ID A0A024UL57_9STRA Unreviewed; 1095 AA.
AC A0A024UL57;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:ETW07186.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07186.1};
RN [1] {ECO:0000313|EMBL:ETW07186.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07186.1};
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|ARBA:ARBA00006000,
CC 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; ETW07186.1; -; Genomic_DNA.
DR EMBL; KI913954; ETW07189.1; -; Genomic_DNA.
DR RefSeq; XP_008863276.1; XM_008865054.1.
DR RefSeq; XP_008863282.1; XM_008865060.1.
DR AlphaFoldDB; A0A024UL57; -.
DR EnsemblFungi; H310_01793-t26_23; H310_01793-t26_23-p1; H310_01793.
DR EnsemblFungi; H310_01793-t26_24; H310_01793-t26_24-p1; H310_01793.
DR EnsemblProtists; ETW07186; ETW07186; H310_01793.
DR EnsemblProtists; ETW07189; ETW07189; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; 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 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: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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, 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 866..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 898..915
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 936..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 997..1016
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1068..1088
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 1095 AA; 118947 MW; 589D8EEE4EEDCF02 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
VRVDPTDDQL ISLAQTSTTW LALGDLDTLL DLDFDLTITG AALDVVIASS LPPLLVSRLV
QKAKIFARTK PHTKTWIVGR LMDAGLFVGM TGDGTNDCGA LKAAHVGLAL SDAEASIVAP
FTSRGKAIED VVALLREGRC ALTTSLLSFK FMVMYPIIET AMVAYLNHMQ ASFSNNQYLF
GDMFVVLGMS VLMLQTPPAA NLTKARPPTS LFSPTIVWSV ASQSVVFALY FSATLAVAQR
QPWFCALPDV AAGRAHCYPY RPNESGDMTT HAFEVSIVWL LGHWHYVVLA IAFNLNDPFR
EPAWHNRAFV LYTAAVGAIL LGLVLWPGNA MAVAWLDLTT PLPLSFCFEM AASCALALVT
AVGVEMAVRI TFAQS
//
