ID A0A2P7Z068_9ASCO Unreviewed; 1111 AA.
AC A0A2P7Z068;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=C7M61_001302 {ECO:0000313|EMBL:PSK41615.1};
OS Candidozyma pseudohaemuli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Metschnikowiaceae; Candidozyma.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK41615.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK41615.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK41615.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:PSK41615.1}.
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; PYFQ01000001; PSK41615.1; -; Genomic_DNA.
DR RefSeq; XP_024716314.1; XM_024856715.1.
DR AlphaFoldDB; A0A2P7Z068; -.
DR STRING; 418784.A0A2P7Z068; -.
DR GeneID; 36564692; -.
DR VEuPathDB; FungiDB:C7M61_001302; -.
DR OrthoDB; 158672at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:TreeGrafter.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IEA:TreeGrafter.
DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IEA:TreeGrafter.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:TreeGrafter.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:TreeGrafter.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:TreeGrafter.
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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR050510; Cation_transp_ATPase_P-type.
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:SF21; CATION TRANSPORTING 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
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 164..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 905..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 948..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1090
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..188
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1111 AA; 123946 MW; 891FD1778DA70CDD CRC64;
MGDKRNSYLV NTVSAETSFT KDDDSDLSFA DKPTNDGIRF ADGERKDGVS VPGRARRRLS
FHSLNRDDDL FTIRERVQPD VVLPAVFKTI SHEVETRSEH QTELDPTASK FAGITYHTDD
PEKLVVDFGT DVTYGLSSAQ LVARRKEFGP NVQSKPPSRL LKKIFMYFFG GFGGLLLTGG
ILCIVSWKPL GNPDPAIANL ILGIILLFVF LFQAMFNFFQ DFSSSRVMDS IHNMIPVETL
VVREGNFEQV DSKILVPGDI IKFGTGVKVP ADIRIVEASP DLSFDRSILT GESDAVPATY
RSDPLHSNYL ESNCIAMQGT FVVGGSGKGI VVATGDHTIF GTIAKLTSEP KKGLTPMQWE
ILRFVLMTTS IIVALVVLII ILWCAWLNKD HKGWLTVSGL IVDIVAVAVA FIPEGLPIAL
TTCLIITANQ MRKSKILCKT LSTVETLGSV SVLCFDKTGT LTRNNMTVTD VCKGDDEDSV
AELKSQVSGE TEFTDALTTH FLTICSLCND ATVSKNGSLN GNATDKAVFT YSDSIMPKWE
LEQKWSSRFQ IAFNSKDKYM ANLLDANSSF QMPEKTWSQI GIELPLGQEE NFSLLTVKGA
PDILLKRCTS ILQRDGDDRV VVQNLDDQIL DKIRTIQQKW SREGKRVIML TSKMVQPSTI
DFTDRFSATE RLREELSDGM TLVGMLGIED PPRKNIDTVI SRLRDAGVKI VMITGDFELT
GLSIAKQVGI VTGNVDTYQD VIVAATKEPV SNDDTPIPRA VSIVGSDLNT LTEDEWSRVV
RYEELVFTRT TPEQKLMIIK QFQKHKHVIG MTGDGINDSP SLKQADIGIS LIDASDIAKE
ASDIILMNNT GAEDELFNSI IDALEYGRLV FENLRKTIGY LLPAGTYAEL WPVLMNVIFG
MPQMLLSFLM IIICCITDCA GAIILAYESS ERNLLQKKPR SVTKEKLVDW KLFLHSYFTI
GTYYCFTSFM VAFLNLTRRG YKFSDFSLSY GTYEDLPDVE DYINMSSSIY FVNLVIMQLF
NLFAMRTRYL SMFQHLPMKN KYLFAVVPIT LGVTFIVNYI PAIHSALGTA QVPVEYYFIA
VGFGAVVLVY DELRKWYNRK HPNSFLAKIA W
//
