ID B0E000_LACBS Unreviewed; 1083 AA.
AC B0E000;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Sodium-potassium ATPase {ECO:0000313|EMBL:EDQ99847.1};
GN ORFNames=LACBIDRAFT_186573 {ECO:0000313|EMBL:EDQ99847.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDQ99847.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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DR EMBL; DS547158; EDQ99847.1; -; Genomic_DNA.
DR RefSeq; XP_001889539.1; XM_001889504.1.
DR AlphaFoldDB; B0E000; -.
DR SMR; B0E000; -.
DR STRING; 486041.B0E000; -.
DR GeneID; 6085160; -.
DR KEGG; lbc:LACBIDRAFT_186573; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; B0E000; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 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; 3.40.50.1000; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; 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; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194};
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 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..161
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 118938 MW; 3B5CF00BE6B05F50 CRC64;
MQSPASDLES QKEPPENPDI FLEGLPNGLD TDANIQSTHP RFEGGRDAGH RLPIEFRTLS
IHVDTRATIG GDKDKPRAAA VKELVSLDWH KISTEEALRR LGVSPVTGLD TTQAQRRLKT
GGKNVISPPK NNYFRKVLEW VLGGFGSLLL VASIVCFIAW KPLGKPKPEV SNLALAVVLL
LVLVIQAFFN AWQDFSTSRV MSSIKGMLPS DVMALRNAVQ EKIPASELVT GDLVYISMGE
KVPADLRLIE VSMDLQFDRS ILTGESEAVS GRVDMTEENF LETKNVALQG THCVNGSGLG
VVIQTGDRTV FGLIAKLSSV ETKGLTTLQR ELFRFVGIIA GMATIVAAII VILWAAWLRR
SFPSYINVSN LLIDVVSVMV AFIPEGLPVA VTLSLAKVAS RLGKHKVLCK SLSIVETLGS
VNVLCSDKTG TLTQNIMHVE NVAVLDVVFD SKDYPSTVSS SSSDVAANLS QIVAAASICN
TAVFDAGTGS TDEKKERVIV GNATDVAIFK FADSVASVDD TRRRWEEVFR MNFNSKTKFM
LILSKLAPSV SLDDGLVAPL APWDEFTPTS FLLTSKGAPE ILLPRCSFVL DPEGGAPIPI
NTSICEKICA IQERWAENGQ RVLLLARRII KGECLTHVDP HSEEFSALIE EYHRDLVIVG
LVGLIDPLKP DIKDTVKICR RAGIRFFIIT GDHPTTAVSI AGQAGIITDT STVHHASDLV
APLDSKMLSY DPDLDDRRLK GIVVTGPELQ TLKPAQVEQL CQYEEIVFAR TTPEQKLRIV
NDFKSRGNVV AVTGDGVNDA PSLKAADCGI AMGQGSDVAR EAADLVLLGD FSSIVIAIEF
GRLVFDNLKK TVLYLLPAGS FSELMPILFN ILFGLPQLLS NIQMIVICVA TDVLPALSMC
LEKPETGLLQ RKPRNVKKDR LVNWKLLLQA YGFLGMSETL CAMSMSFWYL KRHGVPFSAL
FLGFGNWPGL TDELLFTAQS VYFFTLVIMQ WGNLFATRGR RLSIFQHTPA SNWYVFPAAD
MALVLAIFFS YVPWFQKVFQ TRPIPVEFFF IPITFGLGLL FLDEMRKYLV RAYPGSFIDR
MAW
//
