Q9Y088 (Q9Y088_ENTHI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Cation transporting ATPase EMBL CAB45102.1

Submitted name:
Phospholipid-transporting P-type ATPase, putative EMBL EAL45549.1

Gene names

Name:	atpase EMBL CAB45102.1
ORF Names:	EHI_168260 EMBL EAL45549.1

Organism

Entamoeba histolytica EMBL CAB45102.1

Taxonomic identifier

5759 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length	1057 AA.
Sequence status	Complete.
Protein existence	Predicted

General annotation (Comments)

Catalytic activity

ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out). SAAS SAAS023299

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix SAAS SAAS023306
Ligand	ATP-binding SAAS SAAS023306 Magnesium SAAS SAAS023299 Nucleotide-binding
Molecular function	Hydrolase SAAS SAAS023299
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9Y088 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 722E5EF24310A2D9	FASTA	1,057	120,962
	10 20 30 40 50 60 MNKAWDFLQK KIPFLRKKPE QPRTIIIPIT KQNKKFCSNK VENNRYTYLN YIPKCLFNQF 70 80 90 100 110 120 KYFYNLYFLI TALSQFVPIL QVGYRFTYTM PLAFVVILAM AKDAYDDIRI RIRDKQTNSQ 130 140 150 160 170 180 PFTQLIGGEP KEIQSKDIVV GNILKLKKDE RVPADCLILR STEESGSIFI RTDQLDGETD 190 200 210 220 230 240 WKLRRAIGET QKMDIQTICN SQFELNVEAP HADVYSFQGT IRINEDPKIY SLNVENTAWA 250 260 270 280 290 300 NTIVASDEMC ALVIYTGNDT RLARNRKQSG NVKRGKTEDE VNFLSKILFC SLMGLSILMI 310 320 330 340 350 360 MPDLIQHPNW FILVSLTRFM ILFSSIIPIS MRVNLDIAKM VYAFFINRDK DIAGAEVRNS 370 380 390 400 410 420 TLPEELGRVD FVLSDKTGTL TKNEMTFQVL CMQSETIRST NFDDIKDDIR ECLQSNEEKV 430 440 450 460 470 480 LFKKKKNPKF IMRCVQAMAL CHNVTPSFNE NGEKYYQASS PDEVALVKFA ESVGVVLEER 490 500 510 520 530 540 TFKKIVLNMP MIGNVEYEIL NVFPFSSSTK RMGIIVRNNK DNEIYLLMKG ADNVMSKIIK 550 560 570 580 590 600 DNEWLSEECN NLAREGLRTL VFGSRKMSQE EYQAFNERYD HANTLMTGRE EEVLKVQESI 610 620 630 640 650 660 EHGLNAMCIT GVEDELQEDV QKTLEMLKQA NVRVWMLTGD KVETATCIAK STKLVDIDQE 670 680 690 700 710 720 IIQFFANSID EATSLIFNNE GSIGTKALIV DGNTLSLMLK EMSKEFIQFA LKAQAVVCCR 730 740 750 760 770 780 CLPSQKADIV RLVKSSGLTT CAIGDGGNDV SMIQEADVGL GIEGKEGKQA SMAADFSIKQ 790 800 810 820 830 840 FSHMLKLLLW HGRNSYIRTS DLALFIMHRG MIISIMQAVF SMVFYFTPIT LFTGILLVGY 850 860 870 880 890 900 STFYTMAPVF SLVLDERISL KDIMQFPVLY AEMQKGQNLS FKTFSAWMFI SILQGSVIMM 910 920 930 940 950 960 LAMILFDSSF VHIVSISFTV LILIELLNIG FTIRRWNWII FASEASSVLM YLISIIVLRP 970 980 990 1000 1010 1020 TFEPSFVFSL GFWWRVAVIT LINSFPFILK FIYELLNPPK HMTVGHKKFP ISFDLTCCCN 1030 1040 1050 CHNIRKKNDY QDINFSEIYD KTETNDDSTK ALIDHLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the protist parasite Entamoeba histolytica." Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P., Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M., Duchene M., Ackers J., Tannich E., Leippe M., Hofer M. , Bruchhaus I., Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z., Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D., Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H., Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S., Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U., Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M., Barrell B.G., Fraser C.M., Hall N. Nature 433:865-868(2005) [PubMed: 15729342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HM-1:IMSS.
[2]	Bruchhaus I. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91644 Genomic DNA. Translation: CAB45102.1. DS571263 Genomic DNA. Translation: EAL45549.1.
RefSeq	XP_650935.1. XM_645843.1.
3D structure databases
ProteinModelPortal	Q9Y088.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3405233.
KEGG	ehi:EHI_168260.
Organism-specific databases
EuPathDB	EupathDB:EHI_168260.
Phylogenomic databases
ProtClustDB	CLSZ2730508.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01530.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9Y088_ENTHI

Accession

Primary (citable) accession number: Q9Y088
Secondary accession number(s): C4M4R2

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)