ID A0A1L0DGI9_9ASCO Unreviewed; 1338 AA.
AC A0A1L0DGI9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=SAMEA4029010_CIC11G00000000421 {ECO:0000313|EMBL:SGZ51526.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ51526.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ51526.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ51526.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR EMBL; LT635758; SGZ51526.1; -; Genomic_DNA.
DR STRING; 45354.A0A1L0DGI9; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000182334; Chromosome iii.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 1.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 418..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 614..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1130..1147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1167..1189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1246..1263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1283..1305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 235..359
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 156..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 151973 MW; 9B3BB139E2624A92 CRC64;
MDSMVDENNY EMFSGAASEI IPSSISSFHY PHHFGSHRSE DGVLRETSPL LTTARLYGTG
GRDLDLRPIQ LNASTDTASV NFRFFSPDEI EQAPGGSTLE NPADPVDYDT NWDYSVDKYE
ENEDAVESVH EMQAYGRSRG SLSSERFLEG ARSFAERLPR SPHQRREEVV EDDSDNESTY
ATMLDDRYRR RSEDSGSKSS RSIGLRSEVS DSDEHAFLED FLPVAKYQRY YLAEEDIVIG
IAGYSNCWWK VFVYYLICIF SFGIGYLILR WLPRYRINLK GTRCPLGKAD WVVIENEYGE
LTIKDISRMR FGGRLSHFMT LNSKEDDDGQ VHLDDVKESN PTIPFILSFD YRYLNFFYNP
VEDIFRTNST WYDLHWLNVK NLRDGTSQTL QEQRATIFGH NNINIEEKSI AQLLMDEVLH
PFYVFQIFSI FLWLADDYFY YASCIFIISV VSIANSLIET KSTIKRLQEM SKFSCDIRAW
RNEFWTQIDS NDLVPGDVFE VDPSMTVLPC DALLVNGECV VNESMLTGES VPVSKISATN
ETVKYLTENF THPVLAKSFL YNGTKLLKMK SSNDEPVLAM VLKTGFNTTK GSLIRSMLFP
KPTGFKFYQD SFKYIGFMTL IAFIGFIYST YNFIQLGLSK RIMILRALDI ITIVIFCIAP
TRVNIGGKLD VACFDKTGTL TEDGLDILGV HPTKNAEGRK EIVFEEILET IEKLGNEVEL
SSHKTQSDKY LLGCMASCHS LRLIDDKLVG DPLDVKMFDF TGWNFTEDFG GSNIPLVYEH
VGKETFGYKI FKEYEFIAAL RRMSVVVEKD SLKYVFTKGA PEVMLDICDP TTIPANFEEL
LHKYTHGGYR VIACAYKELN KKVNIKSLER GEAENDLSFA GFIVFENKLK ASTKATLKEL
RAAAIRTVMC TGDNVLTAVS VGRECELIDP AVTQVYIPRF ASDEEFSLTG DTGLIWEDIH
DPQNKLDPVT LQRTSRDIRY DVSEYILALT GDVFRYVLAE LQRENITQAI LMRCNIFARM
SPDEKHELVQ QLQKLDYTVG FCGDGANDCG ALKAADVGIS LSEAEASVAA PFTSRIFEIS
CVLDVIKEGR SSLVTSFSCF KYMSLYSAIQ FITVSILYKR GTNLGDFQFL YIDLFLILPL
AILMSWSSPY SGLVIKRPTA NLVSPKVLIP LVCHIVVILV FQIAVWLYVQ DQPWYVKPIP
SDSDDDVKSS DNTVLFLFTN FQYILNAVVL STGPPYREPT VKNKPFLINL VVALMLSVGI
FFIKGDSWWG DFMQLTDMST LAYWIILLAG MMNFLVLTYG ENHLFKVIAQ MYKRLVHGRV
AISKKKFKNL GKDFVPIV
//
