ID A0A168EUL6_CORFA Unreviewed; 1088 AA.
AC A0A168EUL6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=ISF_01146 {ECO:0000313|EMBL:OAA74245.1};
OS Cordyceps fumosorosea (strain ARSEF 2679) (Isaria fumosorosea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=1081104 {ECO:0000313|EMBL:OAA74245.1, ECO:0000313|Proteomes:UP000076744};
RN [1] {ECO:0000313|EMBL:OAA74245.1, ECO:0000313|Proteomes:UP000076744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA74245.1,
RC ECO:0000313|Proteomes:UP000076744};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA74245.1}.
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DR EMBL; AZHB01000001; OAA74245.1; -; Genomic_DNA.
DR RefSeq; XP_018709203.1; XM_018844753.1.
DR AlphaFoldDB; A0A168EUL6; -.
DR STRING; 1081104.A0A168EUL6; -.
DR GeneID; 30017438; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000076744; 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; 2.
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; 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: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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 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:UP000076744};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..104
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 119713 MW; 4A05D1059457BE20 CRC64;
MGQGKRQQEE QQERLQAHVS GQANKPMTAP AHALSYADVE KELQVDHEVG LTPEEAKNRL
EIYGRNEFGE QEGVQPLKIL IGQIANALTL VLILAMVASF AIQSWIEGGV ITAVIVLNIV
VGFLQEFKAA KTMDSLRSLS SPTAQAVRAG ANQTVVTAEI VPGDVVELKT GDTVPADVRL
VEAVNFETNE ALLTGESLPV RKETATTFAA DTGPGDRLNV AYSSSTVTKG RAVGVVFATG
MFTEIGQIAV ALRGKSSRRR EPKKRREDGS ASFHRWVEAW GLTFSDAVGR FLGVNVGTPL
QRKLSKLALL LLGTAIVCAI IVLGANSFSN SQEVIIYAVA TGLSMIPASL IVVLTITMAA
GTKRMVQRHV IVRNLKSLEA LGAVSNICSD KTGTLTQGNM IVKKAWIPGR GTLSVGTTSE
PFNPTVGTIG LTPEQPKDIK FSAENPEGDT VDTAQLPTKD VTVCEYLNVA SLANLATVQQ
VEGEWQVRGD PTEIAIQVFA SRFNRNRLRL CHGKDAEWSE VAEFPFDSDV KKMSVIMEHK
PTGKQHLFTK GAVERVLTSC PRYVDGDEVK ELTEDVKEDT LRNMEALARL GLRVLALASR
TDIPHVKHNE AELERSTFEK DFIFRGLIGL YDPPRPESGP SVRKCHEAGI SVHMLTGDHP
ETARAIALEV GILPSRMSEV AADVARTMVM AASDFDKLTD QEIDNLPILP LVVARCAPQT
KVRMIEALHR RRAFVAMTGD GVNDSPSLKR ADVGIAMGQA GSDVAKEASD IVLTDDNFAS
ILNAVEEGRR MFDNIQKFIL HVLAENIAQA CTLLIGLAFK DSRGISVFPL APVQILWIIM
ITSGMPDMGL GFEIAAPDIM QRPPQNLKQG VFTPELLIDM VVYGLWMSAL CICSFIVVLY
GFGRGAADLG DDCNNNYHES CKVVFRARAT TFACLTWFAL FLAWEMVNLR RSFFRMQPKS
KRYFTQWILD VWRNKFLFWS IIAGFVTMFP IIYIPVINTV VFKHAPISWE WAVVFIEAFL
FFLGIEAWKW AKRVYFRRQA RKKTADRKGG DLEERVFGHY FRSNTHSSAG CSDEGPVEKK
HSKNAGAQ
//