(data stored in ACNUC7421 zone)

SWISSPROT: Q750N5_ASHGO

ID   Q750N5_ASHGO            Unreviewed;       909 AA.
AC   Q750N5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 132.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   ORFNames=AGOS_AGL085C {ECO:0000313|EMBL:AAS54405.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54405.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54405.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU362083};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|RuleBase:RU362083}.
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DR   EMBL; AE016820; AAS54405.1; -; Genomic_DNA.
DR   RefSeq; NP_986581.1; NM_211643.1.
DR   STRING; 33169.AAS54405; -.
DR   EnsemblFungi; AAS54405; AAS54405; AGOS_AGL085C.
DR   GeneID; 4622880; -.
DR   KEGG; ago:AGOS_AGL085C; -.
DR   HOGENOM; HOG000160005; -.
DR   InParanoid; Q750N5; -.
DR   KO; K01535; -.
DR   OMA; DNAPFSK; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; IBA:GO_Central.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750N5.
DR   SWISS-2DPAGE; Q750N5.
KW   ATP-binding {ECO:0000256|RuleBase:RU362083, ECO:0000256|SAAS:SAAS00832164};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW   Ion transport {ECO:0000256|RuleBase:RU362083};
KW   Magnesium {ECO:0000256|RuleBase:RU362083};
KW   Membrane {ECO:0000256|RuleBase:RU362083, ECO:0000256|SAAS:SAAS00832173};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362083,
KW   ECO:0000256|SAAS:SAAS00832168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Translocase {ECO:0000256|RuleBase:RU362083, ECO:0000256|SAAS:SAAS01237809};
KW   Transmembrane {ECO:0000256|RuleBase:RU362083,
KW   ECO:0000256|SAAS:SAAS00832175};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362083,
KW   ECO:0000256|SAAS:SAAS00832181}; Transport {ECO:0000256|RuleBase:RU362083}.
FT   TRANSMEM        94..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        122..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        277..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        310..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        673..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        700..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        736..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        806..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        847..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          50..121
FT                   /note="Cation_ATPase_N"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..48
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   909 AA;  99181 MW;  98CD26ED2C4631F9 CRC64;
     MSGAVMEPKR EEVVKPVMSD DEEEDIDQLI EDLQSNQGLD EEDEDEDLAP GSARPVPEEL
     LQTDPSYGLT SDEVSRRRKK YGLNQMSEAN ESMILKFVMF FVGPIQFVME AAAILAAGLE
     EWIDFGIICA LLLLNAAVGF IQEFQAGSIV EELKKTLANS AVVIRDGSLV EIPANEVVPG
     DILQLEDGVI IPADGRIVTE GCFVQIDQSA ITGESLAVDK RYGDATFSSS TVKRGEGFMI
     VTATGDSTFV GRAAALVNKA SAGSGHFTEV LNGIGTILLI LVILTLLVVY VACFYRSIDI
     VTILRYTLAI TVVGVPVGLP AVVTTTMAVG AAYLAKKKAI VQKLSAIESL AGVEILCSDK
     TGTLTKNKLS LHEPYTVEGV EADDLMLTAC LAASRKKKGL DAIDKAFLKS LINYPRAKAA
     LTKYKVLEFH PFDPVSKKVT AIVESPEGER IVCVKGAPLF VLKTVEENHL IPEDVKENYE
     NKVAELASRG YRALGVARKR GEGHWEILGV MPCMDPPRDD TAQTVNEARH LGLRVKMLTG
     DAVGIAKETC RQLGLGTNIY NAERLGLGGG GDMPGSELAD FVENADGFAE VFPQHKYNVV
     EILQQRGYLV AMTGDGVNDA PSLKKADTGI AVEGATDAAR SAADIVFLAP GLSAIIDALK
     TSRQIFHRMY SYVVYRIALS LHLEIFLGLW IAILNQSLNV HLVVFIAIFA DVATLAIAYD
     NAPYDPQPVK WNLPRLWGMS IVMGILLAIG SWITLTTMFM KKGGIIQNYG AIDHIMFLEI
     SLTENWLIFI TRASGPFWSS IPSWQLSGAV FIVDVIATLF CVFGWLHEKN VVDAGVLRPR
     THIVTVVRVW IFSFGVFCIM GGAYYLMFTS KSFDRFMNGK PLREKPSGRS VEDFLVAMQR
     VSTQHEKEN
//

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