ID Q4WD68_ASPFU Unreviewed; 1060 AA.
AC Q4WD68;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=AFUA_6G03690 {ECO:0000313|EMBL:EAL85670.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85670.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL85670.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL85670.1}.
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DR EMBL; AAHF01000012; EAL85670.1; -; Genomic_DNA.
DR RefSeq; XP_747708.1; XM_742615.1.
DR AlphaFoldDB; Q4WD68; -.
DR STRING; 330879.Q4WD68; -.
DR EnsemblFungi; EAL85670; EAL85670; AFUA_6G03690.
DR GeneID; 3505061; -.
DR KEGG; afm:AFUA_6G03690; -.
DR VEuPathDB; FungiDB:Afu6g03690; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR InParanoid; Q4WD68; -.
DR OMA; ASRFNWG; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140679; F:ABC-type sodium transporter activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008554; F:P-type sodium transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
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; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF77; 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; 2.
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 Hydrolase {ECO:0000313|EMBL:EAL85670.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
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 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..980
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 992..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 404..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 116447 MW; 3FEFDBEBBAB6CDAD CRC64;
MGAQKKQSSD NSQALSQPAH ALRYEDVLRE LAVDPDQGLT VGEAKRRLQQ YGPNELEGGE
GVSIVKIVIR QIANAMMLVL IIAMAVSFGI QSWIEGGVIG AVIGLNIVVG VYQDYAAEKT
MDSLRSLSSP TGTVTRDGKT STIPANEIVP GDMIELKVGD TVPADLRLVD AMNFETDEAL
LTGESLPVQK EVDTTFDPDT GPGDRLNIAY SSSTVTRGRA RGVVISTGMQ TEIGAIAAAL
RASDSKRRPV KRGPEGETKK RWYVQAWTLT CTDAVGRFLG INVGTPLQRK LSKLALALFA
IAIIFAIIVM GVNGFRNDKE VIIYAVATGL AMIPACLVVV LTITMAVGTK QMVERHVIVR
KLDSLEALGA VTNICSDKTG TLTQGRMVAK RAWIPSVGTF SVGSSNNPLN PEEGDLSLLP
DPPVKVGPDA HGEPSRPEDL LKDNPLLEQY LNVAAMANLA HVHRSEHNEW QARGEPTDIA
IQVFASRFNW GRDRWTKGEK PVWRQKAEYP FDSTVKKMSV IFKNTNDDRE MIFTKGAVER
VIEACTTVTW TAGSDPIALD ENIKEEILQN MEALAKEGLR VLCLACRENH NPVKGEVVPA
REEVEKDLTF CGLIGLYDPP RPETAGAIDE CYRAGISVHM VTGDHPGTAR AIAAQVGIIP
ANMDSLAKDV ADAMVMTASQ FDKLTDEEID ALPTLPAVIA RCAPNTKVRM IDALHRRGRF
AAMTGDGVND SPSLKRADVG IAMGQSGSDV AKDASELVLT DDNFASIING IEEGRRIFDN
IQKFVLHLLA ENVGLALTLL IGLCFKDDNG QSVFPIAPVE ILWIIMITSG LPDMGLGMEI
AAPDIMDRPP QSKQGIFTWE VIVDTMVYGV WMAALCLASF SLVLFGWGDG NLASGCNSDY
SPECDGVFRA RATTFVCMTW FALFLAWEMI DMRRSFFRMQ PNSKRYFTQW MFDVWRNKFL
FSGIMIGFVT TFPILYIPVI NDVVFKHVGI SWEWGVVFVE AILFFAGCEA WKWCKRIYFR
HTSQKETGRE RVLRDFSRYT TMSRSETQAT GDLNVEKSMV
//
