ID V9ERF8_PHYPR Unreviewed; 1045 AA.
AC V9ERF8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=F443_13665 {ECO:0000313|EMBL:ETI41083.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI41083.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI41083.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI41083.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ETI41083.1}.
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DR EMBL; ANIZ01002386; ETI41083.1; -; Genomic_DNA.
DR AlphaFoldDB; V9ERF8; -.
DR EnsemblProtists; ETI41083; ETI41083; F443_13665.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_2_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02083; P-type_ATPase_SERCA; 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; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF4; CALCIUM-TRANSPORTING ATPASE 1, ENDOPLASMIC RETICULUM-TYPE-RELATED; 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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 849..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 965..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..81
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1045 AA; 114640 MW; C264CCB565BAD250 CRC64;
MADDGFRYEL ETPEAVLKHL GVTEEQGLST AEVEKRRAVH GYNELDKEEG TPLWKLVLEQ
FDDALVKILL GAAVVSFILA IFDGEEEGIG AFVEPLVILV ILVLNAIVGV WQESNAEAAL
EALKDLQPEN ARVMRDGEMV TLPARELVPG DVVEIRVGDK VPADLRLLSM KTTAIRVEQA
QMTGESTSVN KDIDALPKGT ENIIQAKTNM LFAATVVVNG LGHGVVTEVG MKTEIGKIQQ
SVQDASKEEE DTPLTKKLDE FGELLSKVIA IICIVVWIIN YKNFFDPIYG SVFKGCIYYF
KIAVALAVAA IPEGLPAVIT TCLALGTRKM AKKNAIVRKL PSVETLGCTT VICSDKTGTL
TTNEMSCVTF SHVGKSETEL VTYDVEGHTY APMGKIEGAP LGQFKAVASL ATVCALCNES
AIEYHDGKYV RIGEPTEAAL KVLVEKIGFP HDGVKQAEMQ SLRAANPEKA VQFCNEYLEE
QNKKLAVLEF SRDRKSMSVL CAKTGATSQR ATRSSASNQN VLLVKGAPEG LIDRCTHVEL
GDGTVKPLTD AGRQVLLTQV SSLARKSLRC LALAKKEDLG DLASYDGDRH HPAHKQLERT
ENFAAIESGL TFIGLASMLD PPRPEVRPMI ETCHTAGIRV ICITGDNKLT AESICHKIGI
FKDGDDLSTR SFTGAEFFAL PIEKRNQYLS DGHGMVFSRT EPKHKQQLVK MLKQLGEVAA
MTGDGVNDAP ALKQADIGIA MGITGTEVAK EASDMVLADD NFATIVAAVE EGRAIYNNMQ
AFIRYLISSN IGEVAAIFLT AALGLPEGLI PVQLLWVNLV TDGPPATALG FNPPDADIMK
KPPRRSDDAL ITGWVFFRYM VVGIYVGFAC VGVFAYWYMY YEASGDGHTL ITWDQLTHWT
KCHEWENFTV NNFDGMDFSS DPCRYFTDGK KTASTLSLSV LVAIEMFNAL NALSEDGSLI
TMPPWSNPYL MIAMVVSFAM HFVILYVDVL ADTFSVIPLD FKEWLVVLAF SLPVILIDEV
LKFIGRRMHE RELKERMEEW EKKTQ
//
