ID A0A2A2JBM2_9BILA Unreviewed; 1058 AA.
AC A0A2A2JBM2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=WR25_10818 {ECO:0000313|EMBL:PAV59146.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV59146.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV59146.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV59146.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV59146.1}.
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DR EMBL; LIAE01010543; PAV59146.1; -; Genomic_DNA.
DR EMBL; LIAE01010543; PAV59147.1; -; Genomic_DNA.
DR EMBL; LIAE01010543; PAV59148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JBM2; -.
DR STRING; 2018661.A0A2A2JBM2; -.
DR Proteomes; UP000218231; 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; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000218231};
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 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 625..643
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 698..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 732..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 762..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 797..824
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 585..830
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 932..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 119627 MW; 7EC982693FB1E59E CRC64;
MSKYRGAFIL IVCEFEFPGI DQLLLRGARL KNTPWIFASV IYTGHDAKLL MNSNKAPLKS
GTIDIQTNYR IIFLFFVLVA LAIISAAGTV VWTKNNIPDA WYLEFLQHGS RTGFFWGCLT
FFILYNNLIP ISLQVTLEVV RFFQAFYINN DIEMYDVNSD SCAVARTSNL NEELGLVKYV
MSDKTGTLTR NVMKFKRVSV GGENYGDNEN DEFCDPDLIK DLNENKNSPK GRAIREVLTM
MAVCHTVVPE HKDDQILYQS SSPDEGALVR GAASQGFVFH TRQPQKVIVK MMDEDETMEV
LDVIDFTSDR KRMSVIVKNH SGVIKLYCKG ADSIIFDRLG KGMDAEMETA KQHLEEYATL
GYRTLCFAAR EIKPEEYADW APKYREASLK IDGRTQAMGE LAEHIEKDLE LVGATAIEDK
LQEYVPETIQ ALIAADMRVW MLTGDKRETA INIAHSCALI SSQTELMIVD KHTYEDTYVK
LDQFAKLSED FEAQQKEFAM IIDGKSLVHA LVGEARTHFA ELCLRCRAVV CCRMSPMQKA
EVVDVVRKIG KHVVLAVGDG ANDVAMIQAA NVGIGISGEE GLQAASASDY AIPRFHFLRR
LLLVHGAWNH DRSVKVILYS FYKNICLYII ELWFAIFSAW SGQTIFDRWT IGMFNVIFTA
WPPLILGLFD RPVPAHQMLR YPALYHSFQK RAFSIWNFSL WIGMALVHSL SLFFLSYFFL
ESQVVWANGR VGGWLMLGNC CYSFVVTTVC LKALLECDSW TWPLFASCFG SIALWIIVLW
IYAAVFPDVF TFVGSDVAGM AFIMMSSPTF WLAFLFIPVA TLLWDLVIKS TLMLHPRLSV
AYRPFLRPLL AIRLPISKSL INVNIWHVQP AQSQSLENER RSRHLFTITY PTPREQAVMH
IKQAQSGGFE RAWLPSSIGP RRVSISWRRS LRTVGDSSHR TAQTTTTTPA SPSGSNGSAA
RRRKRQQEAE EERARLRGYD NQAMEYGSTE LFPIQSSPND RDRSFSQGPP PPYINSASSN
STSNVTYFRP SPASAKPTHV TRIAVPPLDE TQQQLQHL
//
