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Database: UniProt
Entry: A0A100IKJ7_ASPNG
LinkDB: A0A100IKJ7_ASPNG
Original site: A0A100IKJ7_ASPNG 
ID   A0A100IKJ7_ASPNG        Unreviewed;      1544 AA.
AC   A0A100IKJ7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=ABL_05580 {ECO:0000313|EMBL:GAQ42919.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ42919.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC       {ECO:0000256|ARBA:ARBA00037422}.
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:GAQ42919.1}.
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DR   EMBL; BCMY01000008; GAQ42919.1; -; Genomic_DNA.
DR   PaxDb; 5061-CADANGAP00010947; -.
DR   VEuPathDB; FungiDB:An12g10680; -.
DR   VEuPathDB; FungiDB:An14g02290; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1085788; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1148992; -.
DR   VEuPathDB; FungiDB:ATCC64974_2050; -.
DR   VEuPathDB; FungiDB:ATCC64974_2060; -.
DR   VEuPathDB; FungiDB:M747DRAFT_320192; -.
DR   VEuPathDB; FungiDB:M747DRAFT_349153; -.
DR   OMA; HASAFKE; -.
DR   Proteomes; UP000068243; 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:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; 3.50.50.60; FAD/NAD(P)-binding 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; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
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; SSF51905; FAD/NAD(P)-binding domain; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
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        602..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        634..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        793..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1373..1401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1436..1453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1474..1493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1505..1523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          550..623
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          470..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1544 AA;  171151 MW;  708FDF38E3B82D9D CRC64;
     MSKPNSQRPF HVIIVGASIA GLTLAHCLSN TEIEFTILEA RSDTYPDGAG LAILPNGARI
     LDQLGLYQDV LDQGQCMVSH STWLETGHLL RRVDAGRIRS FGRFDYPVLV IARRALLGIL
     YTRLRSSRLF FNRRVVRIVS SPDNVTVHSA DGMSVLGDLV VGADGVHSIV REQMWHHIRA
     TNGAVASSRW FSEVPLTDSF AGVFGIAQSI PKLNRGDVHR TYGHGWLTVI MVGADARVCW
     FMSIARTMMP VLIPRHTSDR AYVSRIVEPF LKKHVTRDVT FGEVFNCSET CVVASLEEGF
     QNRWSWGRFV GIGDAMAPNI AEGANCAIES AASLANHLVF FARGSTPLYT EDRLTPMLKA
     WEDSRKRRTR GLFLISQCAV RIEAATSWML RLNQVFLSRF HGTGIGLLTS ITSRTARVDY
     LPLPLLQQSS TQQVLEKKER ESVWNWQFIK MDAKSGVSLN AEATRLRWQE GDEEKGVAAR
     RDPLQLSRTT SVASNSSARS RARRATVDPS LSLPIHYRTV SFDIDEARDR ERAEAAKTKS
     NVATDLSNLD WHMVSPEEIQ KRWRVDISQG LSHDQVQQRV REFGKNALSP LPHQWFWQIF
     GYFFKGFGGI LLIGCILVFI SWKPLGQPPA PANLALAIVL LAVFFIQAGF NAWQDWSSSR
     VMASITAMLP ESCLVLRDSS LVVVSAPDIV PGDVVHLKAG NKLPADVRLV EVSNDVCFDR
     SILTGESLPV NGTVDSTDDN YLETHCIGLQ GTHCVTGSAV GVVVSTGDST VFGRIAKLTS
     EPKKGLTTLE KEVLRFVLLI VLIMLTMIII VIIVWATWLR VDHPGWINVP TLIVDCVSVA
     IAFIPEGLPI ALTANLTITA NLMSKNKILC KSLKTVETLG AVSVICSDKT GTLTKNKMFV
     TDCALSMSRF STELARDEMV IKGRKTGIHQ LRGIAGLCNA AEFDASSMNQ PLHEREIHGD
     ATDQAVLRFS EGLGSVAELR RTWRKTYELA FNSKNKFMIR TFSLVESAGL SLGMSAAESA
     QFKRNDTLLT IKGAPDILIE RCTQIVDTDG SVLPLDGRIL AHIKYVKDQW SSEGKRVILL
     ARKVLPASDI MPLPSSREFE SEVMNHAKTG LVLVGLVGIV DPPREEIPDV VRTLRRAGVR
     IFMVTGDYGL TALAIARQCG IVTTHGPVDT ASSLKRLPDY DEKPPSTPST TAITLSGAEL
     MSLNDHQWEQ LCQYQEIVFW RTTPEQKLRI VREFRARDEI VGMTGDGVND APSLKAADIG
     IALGSGSDIA IEASDMVLME SFSAIVEAVQ YGRVVFDNLK KTIVYLLPAG SFSEFWPVFT
     SVVFGLPQVL SSFLMIIICC FTDCAAATVL AYEAPEADVL LRPPRKPKQN RLVNWKLIFH
     AYGILGMIET IASFAMAFWY LERNGIPFSA LWFKFGATPN NIDSDWLNAR LNEASSVYFI
     NLVVMQWFNL MAVRTRRLSI FSHPPAFNKQ TQNLLLFPAI LFALAMAVFW LYIPPLQRVL
     DTSSVPVEHY FLPAAFGLGI LILDELRKAG VRRWPGGVLD RLAW
//
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