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Database: UniProt
Entry: G8YQX4_PICSO
LinkDB: G8YQX4_PICSO
Original site: G8YQX4_PICSO 
ID   G8YQX4_PICSO            Unreviewed;      1382 AA.
AC   G8YQX4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE            EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN   Name=Piso0_001096 {ECO:0000313|EMBL:CCE79059.1};
GN   ORFNames=GNLVRS01_PISO0C10804g {ECO:0000313|EMBL:CCE78473.1},
GN   GNLVRS01_PISO0D10871g {ECO:0000313|EMBL:CCE79059.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE79059.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|EMBL:CCE79059.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; FO082057; CCE78473.1; -; Genomic_DNA.
DR   EMBL; FO082056; CCE79059.1; -; Genomic_DNA.
DR   STRING; 559304.G8YQX4; -.
DR   eggNOG; KOG0208; Eukaryota.
DR   HOGENOM; CLU_001828_1_1_1; -.
DR   InParanoid; G8YQX4; -.
DR   OMA; FSCFQYM; -.
DR   Proteomes; UP000005222; Chromosome C.
DR   Proteomes; UP000005222; Chromosome D.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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:UP000005222};
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        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        432..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        633..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        669..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1141..1159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1171..1188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1209..1231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1251..1273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1285..1303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1323..1341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   DOMAIN          252..378
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1382 AA;  157209 MW;  C2039DBD54A9A557 CRC64;
     MTHDNSRGNS FKSKRPSMVG RRSRQNSVLS VESSVSHLVD ENTQEMYSGA ASEIIPSSIS
     SFHYPHNFRS KRAGSSVNTL SNEASPLLQT TDHTLENFDL HSVHSGSSHK SNDNALGFRF
     FLPQEIEGAP GGSTLENPED PVDYNTKWDY SVDKYDDEEI DPLSREGTSA LFRRGSRETS
     EGYDNESAFT EGEGGIGSRS SSESHFERRM RRDSEDSDKN DSSIEELLDD TVKEDLNFPA
     SSEYQRFYLA EEDLVIGVAG YKDNDLKKAL YYFFCILTLG MGYLVLRWLP KYRVSFMGDK
     TPLGKADWCV IENEYGELTI VPITKEKYDG RLSSFLNVQT EDSSKSSYSK QNYQERENDP
     FVTRIHSFTY RYLKFFYSPV EDIFKTNGNW YDIHWLNLKN TKDGISETTH KSRSQIFGKN
     DIIIDEKSVP QLLVDEVLHP FYIFQVFSIF LWLADNYYYY ATCIFLISLL SIVNSLVETK
     STLKRLKEMS VFSCEVRVWR NDFWTQINSC DLVPGDVFEV DPTLTVLPCD ALLVNGECIV
     NESMLTGESV PVSKISASPE TLQCLLDDFT TPKLAKSYLY NGTKLLKMKT SNDEPVTATV
     LKTGFNTTKG SLVRSMLFPK PTGFKFYQDS FKYIGFMTMI AFIGFTYSTY NFIQLGLPKR
     LMLLRALDII TIVVPPALPA TLTIGTTFAV NRLRKKNIFC IAPTRVNIGG KLDVVCFDKT
     GTLTEDGLDV LGIHVAENAA GRKEIVFKDI IDDIGFLESG FRGKDHYSTN NSKYLLGAMA
     ACHSLRLVDN ELIGDPLDAK MFQFTKWNFM EEYDGPHSLV YPVYESEGYI IVREFEFISY
     LRRMSVVVRD RNDDTFIFTK GAPEVMSDIC IPETLPENYE DILHRYTHQG FRVIALAYKE
     LRDVKELSSL SREETENGLS FAGFIVFENK LKESTKPTLQ KLNEANIRTV MCTGDNILTA
     VSVSRECELL EKSVQNVYFP VYQEGANETN LVWEDLNDSE NKLDPILLKP LNSNIRNEVT
     QQNSEYYRLA ITGDIFRYLL TEVKNVSLIQ RVLMKCDIYA RMSPDEKHEL VEQLQKLDYT
     VGFCGDGAND CGALKAADVG VSLSEAEASV AAPFTSRVFE ITCILDVIKE GRSSLVTSFS
     CFKYMSLYSA IQFVTVSIMY KRGINLGDFQ FLYIDLFLIL PLAIFMSWSK PYDTIVVKRP
     PANLVSIKVL IPMCCHILTL LVFQVALWLL VQQQPWYIKP VPGDDDDVQS FDNTILFLFS
     NFQYIFIAIV LSVGPPYREP VMKNVPFLVN VVVSTCISLA LFWVDGDSRW GTFMQLTNLP
     TSFYYIIILA ALANLALMYA GEDSWFVRLA KTAKRCYLRG KPRKSKKLFK NLRKEYVSLQ
     EV
//
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