ID Q4DXI9_TRYCC Unreviewed; 1217 AA.
AC Q4DXI9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Tc00.1047053506941.60 {ECO:0000313|EMBL:EAN97225.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN97225.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN97225.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN97225.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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:EAN97225.1}.
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DR EMBL; AAHK01000108; EAN97225.1; -; Genomic_DNA.
DR RefSeq; XP_819076.1; XM_813983.1.
DR AlphaFoldDB; Q4DXI9; -.
DR SMR; Q4DXI9; -.
DR STRING; 353153.Q4DXI9; -.
DR PaxDb; 353153-Q4DXI9; -.
DR EnsemblProtists; EAN97225; EAN97225; Tc00.1047053506941.60.
DR GeneID; 3551464; -.
DR KEGG; tcr:506941.60; -.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; Q4DXI9; -.
DR OMA; KAPDYCT; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000002296; 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:SF19; 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; 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:EAN97225.1};
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:UP000002296};
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 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 368..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1064..1083
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1090..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1128..1151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..98
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 911..1158
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1217 AA; 135569 MW; CCF4C2CC403AF7A1 CRC64;
MVVASCNRFL SVIGVRGDRA TGEKRTQLAP TMRTVRPLDP AVAAAYPDNT VINSHYTFYN
FLFLSLYEQF RRPLNFYFLL VACLQFISVI APVSPFSTLL PLLFAFTLTS LKEGYDDIKR
HQQDDKYNNK ARTVLDPVSV SWQSRPNYRI RVGDVILLKG DEEIPCDVVV VAATASTVYI
RTDNLDGELD LKPREIVFPH SVSSNNATKD DTTTSSDLNL ICVDDTCETI INKVGNIKLV
IPPPSAIIES FDGVAEFTCA SGSSEDATTI SVSMSHHHLL PQSCLLKKTK AALCVAVYTG
EETKCGMNKS PPPVKWAKID QDVSRYSIFV FFCQLASALT FGLLGYFLNS RVEEDYWYLK
LPSNELDASL IIYPLRFFLL TAVMIPVSFK FVVDMSKYYM ALAVEWDETM KPDGPNSEGC
RVKNSDILED LGQLDYVLSD KTGTMTQNVM ELLYVTIGDE RLCLHQEIKE LVNKSGLGIP
NNERVLHFGR ILSLCNTVET LGKSGSSSPE GAFVLPQYQA SSPDEEAICR GCVSLHVQLL
YRDANKAVLE VNGVKETWII HHVFPFLSEL KSMGVIVEEK STGTLYFFVK GADDRIMEMA
APTSTPLFST LRSRESQVDL LTSHLNSYAR KGLRTLLVAE KKLSESDLNT FMEEMRVAEL
SLQNRREQVQ KVRLKMENGV TIAGITAIED KLQEGVQDTV RDFIRAGIKV WMLTGDKVQT
AVQIGLSCSL YAPGNRLIYI VSGNSTDGVG WEEHMMSIPL PDPPKTTDGG LGIFLTGAEI
LDEENIRGFE NLEDGDSLKN EVKNENGQCD TTPPANFQKD NSVLVVEGGR VLERILSTSE
LRARFAALSD NCVCVICARV TPNQKAALTG FVRSRGFMTL AIGDGGNDVA MLQEAHVGVG
IVGKEGQQAS RAADFSINRF SDLRALVFVH GQQAYIRTAF VIKYSFYKSM LISFIQVAYN
VVGTYFSGGT FWNSFGLTVW NGVYTLPQTM FYCLDRIAPR VVLERHTFLY KRTRRASDMN
IKEFFIVFIA RGIVQSVLTL FLVTGVFNLS FAFSETGWAA THDVTFSVAY SALIISQMLT
MLLESHSITF LNAIGIFGMP AFYVVMTAIY SSFQRFQYFG VWNNTMNVIS FLTAFAVAFV
LVLPVLGMLS LRRALTPNAR DVLRTAAVQN QMRRQMRWGR GGCCSRFFRW ISCVSEEASC
LLRHPSPVGP LDDIVQV
//
