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Database: UniProt
Entry: E9EXR7_METRA
LinkDB: E9EXR7_METRA
Original site: E9EXR7_METRA 
ID   E9EXR7_METRA            Unreviewed;      1022 AA.
AC   E9EXR7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE            EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN   ORFNames=MAA_04816 {ECO:0000313|EMBL:EFY99887.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY99887.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFY99887.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFY99887.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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   -!- 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:EFY99887.1}.
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DR   EMBL; ADNJ02000001; EFY99887.1; -; Genomic_DNA.
DR   RefSeq; XP_007821103.1; XM_007822912.1.
DR   AlphaFoldDB; E9EXR7; -.
DR   GeneID; 19259102; -.
DR   KEGG; maj:MAA_04816; -.
DR   HOGENOM; CLU_002360_3_0_1; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000002498; 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   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; 2.
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; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        97..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        771..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        949..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        981..998
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..122
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1022 AA;  109551 MW;  DE95FE8529DA243A CRC64;
     MGEPLVISTN GAEHANSSSD SEALAGPDDQ PPIAEPPDIP YTSEKPNCHH THSAQHVAEL
     LATDQDHGLS DEEAAARLAR DGPNAIKGAK GLSIGEIFLQ QVANALTVVL IAVAAISYII
     GDYVEGSVVV AVIVLNIVVG LIQDYRAEQT IQSLYALSTP KCKVIRDGHS DTVKAETLVK
     GDLVSLATGD VVPADLRLVQ GINLSTDEAH LTGESIAISK KPEAVFTDPD MPVGDRINLA
     FSGSSVTRGR ATGIVISTGM DTEVGQIAEL LRKKKKEAKG SNAVAKALYS FYQTVRSILG
     LEGTPLQVTL SKFALLLFGL AILLAVVVFS VNLWEIDDDV LLYGICVGVA VIPESLLAVL
     TVTMAVATKA MVKGHVIVRQ MPSLEAVGGV TNICSDKTGT LTQGRMIARK VWLRDGLTGT
     VDGTSDPYDP SSGTVSWSGS LVGTCINPFL NTLVLCNNAT VSDGKKEPET DSSSVTTALE
     PADWKAMGEP TEIALKVFAM RFGKTTGSDL LTAEHPFDSS CKLMSVVYGN GLERQRHVYT
     KGAFEVLLPI LAEDDGMKKA IRAKAEEFAG EGLRVLCIAD KLMEGGAEDF QDRAKVECDL
     RFLGLAGLYD PPRSETAGAV KQCREAGVTV HMVTGDHIKT ATTIAYEVGI LPKDMPLGPN
     TVMSAAELGS MTDEQIDELD SLPLVIARCS PLTKVRVIQA LHRRRAFCIM TGDGVNDSPA
     LKQADVGIAM GDRGSDVAKE ASDMVLTDDN FASIVTGIKE GRRLSDNIQK FLLHLLTSNL
     AQVILLLIGL AFKDKEGVPV FPLSPLEILW ANLVTSSPLA LGLGLEEAQP DILQRPPRSL
     HSGVFTLDLV RDQLMYGTFM GSLCLAAFML VAYAASGKGF HNLTHGCNDG TGGICSAIFR
     ARAATFATLS FLLLVTAWEV KHFHRSLFNM DKRWSGPFSV FKTVYHNTFL FWSVVAGFLA
     TFPVIYIPYV NTTVFKHKGL TWEWAVVAGC VVTYIGLVES WKAVKRRFGL GITRHPSTPG
     QV
//
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