ID J3NLZ2_GAET3 Unreviewed; 1174 AA.
AC J3NLZ2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=20342755 {ECO:0000313|EnsemblFungi:EJT82323};
GN ORFNames=GGTG_02297 {ECO:0000313|EMBL:EJT82323.1};
OS Gaeumannomyces tritici (strain R3-111a-1) (Wheat and barley take-all root
OS rot fungus) (Gaeumannomyces graminis var. tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Gaeumannomyces.
OX NCBI_TaxID=644352 {ECO:0000313|EMBL:EJT82323.1};
RN [1] {ECO:0000313|Proteomes:UP000006039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3-111a-1 {ECO:0000313|Proteomes:UP000006039};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Gaeumannomyces graminis var. tritici strain R3-
RT 111a-1.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EJT82323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R3-111a-1 {ECO:0000313|EMBL:EJT82323.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EJT82323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R3-111a-1 {ECO:0000313|EMBL:EJT82323.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Gaeumannomyces graminis var. tritici R3-111a-1.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:EJT82323}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R3-111a-1 {ECO:0000313|EnsemblFungi:EJT82323};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:EJT82323}
RP IDENTIFICATION.
RC STRAIN=R3-111a-1 {ECO:0000313|EnsemblFungi:EJT82323};
RG EnsemblFungi;
RL Submitted (APR-2018) to UniProtKB.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL385395; EJT82323.1; -; Genomic_DNA.
DR RefSeq; XP_009218332.1; XM_009220068.1.
DR AlphaFoldDB; J3NLZ2; -.
DR STRING; 644352.J3NLZ2; -.
DR EnsemblFungi; EJT82323; EJT82323; GGTG_02297.
DR GeneID; 20342755; -.
DR VEuPathDB; FungiDB:GGTG_02297; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000006039; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF346; 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 PRINTS; PR00120; HATPASE.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000006039};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 226..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 471..498
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 921..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 954..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 996..1017
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1071..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1103..1121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 146..242
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 13..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 124872 MW; 65EC443747A5A9A4 CRC64;
MVPGIFNKAV ESIDENSPVE PRPFEPVVLA GHGRSPSDAT TIRPFTGAST ASPDGSITSY
SHSKNPFATP SLRSFSSLAT AVAVPVDVEA ALRPDPGTEA DFTVAGDNPF AFTPGQLGKL
LNPKSLDAFR ALGGLRGIEK GLQTDVASGL SVDETAAPFR VSFDQAVGGG GLPQKSIEKS
GNHNAAAAAA AGRYADRSRV FGKNVLPSKK ATPIYKLMWA AYKEKVLIVL SVAAAISLAL
GLYETFRPNH KTNEVRVDWV EGVAICIAVI IVVVVGGLMD WNKERAFVRL NAKKDDREIK
VIRSGKSQLI NVAELVVGDV VQLEPGDVAP VDGIFISGHD VKCDESSATG ESDALKKMGG
EQVMRMLESG TRAKNLDPFI ISGARVLEGV GTYVATSVGV HSSFGKIMMS IRIEADPTPL
QVKLAGLAVN ISKWAVSSAS FLFFVLLFRF LANLGNDARE PSEKASFFLE IFIVAITVIV
VAVPEGLPLA VTLALAFATK RLLKENNLVR VLRSCETMGN ATTVCSDKTG TLTTNKMTVV
AGTFGSTKFT KPGGATTPSS SDSDSDSSAM NVAQWSSSIS PAARAAIVQS VAVNSTAFEG
TDDNGQPTFI GSKTETALLQ LARDHLGLQS VQEARANEWV VQMMPFDSAK KCMAAVIGLR
GGAGYRLLVK GASEILLEYC DKKAGVSGPS FSAEALDVTD LTASDTMALR ATIEAYARGS
LRTIGLVYRD YPSWPPPGVH ADEDGHVKLA ELLRGLVFLG VVGIQDPVRP GVPEAVAKAK
KAGVAVRMVT GDNAVTAKAI ATECGIYTDG VIMEGPAFRA LSDADMTAVV PRLQVLARSS
PEDKRVLVRK LKALGETVAV TGDGTNDAPA LKAADVGFSM GISGTEVAKE ASQIVLMDDN
FSSIIVALKW GRAVNDSVQK FLQFQITVSI TAVILAFVSA VTHPEMKSVL TAVQLLWVNL
FMDTFAGIVL ATDPPTDSIL NRPPQGKAAP LITMNMWKMI VGQSIFQLAV TVTLYFAGSR
IFGFDPSNRD QMLQLSTMVF NTFVWMQIFN ELNCRRLDNG FNMFEGLQRN PYFICINLFM
IGCQVAIVFV GGAVFSVTPI GPAQWAVCIV LPLFSLPWAM VVRSFPDAWF ESVVGVVVAP
FVPAYAGLAK VFAPLSRLVL RKGASEGDAE KGRS
//
