ID G3ALP7_SPAPN Unreviewed; 1320 AA.
AC G3ALP7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=SPAPADRAFT_55183 {ECO:0000313|EMBL:EGW33290.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW33290.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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}.
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DR EMBL; GL996501; EGW33290.1; -; Genomic_DNA.
DR RefSeq; XP_007374805.1; XM_007374743.1.
DR STRING; 619300.G3ALP7; -.
DR GeneID; 18871914; -.
DR KEGG; spaa:SPAPADRAFT_55183; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_1_1_1; -.
DR InParanoid; G3ALP7; -.
DR OMA; FSCFQYM; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
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:0022890; F:inorganic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:UniProt.
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; 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; 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; 3.
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; PF00690; Cation_ATPase_N; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709};
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 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 395..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 417..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 590..614
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 626..647
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1079..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1109..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1147..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1192..1210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1222..1239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1259..1279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 226..336
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 356..409
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 150744 MW; 7B186DE045CABB7D CRC64;
MRQEQVVRRS SSFDKRRRSL SRTRSRSRAN SIQSQTSSSA SILVDDNNYE MFSGATSEII
PSSITSLHYP HNFLRRSSRV SRETSPLLSP DEEVMLDHVT SRVSQAPSID IAANFKFFSA
DEIEQAQGGS TLENKEDPVD YNTNWDYNVD KFQEEDDFNQ VFESERYSPE ETPDYGSLDY
DRRRRDSDES SKSVLLDETT ETVDESTFFK QYPAKLQYQR YYLAEEDLVI GIAGYRNCWW
KSVIYYIVCL FTLGMGYLVL RWLPKYRVNL MGTRCPLGVA QWCVVENEFG ELQIVSINRQ
RFEDVLSNFM TNEGEANPVV PYIHSFTYRY IKFFYNPLED IFKTNSNWFD NRWLNFKTTK
DGISHQTHQQ RVEIFGENKI EIVDKSVGQL LVDEVLHPFY IFQVFSIFLW LADDYYYYAS
CIFIISMISI INSLIETKTT MKRLQQMSQF SCDVRVWRNE FWKQINSTEL VPGDVFELDP
SLTMIPCDCL LINGESVINE SMLTGESVPV TKFMATKDTV RLLTSNFIDA TLSKSFLFNG
TKLLKIKGND QPVTAMAIRT GFNTTKGSLI RSMLFPKPTG FKFYRDSFKY IGFMTIIAAL
GFTYSTYNFI QLGISKKIMI LRALDIITIV VPPALPATLT IGTTFAVSRL KKLQIFCISP
TRVNVAGKLD VLCFDKTGTL TEDGLDVLGV HLANNAKGRK EIIFGDLLED VNALGVSKAS
EHSTNNGKYL LGCMTSCHSL RHIDNELLGD PLDVKMFEFT NWEYNGESHV PIVFQGNSQY
EIIHEFEFMA SLRRMSVIVK SDKGSLVFTK GAPEVMQEIC QVDTLPSNYE EILHHYTHSG
YRVIACGYKQ IKEVTNRQHA ESELIFTGFI VFENKLKAST KETLQKLQGD AQIRTIMCTG
DNILTAISVA RECQLIPDKI EQIYVPSVDY KQDGEYLITW EEVNDPTNTL NPDTVKPNNI
RQDAYKLAIT GDIFRILLTE IKNKDLIQNV LMNCDVFARM SPDEKHELVE QLQKIDYTVG
FCGDGANDCG ALKAADVGIS LSEAEASVAA PFTSRVFEIS CVLDVIKQGR SSLVTSFSCF
KYMSLYSAIQ FITVTILYKT GTNLGDFQFL YIDLFLILPL AIFMSWSKPY NELIAKRPTA
NLVSPKILIP LICQIIVILI FQVILWLWVK TEPWYVKPVP GGDDSVKSSD NTVLFLFSNF
QYIIIAVVLS QGPPYRESML KNYPFMINLV FAVLISMWMF SIDGNSGLGD FMQLTNLSTA
FYCYIVLFSV VNFGVMMIGE HNWFKKVAMG YKRVFQRSKI GKSKKLFKNL NKEFSQIEIV
//
