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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//