ID G8YKT1_PICSO Unreviewed; 1138 AA.
AC G8YKT1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Piso0_001441 protein {ECO:0000313|EMBL:CCE88665.1};
GN Name=Piso0_001441 {ECO:0000313|EMBL:CCE88665.1};
GN ORFNames=GNLVRS01_PISO0F06473g {ECO:0000313|EMBL:CCE88665.1};
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:CCE88665.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {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).
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DR EMBL; FO082054; CCE88665.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YKT1; -.
DR STRING; 559304.G8YKT1; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; G8YKT1; -.
DR OMA; QWGYSIV; -.
DR Proteomes; UP000005222; Chromosome F.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:UniProt.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 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; 3.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000005222};
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 125..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..972
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..141
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 125524 MW; 3E27D331B7D0C923 CRC64;
MSISSTEAEG GRKKKSFLTV ERNPPPEYVD ASSVNSGSPL AVGRFEIGHH DMTELHDPKS
IKKLHELGGI SSLEAALHTN LKSGLNTYDK EDMDQRRKFY GANRLPVRAR KNFFQLCFEA
MKDKVLILLS VAAVVSLALG LYETFGTGPE YEHGERVPKV DWVEGVAIIV AIVIVVVVGA
ANDFQKERQF AKLNAKKEDR ELAVIRNGNQ QMISIYDLQV GDIMCVETGD IISADSILVS
GEVECDESSL TGETDTIRKV PANEALKVYE EHLPTTEDLG SREISFADPF LISGSKTLSG
RGHSIVTAVG LNSIHGRTMA SLSEEGETTP LQERLDGLAE GISKYGFLAA LILFIVLFIR
FCIEIAPGGR NHDLKGPEKG KRFMDILITS ITIVVVAVPE GLPLAVTLAL AFATTRMAQN
GNLVRVLRSC ETMGGATAIC SDKTGTLTEN RMRIVKAYFG SGEFDDTVGS TGAKSSETLR
GLPSELLSAI CENIVHNSSC FENQNYDEEL ARRVKQRPKK QSLIVSLFKN DDSKRQKDLA
KWSEANEPYI GNKTESALMI LATEKLGLFK DSSLEELRSR KYSSVVQVIT FESSRKWSGL
VMRIGDNYRL YVKGAAEIVL KNCGFIYNAN GEVVKIDRNT REEALNKVDE YANDALRAIT
LCHRDFAGLS SWPPAGFESR ENPREADPDL LLYTSGMVED NKKLMILDGT VGIQDPLKEG
IPEAVNNCKL AGVSVRMVTG DNLITAKAIS RSCNILTPDD LSNEHAYMEG PAFRKLSPDE
RKSIAPDLRV LARSSPEDKR ILVETLRSVG EVVAVTGDGT NDAPALKLAD VGFSMGIAGT
EVAREASDII LMTDDFTDIV QAIKWGRTVA SSIKKFIQFQ LTVNITACVL TFVSAVASSE
NKSVLTAVQL LWVNLIMDTL AALALATDKP DDSFLRRKPA GRNSPLISVS MWKLIIGEAI
TQLTVTFILH FAGDALFFGD EPITTRQNRQ LDAMTFNTFV WLQFWKLVVC RKLDEADEVR
NIRGRITREN LDFSQHLFRN WYFIIIAAII GGCQVLIMFV GGAAFSVVRQ TPGMWATALL
CGFISIPVGI ILRIIPNHWV VAIFPTRLFN CILYYLSFSF LKRKRQTDLE IGDVPNKD
//
