ID E6ZQE8_SPORE Unreviewed; 1120 AA.
AC E6ZQE8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=K, P-type ATPase (Mediates high-affinity potassium or sodium uptake) {ECO:0000313|EMBL:CBQ69455.1};
GN Name=Acu2 {ECO:0000313|EMBL:CBQ69455.1};
GN ORFNames=sr15919 {ECO:0000313|EMBL:CBQ69455.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ69455.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ69455.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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DR EMBL; FQ311436; CBQ69455.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZQE8; -.
DR EnsemblFungi; CBQ69455; CBQ69455; sr15919.
DR VEuPathDB; FungiDB:sr15919; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000008867; Chromosome 15.
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; SFLDG00002; C1.7:_P-type_atpase_like; 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 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 167..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 880..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 952..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..191
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 121783 MW; 5149830C215A2D6A CRC64;
MAPLSRATSS GESSDEKAGA DIERADASTA RKLPRSLSFG ANLTAARSRT TRFDESTKLE
RTHSIAASLR APPRIDPSAK VPVEFRTLSI QLSHGGLADA DARHKSDKRT VRELNDLDWH
RISVDDVLTR TATSAQAGLD GAQVERRLKQ YGKNVMSKPN KRIIRKIIGY VFGGFGTLLI
GCSVLAFIAW KPLGNPNPQT SNLALAVVLL VVVVIQAVFN AWQDFSTSRI MDSIAGMLPD
TVTVIRNGSH NNVEAAELVQ GDIVIVSLGN KIAADLRLIS CSEVKFDRSV TTGESEPLAG
SVDMTDDNYL ETRNIALAGT SCVSGSAIGV VVSTGDNTVF GRIAAMTNRP KSGLTTLEKE
VRYFVLTIAA IAVALAVVCI VIWGAYLRPK HRGFMSVSQL LVNIVSILVA FLPEGMPVAV
TLSLTVIAAK LSRAKILCKQ LSTCETLGAV SVLCSDKTGT LTSNSMTATS VGVLAFESTP
QDASQHVTTG APIGHAFEQL QFVAAVCNAA VFDAATASLP VAERKIFGDA TDSAVLRMAE
EIRPVHETCR PWDQEYRLNF NSKNKFMLQL ISLRPEVEAV EVQKCIASAM STSEAAGFRA
AEDKMLLVKG GPDVLLKRSS SALDASGQVV ALTEQVKDVI VAMQSRWSSR GQRVILLARR
IVRAEQLDTT LAIEDAALAL NTDLTVVGLV GIVDPPHPEI PSVVATCRGA GIRFFMVTGD
YSKTAEAIAR QCGIVTASQI HTFDTLHSPT LALYDAQSDN DTRPQHALSL TGADLMKLSP
TDWEQICRFD EIVFSRTTPE NKLRIVREFQ QRGECVGMTG DGVNDAPSLK QADIGIAMGG
GSAVAMEAAD MVLLDSFAAI VDALLYGRLV FVNLKKTVGY LLPAGSFAEL WAVLLSFLFG
LPQILSNLQM IFVCIGTDGV SSLCLVHEQP ELDLLKRKPR STKKDRLADW RLLLHAYVFV
GIPLTLTSSA MAFWYMQRHS VPFSDMWLKY GGGTVQSTQP DRFNEVLYRA NAVYFFNLVI
QQWFNLLGWR TQTRSLFQQL PLGRKATQNV YLFPAMAVSL LIAVFFSYVP AFQHVFLTRG
VSVEHYFLPV AFGVAMLLLE EARKLVVRKW PRSGVGKVAW
//
