ID A0A180H4E2_PUCT1 Unreviewed; 992 AA.
AC A0A180H4E2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=PTTG_01479 {ECO:0000313|EMBL:OAV99880.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV99880.1};
RN [1] {ECO:0000313|EMBL:OAV99880.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99880.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV99880.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99880.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC ion pump. The proton gradient it generates drives the active transport
CC of nutrients by H(+)-symport. The resulting external acidification
CC and/or internal alkinization may mediate growth responses.
CC {ECO:0000256|ARBA:ARBA00003417}.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC ECO:0000256|RuleBase:RU362083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV99880.1}.
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DR EMBL; ADAS02000001; OAV99880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180H4E2; -.
DR STRING; 630390.A0A180H4E2; -.
DR VEuPathDB; FungiDB:PTTG_01479; -.
DR OrthoDB; 1058547at2759; -.
DR GO; GO:0005886; C:plasma 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:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR CDD; cd02076; P-type_ATPase_H; 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; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF21; PLASMA MEMBRANE ATPASE; 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; SFLDS00003; Haloacid_Dehalogenase; 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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW Hydrolase {ECO:0000313|EMBL:OAV99880.1};
KW Ion transport {ECO:0000256|RuleBase:RU362083};
KW Magnesium {ECO:0000256|RuleBase:RU362083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362083};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362083};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT TRANSMEM 304..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 706..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 734..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 770..793
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 813..834
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 846..867
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 879..899
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 73..145
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 108440 MW; C6D3503258FE832C CRC64;
MSDPDPDPQL QPEKQSTLDP TSITTTEKTS DGSKKPGRFD KTFESEEKPV HALVDMSLIQ
LKAEDLYDKD KVDLEQVELD DVWALLQCTE EGLTETEAQR RLEIFGPNKL ETKEINPFLQ
FLGFMWNPLS WVMEAAAIVA IALSNGEGEP PDWQDFVGIV LLLLINSAIG FYEERSAGNA
VAALMDSLAP KAKVRRDGSW KEIDSAQLVP GDIVAFKIGD VVPADNRLYD AINVSIDQAA
LTGESLPASK KLGDQCFSGS TCKQGEAEGV VIATGANTFF GRAAALVGAD DDSSGHLQKI
LAQIGTFCLV SIGIFIILEI LVMYAGFRYR YRRGINNLLV LLIGGIPIAM PTVLSVTLAV
GAQQLAKYKA IVTRITAIEE LAGVTILCSD KTGTLTTNKL TIDKSTVKTY GEYDVDAVCL
LAAYASRTEN QDAIDTCVVG TVGTGPARAG IKLLDFKPFN PVDKRTEITY LEEATGKMKR
VSKGMTGVII ELCSRNKTED VENQLEADVE EFARRGLRAL AVAFEDVPSN DKDAPGNGFE
LVGLLAIFDP PREDTQQTID DAMLLGVRVK MVTGDQLAIA KETGRRLGLG DHMYPAKVLK
DGPEPGGKHL TLDEMILDAD GFAGVFPEHK YEIVKRLQGL GHLCAMTGDG ANDAPALSRA
NVGIAVEGAT DAARGAADIV LTEPGLSTIV HAIRQSRIIF QRMRNYSIYA CAVTIRIVVG
FAVLVFAYKF DFPPFMVLII ALLNDGTIMT LSVDRVLPSM TPDHWDLAEI FIFATFYGLY
LALSTIILVV VIRETSFFPD RFGVDTITDI NDFKLHMIIY LQVAQISQAL IFITRSHGFF
FMERPSFALM GAFCLAQLIS SIIAAYGNWG FTQVEGISGG WIGIVWIWNI IWFLPMDFIK
FSVKYGIRAW NAKRGVKPQS LKLVDEATGI PLTRTASRHE SLYSNHATWI KRAQRRVGLK
KGTTIDPTEL HRVGSHQARA TGAALRHSTS AA
//
