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Database: UniProt
Entry: N1R8U1_FUSC4
LinkDB: N1R8U1_FUSC4
Original site: N1R8U1_FUSC4 
ID   N1R8U1_FUSC4            Unreviewed;      1099 AA.
AC   N1R8U1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Sodium/potassium-transporting ATPase subunit alpha-2 {ECO:0000313|EMBL:EMT62633.1};
GN   ORFNames=FOC4_g10006258 {ECO:0000313|EMBL:EMT62633.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT62633.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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DR   EMBL; KB726995; EMT62633.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1R8U1; -.
DR   STRING; 1229665.N1R8U1; -.
DR   HOGENOM; CLU_002360_4_1_1; -.
DR   Proteomes; UP000016929; 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:UP000016929};
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        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        882..903
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        933..954
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        993..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1030..1048
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1060..1078
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..182
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  122450 MW;  2251C681BFF9D91A CRC64;
     MSDPDIRGTK ESDPEAQIQR ITFQDGPERG REEHDAHRLG RTLSRSLSRR RSHSSSRSRI
     HPTSPYSGVQ IEYRTLSIQV TEAKQVEPTE DSKAAAGQKT DEDYFSKLQY HELQTEQLCQ
     QLNVDVGAGL SESSAATRLE RDGKNTLPHP KTNYIKRTLK YIFGGFCSVL WVGAIIFFLC
     WQPLSNPPSN QNLSLAVLIL IVIFLQAGFS AFQDWSTAKT MNAILDLLPS FAMVKRDGEL
     KSLPTVGLVA GDVVHLKVGD KVPADLRIVS HSGDIRFDRS VLTGESDEIE GAVDATDANF
     LESRNIAFMG TTVMNGNGVG VVILTGGRTV MGRIATSTSG VKDSAALIQR EITRFVMIIV
     CMTIILALAI LLTWVGWLRV DHHAYMSVPA MLVNVMACVV AFIPEGMPVA VALTLMMIAR
     RMKAVNVLPK GLSTVETLGC VNVICSDKTG TLTQNQMFVS SVAFVDKKFD SSDEFQHLLH
     SKDVTEPATA LQRAALLCND ASFDPTTNHL PLHERTIQGN ATDSAVFRFA AYGPSGDSFR
     KTLPRIFEVP FNSKNKWMLT VFQSDDERGA YRVIIKGAPD ILLAGCTKYW SSESNSVETL
     TRDARIKFQE IQDEASRRAE RVIVLCEKFI TPRAVAGTNS FSDEITHSAI QDLTVVGMLG
     IIDPHRPEIP ATVEQCRRAG TRFFMVTGDY ALTAAAIARN TGIFSCQQDP DTIDTLYTGN
     QITESEKPKR KAKKGDRAEI IKRSLLLEGA NLSRLSQEDW DVVCAYEEIV FARTTPEQKL
     RIVTELRERD NVVAVTGDGV NDAPALRAAD VGVAIVTGSD VAIEASDLVL LDRFDSIIDA
     MRLGRLVFQN LQKVISYLLP AGSWSEIWPV ILNVWFGVPL PLSAFLMIII CVFTDLFLSL
     SLIMEKEEFD LLSLPPRNHK RDHLINAKIY TQAYLFTGFM ETITAHAMFF FYMWKYAKMP
     VSELFFLFEG YTEGYRGYTA AELTKFNNTG QCVYFVTLVF LQWGNILAVR NRRLSIFQAN
     PLSKAHRNPW LILSMLISLC IAIFVTEVPG IQNLFDTESV PIEFWLIPIP LGLGILLVDE
     IRKFIVRTYP KSFVARIAW
//
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