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Database: UniProt
Entry: R1E6D7_BOTPV
LinkDB: R1E6D7_BOTPV
Original site: R1E6D7_BOTPV 
ID   R1E6D7_BOTPV            Unreviewed;       658 AA.
AC   R1E6D7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Putative phospholipid-translocating P-type atpase protein {ECO:0000313|EMBL:EOD42937.1};
GN   ORFNames=UCRNP2_10349 {ECO:0000313|EMBL:EOD42937.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD42937.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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DR   EMBL; KB916926; EOD42937.1; -; Genomic_DNA.
DR   RefSeq; XP_007589575.1; XM_007589513.1.
DR   AlphaFoldDB; R1E6D7; -.
DR   STRING; 1287680.R1E6D7; -.
DR   KEGG; npa:UCRNP2_10349; -.
DR   eggNOG; KOG0210; Eukaryota.
DR   HOGENOM; CLU_416763_0_0_1; -.
DR   OMA; APHEYHR; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
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; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        574..593
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..229
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  71892 MW;  BA9325149A42D45A CRC64;
     MSAPHEYHRP NGPDSPDDSD EDLELLDPIG DHPHTSSPPH NSSPNERRPL HELGARIPLR
     NLRVGRLRGN SHMRHNDPDA ESLRGLVDDD DDSTKRHSQQ GSIGTIGDDD APLLPGGSPR
     RREKPQGRMA RLKSHVRLPS FMSSRPLTPP EPPANEVEAD DHDPASNRTV AVGQIQTTKF
     PPNAVSNAKY TPWSFLPRTL YNEFSFFFNM YFLLVALSQV IPALRIGYLS TYIAPLAFVI
     SITLGKEAID DIHRRRRDAE ANSEPYTVLR FDDPSMGSGA SAGAGSKRNK LRRKSKTNRP
     SRMSDAAAEE ERLDGMGRPT ASVSEIVKPS KDLKVGDILK LGKDQRVPAD LVILAAYVSD
     NAIQEPQAPE LPVSAEANLI DTDGDDAGHA QNASEAQKDN AASGNDSTGE AFIRTDQLDG
     ETDWKLRLAS SLTQSLDVSE FTRLRIVAGK PDKKVNDFVG TVELLPKQKG GYDPHDDESV
     AENAKSAPLT IDNTAWANTV LASSSTVLGV VVYTGPETRQ ALSTSPSRSK VGLLELEINS
     LTKILCFLTL ALSFILVALK GFDAETGRPW YVSVMRFLIL FSTIVPISLR VNLDMGKSVY
     ARFIEKDQGI PGTIVRTSTI PEDLGRVEYL LSDKTGTLTQ NGKHSPNYAE IAAMLTSL
//
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