ID A1CMG8_ASPCL Unreviewed; 1060 AA.
AC A1CMG8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=ACLA_096890 {ECO:0000313|EMBL:EAW08755.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW08755.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW08755.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027058; EAW08755.1; -; Genomic_DNA.
DR RefSeq; XP_001270181.1; XM_001270180.1.
DR AlphaFoldDB; A1CMG8; -.
DR STRING; 344612.A1CMG8; -.
DR EnsemblFungi; EAW08755; EAW08755; ACLA_096890.
DR GeneID; 4702410; -.
DR KEGG; act:ACLA_096890; -.
DR VEuPathDB; FungiDB:ACLA_096890; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR OMA; ASRFNWG; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000006701; 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:0030001; P:metal ion transport; IEA:UniProt.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
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 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 990..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1060 AA; 116401 MW; 556456BE564D7A10 CRC64;
MGSEKKAVDA SQPLSLPAHS LLYEDVLREL SVDSDEGLTT AEAKKRLEQY GPNELEGGES
VSMVKIVIRQ IANAMMLVLI IAMAVSFGIK SWIEGGVIGA VIGLNIVVGV YQDYAAEKTM
DSLRSLSSPT GTVTRDGKTN VIPANEIVPG DMVELKVGDT VPADLRLVDA MNFETDEALL
TGESLPVQKE IDEIFDPDTG PGDRLNIAYS SSTVTRGRAR GVVVGTGMRT EIGAIAAALR
AGDSKKRPVK RGPGGETKKR WYVQAWTLTC TDAVGRFLGI NVGTPLQRKL SKLALALFFI
AVIFAIIVMG ANDFRDDTEV IIYAVATGLA MIPACLVVVL TITMAVGTKQ MVQRHVIVRK
LDSLEALGAV TNICSDKTGT LTQGRMVAKR AWVPSIGTFS VGSSNDPLNP EEGDVSLLPD
APVKIDADAR GEPSNPEDLL NANPILEPYL NVAAIANLAH VHKSSEGWQA RGEPTDIAIQ
VFASRFNWGR ERWTKGEKPI WRQKAEYPFD STVKKMSVIF KNSAEGREMI FTKGAVERVL
DSCTSLIWTA GSKPVPLTEE IKDEILQNME ALAKEGLRVL CLACRENTTP VKDEEVPPRE
EVEKDLTFCG LVGLYDPPRP ETAGAIEECY RAGISVHMVT GDHPGTARAI AAQVGIIPAN
MDNIPKDVAD AMVMTASQFD KLTDEEIDDL PTLPAVIARC APNTKVRMID ALHRRGRYAA
MTGDGVNDSP SLKRADVGIA MGQSGSDVAK DASELVLTDD NFASIINGIE EGRRIFDNIQ
KFVLHLLAEN VGLALTLLIG LCFKDDNGQS VFPIAPVEIL WIIMITSGLP DMGLGMEIAA
PDIMNRPPQS KQGIFTWEVI VDTLVYGVWM AALCLASFSL VLFGWGDGNL ASGCNSHYSK
ECDGVFRARA TTFVCMTWFA LFLAWEMIDM RRSFFRMQPD SKRYFTQWMF DVWRNKFLFS
GIMVGFVTIF PILYIPVIND IVFKHVGISW EWGVVFVEAV LFFLGVEAWK WCKRIYFRRQ
AHRQKDDVGE KNLRDFSRYT TMSRSETQAT GDMKVEQSMV
//
