ID Q5CYM7_CRYPI Unreviewed; 1278 AA.
AC Q5CYM7;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=cgd7_1760 {ECO:0000313|EMBL:EAK90606.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90606.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK90606.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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:EAK90606.1}.
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DR EMBL; AAEE01000001; EAK90606.1; -; Genomic_DNA.
DR RefSeq; XP_628353.1; XM_628351.1.
DR AlphaFoldDB; Q5CYM7; -.
DR STRING; 353152.Q5CYM7; -.
DR EnsemblProtists; EAK90606; EAK90606; cgd7_1760.
DR GeneID; 3371791; -.
DR KEGG; cpv:cgd7_1760; -.
DR InParanoid; Q5CYM7; -.
DR OMA; DMMIYQR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000006726; Chromosome 7.
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; PF00122; E1-E2_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 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:UP000006726};
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 50..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 343..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 407..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1059..1080
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1092..1114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1143..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1176..1197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1204..1230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1245..1265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 15..74
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1030..1270
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 611..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAK90606.1"
SQ SEQUENCE 1278 AA; 143925 MW; 002FF7AFA3BE7507 CRC64;
LYDITSSRPR LVVINNRQVR NFSGNFIRTS RYTVLNFIPK YLFEQFCRPV NFYFLVISLL
QIFPSISSTN GIPTLALPLV FVLFVGAVKD GWEDLNRHQN DRIENEREVI VIKRFPFINY
IHGRTLACDL EEAEKPKNKN PSLKHVISFK SENDKQSNTS HSWFLGIEGS ERSSSSELKV
GDIVLLRNHE TIPADIVLLS TSSENGDVFI DTSSLDGESN LKRRFSHKES TKMLGNNIHD
VIKRARYLEG LIECSPPGKD LHNFDGTAII RLPPISEGLV TQGNTITQFP INLDNIVLRG
CILRSTEWAI GCIVYAGHES KIQMNSLKPT KKMSNVDKFT NKMVLVVLVI LFCLCMTGSL
LTYKYIFDGV FDHLDYLGVS DVNEISYRAT GQAIPISFVP VVRFCTWIVL LANIIPIALV
VSMKIVKAIQ GQFISRDRAM YDAVNNTYAV ARNSDLNEDL GQVRYIFSDK TGTLTRNIME
FKSLSVGGVH YGSTETSSSK EDNLIREIEI PQVNIKDENI LLDIKSRNSQ SIKIGNLLIG
IAVNNSIVIE NQSEMFSMLY NSGRIEPDIL PETFSPSTYL TGLNSDITLN PDNKPKSRLG
SNFMTSIKSI SSQSSKSASN NSSNTKQKPK SNFPLYSAQF PDEAALCYGA QYLGVSLICL
NPKTKHLILD VFGELLDVEI LAKIPFTSDR KRSSTVVRIK RLNSEHNMKD LRIMSELYRE
RIMVFSKGAD SAMIPLLRQS NMEKFQKDLE IGNKMANQAL RVLCITEKEI SEDEFADWNQ
KYQLAVNNVE NRESSLQEAA SMIEKDLLLQ GVTGVEDRLQ DEVPETIKCL RDAGIKIWML
TGDKVETARE IAASAGLLSP GHEILELTES TCSNKSEIKK RVLSICKSLG IDLESDKSER
FLRKVKASGS KSEKKETNFS ILIDGAVLGE IFSGSLANND FVSECKRFED ITSSISSIEK
LFVQMCCKCR TVVFARFAPS QKGNIVRIVR KHMDEITLAV GDGANDCNMI QTANVGVGIR
GLEGNQAFLT ADYGITSFKD LKVLLLVHGR LAYRRICKLA LYMFYKNLTV GIPVFIYGFF
TLWSGTRLYF DYWYQVYNVI LSSVPIVVVS VFDFDVTKSE SLSKPHLYSF GPENKFLNTK
ICLIYLLNSA WHIFVVFTIP YILFRVNSTN LFGSNQSIVG AAIYYLVILV VNIKVLLMAD
HIHYLLGFAV AFSLFSWICT LFVCAASFSI GSDVYTIWIP LYNNVLLWIT LISGLSISLW
PDYFFKVLFS EWLKVDDK
//
