T0; FVEG_09346T0; FVEG_09346.
DR GeneID; 30067005; -.
DR KEGG; fvr:FVEG_09346; -.
DR VEuPathDB; FungiDB:FVEG_09346; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR OMA; CYIAYSV; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000009096; Chromosome 5.
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 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; PR00121; NAKATPASE.
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 4: Predicted;
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:UP000009096};
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 150..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1003
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..174
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 22..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 121013 MW; 9D34FE62D43B6002 CRC64;
MIEDEKKDVA VFGERIHWND DDEAGRVSRH GERRSRRRSR SRSRDSLSIH RAGSRNRADP
SLVLPVTYRT VSFNIEESKG KEQAELAKAK DVTTKALTDL EWHTIAPFDV EKRLTTSSTA
GLSTEQAERR QREYGRNAPS PAKTHWFRTI FLYFFGGFGS ILLTGCILVF VSWKPLGDPP
AVANLALAIV LLAVFFIQAL FNMFQDWSTS RTMSSIKNML PEEGHVIRDG NLVDLNAAEI
VPGDVIKVKA GNKLPADIRL IEASSDVKFD RSVLTGESKP VAGTVDHTDT NYLETHNIGL
QGTHCILGSC TGIVVATGDR TVFGRIASLT NEPKVQMTTL EKEVLYFVII IASIMISMIA
VVCIIWGAFL KKKHPDFINV PTLIVNCVSV AIAFIPEGLP ISITAGLTIT ANLMKKNKIL
CKSLKTVETL GSVSVICSDK TGTLTTAKMA VSDCAVGGLN MTIENARGKF GQSKSTTHPI
IQLRALAALC NASEFDAATK DAPLADRRIF GDATDQAVLR FAEFVDPSSV GYLRACWNKI
YDLAFNSKNK FMIRCFSCTR TEAVAATLSK ETAFNNDDIL LTIKGAPDVL IGRCSYYVSE
HGETIPLNAA MRATVEQLKN TYSSQGKRCL LLARKIIKNS DLPKNRETSE FEHAVTRESN
TGLTFVGMVA IVDPLRHDIP HVVSTLRGAG IRIAMVTGDF ALTALAIARE AGIVTSQTVD
DSTALQRYRP DDTKDSPISH LGAIVLSGPE LMSLNEHQWE TLTHYEEIVF ARTTPEQKLR
IVREFQKGNV VAMTGDGVND APSLRAADVG ISMGSGSDIA MEAADMVLLD TFSSIIIAVQ
YGRVVFDNLK KVISYLLPAG SFSEFWPVMA FVAFGLPQAL SSFLMIIICC FTDCAAATML
SYEKPEADVL TRPPRNIKKD RLVNWQLILQ AYGVNGVLQT VASFAMAFWY LQRQGIPFSE
LWFSFGKLPA GIDPDYYLAK TNEASSIYFV NLVVMQWFNL MATRTRRLSI FQHPPLFNPN
TQNWYLFPAI IFSLAMAIFW LYIPPLQPVL GTTPVPVEHW FLPFAFGIFQ LLLDEARKFG
VRKWPHGILA KLAW
//