(data stored in ACNUC7421 zone)

SWISSPROT: Q750P4_ASHGO

ID   Q750P4_ASHGO            Unreviewed;      1096 AA.
AC   Q750P4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 135.
DE   SubName: Full=AGL097Cp {ECO:0000313|EMBL:AAS54394.2};
GN   ORFNames=AGOS_AGL097C {ECO:0000313|EMBL:AAS54394.2};
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:AAS54394.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54394.2, 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   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000256|SAAS:SAAS00832166}.
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DR   EMBL; AE016820; AAS54394.2; -; Genomic_DNA.
DR   RefSeq; NP_986570.2; NM_211632.2.
DR   STRING; 33169.AAS54394; -.
DR   EnsemblFungi; AAS54394; AAS54394; AGOS_AGL097C.
DR   GeneID; 4622869; -.
DR   KEGG; ago:AGOS_AGL097C; -.
DR   HOGENOM; HOG000265621; -.
DR   InParanoid; Q750P4; -.
DR   KO; K01536; -.
DR   OMA; EPIVIIM; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008556; F:potassium transmembrane transporter activity, phosphorylative mechanism; IEA:EnsemblFungi.
DR   GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; IBA:GO_Central.
DR   GO; GO:0008554; F:sodium transmembrane transporter activity, phosphorylative mechanism; IEA:EnsemblFungi.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:EnsemblFungi.
DR   GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblFungi.
DR   GO; GO:0009268; P:response to pH; IEA:EnsemblFungi.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblFungi.
DR   CDD; cd02086; P-type_ATPase_Na_ENA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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; IPR006414; P-type_ATPase_IID.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01523; ATPase-IID_K-Na; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750P4.
DR   SWISS-2DPAGE; Q750P4.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00832164};
KW   Membrane {ECO:0000256|SAAS:SAAS00832173, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00832168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Translocase {ECO:0000256|SAAS:SAAS01237809};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00832175, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00832181,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        810..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        884..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        939..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        986..1007
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1019..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..94
FT                   /note="Cation_ATPase_N"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1096 AA;  120812 MW;  F2B1BF4586BAFFFF CRC64;
     MSKSQKVAIS GGTDVYERTD FHALPAHEVA RLLGTDLRRG LTAEEARARL EVVGDNTLGE
     EEGINVRAIL LKQMCNAMIL VLIISMVIAL AIKDWISGGV IAFVVALNVS IGAYQEYNAC
     KTMNSLKDLS TPSARVIRNG EDVVMASAQV VPGDIVQVRV GDTVPADLRL VEALNLETDE
     ALLTGEALPV AKDPAAVFEQ DTPVGDRLNL AFASSTVSKG RATGIVVRTG LRSEIGKIAE
     SLQGKQSLIS RDENKSGLQN TVLTVKASVG SFLGTNVGTP LHRKLAKLAL ILFAIAVLFA
     LIVMATQKFI VNREVAIYAI CVALSMIPSS LVVVLTITMS AGAKVMSTRN VIVRRLDSLE
     ALGAVNDICS DKTGTLTQGK MILKQLWVPE FGTVVVNRSN VPFDPTVGDV SLIPRFSPWE
     YQHDEEEDVG IIANFKQRWQ SNSLPKGLNP RKFESWLHTA TLANIATVFK DSDSKEWRAH
     GDPTEIAIQV FATRMDHPHH ALTTEQDEED SDSSQQNDAA RIYEHAAEFP FDSSIKRMSA
     VYINLRDKNT RHVFTKGAFE RVLKCCTRWK LDPGTGVTHP LTEDDLEIIQ KNVDTLSNEG
     LRVLAFATKT IPAEEAESLG ERLTKDRDFV ESDLIFQGLV GIYDPPRVET AGAVKKCHRA
     GINVHMLTGD FPGTAKAIAQ EVGILPHNLY HYPKEVVDIM VMTATQFDSL TDEELDQLPV
     LPLVIARCAP QTKVRMIDAL HRREKFCAMT GDGVNDSPSL KKANVGIAMG INGSDVAKDA
     SDIVLSDDNF ASILNAVEEG RRMSDNIQKF VLQLLAANVA QAIYLMLGLT FLDEDKLSVF
     PLSPVEVLWI IVVTSCLPAM GLGLEKAAPD IMEKPPNDSK AGIFTWEVIV DMIVYGLVMA
     VCCLGCFVSI IYKDGHGNLG TNCNVEYSDS CKSVFSGRAA TFATMTWCAL ILAWEVIDMR
     RSFFAMKPET DTPYTQVFKD IWSNQFLFWS VIFGFTSVFP VVYIPVINTK VFLHIGIGYE
     WGIAFAFSLV FWLVAEFWKF AKRRYYRNKD RAINPESDLE NRRLHDPFEK YSSTLSRATT
     NIGTFRVTAN SEKDIT
//

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