ID A0A024ULW7_9STRA Unreviewed; 1106 AA.
AC A0A024ULW7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=H310_01793 {ECO:0000313|EMBL:ETW07185.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07185.1};
RN [1] {ECO:0000313|EMBL:ETW07185.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07185.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|RuleBase:RU362082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR EMBL; KI913954; ETW07184.1; -; Genomic_DNA.
DR EMBL; KI913954; ETW07185.1; -; Genomic_DNA.
DR RefSeq; XP_008863274.1; XM_008865052.1.
DR RefSeq; XP_008863275.1; XM_008865053.1.
DR AlphaFoldDB; A0A024ULW7; -.
DR EnsemblFungi; H310_01793-t26_13; H310_01793-t26_13-p1; H310_01793.
DR EnsemblFungi; H310_01793-t26_14; H310_01793-t26_14-p1; H310_01793.
DR EnsemblProtists; ETW07184; ETW07184; H310_01793.
DR EnsemblProtists; ETW07185; ETW07185; H310_01793.
DR GeneID; 20078843; -.
DR VEuPathDB; FungiDB:H310_01793; -.
DR OrthoDB; 6047at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; 2.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Translocase {ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 909..926
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 947..969
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1008..1027
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 148..223
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1106 AA; 120036 MW; B8376F35DAAA2D9A CRC64;
MADALATTGS SLPPAFDPAP TVTIVLSTYN ERDPLIKPAA PDLSLLATSK AEYVAIAGFR
ASAVWQAGFV LLCVVTGGVL WIMTTWWPQI YTYLARVRVR SLGVADIVLV RDSHGLMHEC
AVVHSEGGMV RTFEWKHQRY LYIQQSGSFE RVPAMLLDSL ESVTRSLQTG LASSVVADRT
AFYGPNTMEL KTPSLIRLLV EKVVHPFYLF QLISVALWLE EAYTTYALAI LAMSISSIAY
EVHSQVTNAS QMQALVACAI QVQVKRDGGV QSVPASALVL GDFVLVQEQV VAADMVIVVG
ECMADESSLT GEAIPVSKQP SHDDPTKSVL ECHKSSVLCA GSTVVRVKGD SVWAVVTRVG
FSTTKGDLLR QILYPDDVPF QMVTDSYRYL LALSIVAGLT SLQRIYDAIQ AHSTLGDLVI
SVFDLISTTI PAALPMILTV GVGFSLTRLQ QARLCCIDAQ KINVAGHINC FCFDKTGTLT
SDHLDFEGVD MCDGSPLTTK PTSRDVEYAL ASCHGLSVDD QGVVAGYSLE RDMFAATEYT
LSATTNEVQS PNGGHVSLRY DRRYPFDAAL QRSSVVVQAS NEPHFRRIYV KGSPEAIADI
CTGIPSDFYA RVHRYASEGL YCVALAMKKM DGYEPATSRA TVESDVTFLG FLLFLNPIKA
ASRGVIETLE RANIDVRIIT GDNALTAMHV ARELNMHLTT SMLYLDVSPS DGSIMYQLYP
TSTTWLALGD LDTLLDLDFD LTITGAALDV VIASSLPPLL VSRLVQKAKI FARTKPHTKT
WIVGRLMDAG LFVGMTGDGT NDCGALKAAH VGLALSDAEA SIGMFLSSAA QIGLGVVRRR
VEVRSAVVVA PFTSRGKAIE DVVALLREGR CALTTSLLSF KFMVMYPIIE TAMVAYLNHM
QASFSNNQYL FGDMFVVLGM SVLMLQTPPA ANLTKARPPT SLFSPTIVWS VASQSVVFAL
YFSATLAVAQ RQPWFCALPD VAAGRAHCYP YRPNESGDMT THAFEVSIVW LLGHWHYVVL
AIAFNLNDPF REPAWHNRAF VLYTAAVGAI LLGLVLWPGN AMAVAWLDLT TPLPLSFCFE
MAASCALALV TAVGVEMAVR ITFAQS
//
