ID A0A9Q0AKK2_9PEZI Unreviewed; 1096 AA.
AC A0A9Q0AKK2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=JX265_010253 {ECO:0000313|EMBL:KAI1859804.1};
OS Neoarthrinium moseri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Apiosporaceae; Neoarthrinium.
OX NCBI_TaxID=1658444 {ECO:0000313|EMBL:KAI1859804.1, ECO:0000313|Proteomes:UP000829685};
RN [1] {ECO:0000313|EMBL:KAI1859804.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TUCIM 5799 {ECO:0000313|EMBL:KAI1859804.1};
RA Vignolle G.A., Hochenegger N., Mach R.L., Mach-Aigner A.R.,
RA Javad Rahimi M., Salim K.A., Chan C.M., Lim L.B.L., Cai F.,
RA Druzhinina I.S., U'Ren J.M., Derntl C.;
RT "Revisited historic fungal species revealed as producer of novel bioactive
RT compounds through whole genome sequencing and comparative genomics.";
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) + ATP + H2O = K(+)(out) + ADP + phosphate + H(+);
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:ARBA00048599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) + ATP + H2O = Na(+)(out) + ADP + phosphate + H(+);
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:ARBA00049499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC Evidence={ECO:0000256|ARBA:ARBA00049499};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KAI1859804.1}.
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DR EMBL; JAFIMR010000033; KAI1859804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q0AKK2; -.
DR Proteomes; UP000829685; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008554; F:P-type sodium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR FunFam; 2.70.150.10:FF:000016; Calcium-transporting P-type ATPase putative; 1.
DR FunFam; 3.40.50.1000:FF:000001; Phospholipid-transporting ATPase IC; 1.
DR FunFam; 1.20.1110.10:FF:000015; Sodium ion P-type ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000020; Sodium ion P-type ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000047; Sodium P-type ATPase; 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; IPR059000; ATPase_P-type_domA.
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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 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; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000829685};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..82
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 407..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 120272 MW; 7A392E193F24177F CRC64;
MAGEFDRHPY LLTVQDVAKN LGTDLDRGLT GAQVAQLQEK YPPNELDIGG AIPWYTIFLR
QLFNAMILVL FFAMSLSFGI SDWVEGGVLA AVIILNVSIG FFQEYGAEKK MDALRALSSP
SANVLRDGKT QVISNSEVVP GDVILLKMGD TIPADMRLFE VMNLTSDEQS LTGESVPVEK
VESHLDDEEL GIGDRINIAY GTTVVRKGRG RGVVIATGMQ TEVGKIAAST SKKNRKAGRS
MNYKKYGKRQ PVVGLAKRAY DFFGKFLGLT EGTPLQIKLS KLAYMLFGCA LLLAVIVFAV
NRFDIPTEVV IYAISTGIAI IPESLVAVLT ITMVVATTVM RKANVVVRDL SALEALGGVT
NICSDKTGTL TQGAMIVKKA WIPGKTIYTV HDSKDPSDPT VGRVTYADAE EDAAATEPEK
RDYDQERSAS ALKFDVPDEK LKPKQKKHDG PEADMTPELE AFLLSAALCN LATVRQETEA
NADDRKWKTT GEPTEIALQV FAHRFNKGKK TIEGQGWKQV AEFPFDSSIK RMSVIYDGAE
SENSMVFTKG AVERIIDLCT TVGIGGQAEE MTDSYKEHIL KQMDDFASQG QRVLAIASRP
WDGKYQEKSS KEGDDADNAL RQRVESGLTL LGLAGIYDPP RRETTPAIAE CSTAGIKVHM
LTGDHPATAT AIAKEVGIIP HDLSTLPADL AESLIKKASD FDKMSDAEID ALPELPLVLA
RCAPDTKTRM IEALRRRNAF MAMTGDGVND APSLSRADVG IAMGSGSDVA KSAAKIVLTD
DKFNSIVAAI REGRRMFDNI QKFILHLLTS NVGEVILLIC GLAFRDQSGY SVFPISPLQI
LWINMLTSSF PAFGLGREQA SRAVMRKPPH DKRRGVFTNQ ILVDMLVYGL LMGVLTLMTF
VIVVYGANGG ALGADCNKAW SESCRPVFRA RATVFAELTW LILISAWEFK DLRRSMFALN
PDSTARFPFF RDIYENRFLF WAVVIGGLSV FPVVYIPTLN TAVFKHVDIS WEWAIVVAAL
VLFVAGVELW KMAKRTFRLL EDRAVVKGAF SQGSVEEGRR FAHTMSFSSL KSWRSFGRKN
TGDSGMHSRS MSRSKE
//
