UniProt: A0A0A1UED5

Database: UniProt
Entry: A0A0A1UED5_ENTIV

LinkDB:  A0A0A1UED5_ENTIV 
Original site:  A0A0A1UED5_ENTIV

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (27)   

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ID   A0A0A1UED5_ENTIV        Unreviewed;      1227 AA.
AC   A0A0A1UED5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=EIN_248120 {ECO:0000313|EMBL:ELP94848.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP94848.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP94848.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP94848.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) 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}.
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DR   EMBL; KB206169; ELP94848.1; -; Genomic_DNA.
DR   RefSeq; XP_004261619.1; XM_004261571.1.
DR   AlphaFoldDB; A0A0A1UED5; -.
DR   EnsemblProtists; ELP94848; ELP94848; EIN_248120.
DR   GeneID; 14894099; -.
DR   KEGG; eiv:EIN_248120; -.
DR   VEuPathDB; AmoebaDB:EIN_248120; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000014680; 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:SF91; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   Hydrolase {ECO:0000313|EMBL:ELP94848.1};
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:UP000014680};
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..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        95..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        291..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        335..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        972..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1005..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1035..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1078..1098
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          40..98
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          857..1106
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1155..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  139115 MW;  A558102ECBA478A6 CRC64;
     MAPFGCCCST RESLYFLFFN SNVLNNTLEK YPIVKVQSTT PSHKFPKNTV KTTKYNVFTF
     PFKFLYYQYK LLTNVYFLIN MIISCIPYIS TVTPITAIIP IVVVLAVSAV REIVEDLKRY
     SADNKANGKK YTVLKNGEES VVCSKNISVG SVLKLHKDQV VPADVVPIFS SLPDGVCKLD
     TAALDGETSL KTIFVPKMLL DMTEKDVTDF SMDLECEWPR AKFNDFKGLF SSETVKIALD
     EKNLLLRGSV LRKTEYVYCV VCYTGKYTKQ ALNSTKPVNK SSILNTRLNQ FVLSTVFFQL
     LICSILAALS TWRYTVVNPD TGFWYLDSYL PELGYAAYAV KKFFGFFNLI SYTIPISVGV
     TMEICRYVQG FVMEMDADFK IKKVDSEGVE KDEGMRTNSC ALIEEMGEVQ YILSDKTGTL
     TENKMSFSKC SIGGEVISDV MNGTLGQLSE TNKMVSDFLM CLVLCNTCSK EKDQVDGMKY
     SSLSPDEEAL CEAAYVNGVI LEERTQKTVK IQNKGENEEY TIVIQIEFTS ARKMMSVLVE
     KDGEYVLYSK GADSAISTLL HHNTKGTQKE INIGRLDTVE LSEEEEMIKK TQQQVDAFGN
     EGLRTLFIAR RKLSKEYVDD WKRRLDAIDP LAENVKELRY HMYKELECDL ELIGATAIED
     QLQEGVPETI DILRRAGLKI WVLTGDKKET ATSVAKSCKL FDLHQNLLSF NFESEEAFLE
     CANAAMAKIN ELKDTKEIAK EKHKGKPSPT TRVLEKEMQE DVKYAKSNKL GIVISDTNIE
     YLIRNYKVVK PLFIQAESVV CCRVSPRQKA DIALLVKRIT NKSILTIGDG MNDVPMITKG
     DVGVGIFGKE GNQAAVTADF AIQKFRHLTK LVLFYGRNAR YQVSSLIKFC FYKNAAFFLL
     DVSYAFMSNF TCQILFDDWI MTCFNILFTS LPPGAIALFD YELSWNEVKQ FPESHKETFN
     DPNYKIKSYV EWYLYGVLQS ILFFVLFYFL IAGSDVTNFD GKVNGFPFSV VTVTTYSLTS
     IWVTMLIYTK RFSILVVLSF VASIILYIII YTLVMFISGL SVRGISAYGW YIVLQQPSFY
     LICIIAVSVT TLPQIGALQL HRRVVPTNSQ LIQEYTKWKL VEHKELPEIE MKFSQARPIS
     VILTKSKLDE EERKIQEQME AENKRRKKKE HHKWSKKSRN IKIDKTSKNS TNTTDATTSN
     SLNAFVHSVG ENTTTTVSAE TTSTDAK
//

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