ID A0A329RR23_9STRA Unreviewed; 1484 AA.
AC A0A329RR23;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PC110_g16413 {ECO:0000313|EMBL:RAW27187.1}, PC113_g6491
GN {ECO:0000313|EMBL:KAG2862239.1}, PC115_g7755
GN {ECO:0000313|EMBL:KAG2926869.1}, PC117_g8805
GN {ECO:0000313|EMBL:KAG2945022.1}, PC118_g369
GN {ECO:0000313|EMBL:KAG3000120.1}, PC129_g4418
GN {ECO:0000313|EMBL:KAG3224953.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW27187.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW27187.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW27187.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG2862239.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15-7 {ECO:0000313|EMBL:KAG2862239.1}, 4032
RC {ECO:0000313|EMBL:KAG2926869.1}, 4040 {ECO:0000313|EMBL:KAG2945022.1},
RC P415 {ECO:0000313|EMBL:KAG3000120.1}, and P421
RC {ECO:0000313|EMBL:KAG3224953.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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:RAW27187.1}.
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DR EMBL; RCMG01000134; KAG2862239.1; -; Genomic_DNA.
DR EMBL; RCMI01000191; KAG2926869.1; -; Genomic_DNA.
DR EMBL; RCMK01000195; KAG2945022.1; -; Genomic_DNA.
DR EMBL; RCML01000004; KAG3000120.1; -; Genomic_DNA.
DR EMBL; RCMV01000097; KAG3224953.1; -; Genomic_DNA.
DR EMBL; MJFZ01000583; RAW27187.1; -; Genomic_DNA.
DR STRING; 29920.A0A329RR23; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000697107; Unassembled WGS sequence.
DR Proteomes; UP000735874; Unassembled WGS sequence.
DR Proteomes; UP000736787; Unassembled WGS sequence.
DR Proteomes; UP000760860; Unassembled WGS sequence.
DR Proteomes; UP000774804; Unassembled WGS sequence.
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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000251314};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 410..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1064..1083
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1116..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1155..1175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 87..150
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 941..1189
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1289..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1484 AA; 163698 MW; FA684977F49ACB23 CRC64;
MTVLESVIGS GAARVTDVTV DAESTYRTVQ VGGSPVAAST GWAPKMLAEA AAGLGSSTMS
ILSAVSDGAA GDNGIALGIS DTSARCIYVN SAADNAAQKF CNNKVVTAKY TKLNFIPRFF
YGRLSQVANF YFLLVGAGQI IPEISSTQTI PYQWIVLALV LSIDAVFAAI EDRGRHIADA
KMNARVSHIF DLDEPDCFCN DTWRAVAVGD IIKVENYEAI PADVLLLAVS EPDPNAPTGI
CFVETKSLDG ETNLKVRQAL SCTFSQLSDP RALAQLPGRV ICEKPNHDVN TFSGRFEPQS
GHAIPIDLKN VALRGCVIRN TPFIYGLVLN TGADTKIMQA GSHTPPTKIS KILAIVNRGN
ALLMAILASL CVLGAVLCAF WVAQNREGAT YLHLENLSGV APFRNDVVGI LIYLGYFWIL
IASFVPITLY VTIAIVKTYQ TFFLNRDLGM YDEVTDTPAL VRNSDLNDEL GQVTHIFSDK
TGTLTANEMD FRKMSIHGVS YGRGTTEIGR EATRRLGKDL SASDVLADNT PILVKTDNVN
FLDPAGDLER DNDARLHPEQ AARIHDFFVH LAVCHSVVRE TLSENDAGTG FSASSPDELA
LVSGANYFGY SFLARRNGEV AISVPGKREE VVYELLEMVD FTSTRKRMSV VVRTPDKRVM
LLTKGADSVI FPRLAPSADP AIVDTTLAHL ERYATEGLRT LVIAQKELSS DAYAEWSCEY
DAALGDLEQM AMQKRGEPNR IEELEEQLEQ GLELMGATAI EDRLQDQVTL TLGDLSRAGI
KIWVLTGDKE ETAVNIGFAC QLLNNDMERI MINAETTPSA SDLYDMLLAR CVEARKRAEL
QASGAKGETQ QQAIVIDGRC LTMVFSNNVL SELFLEVSQQ CVSVICCRVS PKQKAQVVRL
FKTSLHGCRS LAIGDGANDV AMIQEAHIGV GISGHEGMQA VNASDFAIAQ FRFLKRLLLV
HGHWNYRRMA KLALYVVYKN ILLFGTEFVL AALPQCGSSG TLFFNNMWIN GYNVFWSSMP
IGIVAITEQE VPARIAEQFP GLYHVGAQGE LFSLRIFAQW VAEALYECVV CGLVPALIIG
GPVDSTGNGF SRDLCGAISY CCLISVGWVK LALNMVTWNA ITAFAFIASI IFWYISGYVI
AASFPTSVAD TAFPHIFVLP EFYLAIFLSL LLCLGRDFLW KAYKREMNPE YYHILQEFHR
RGSQNPEKAR WTPPELRYER FQADLTEEKP RFDLPEQQAL PNQRPSQADQ KVYTGFAFST
QVLEDRFLNP LREMVLPVSQ VANAIGRVLS PSGSPITRHN PDSPTRREAS DEPKSFEEKI
LALPIEEQAV YEIQRYQVFT GWGSLRPGHL LINDPPKFTN ALMTDGAGTF DLDHWVVDPG
FGGSDQWQYA TRFKDFLRAQ EKLQQEAVEG VPPELQAHAS GLEPDLQERR RIKKKLNRLV
GRSVRRRRWV RKEKLLAEAI ERANIALAAP DPESSLPRTP TNSP
//
