Q95022 (Q95022_CRYPV) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
P-ATPase EMBL AAC47833.1

Gene names

Name:

CppA-E1 EMBL AAC47833.1

Organism

Cryptosporidium parvum EMBL AAC47833.1

Taxonomic identifier

5807 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Coccidia › Eucoccidiorida › Eimeriorina › Cryptosporidiidae › Cryptosporidium

Protein attributes

Sequence length	1528 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. RuleBase RU000653

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix SAAS SAAS004014
Ligand	ATP-binding SAAS SAAS004014 RuleBase RU000653 Nucleotide-binding
Molecular function	Hydrolase SAAS SAAS004014 RuleBase RU000653
PTM	Phosphoprotein SAAS SAAS004014 RuleBase RU000653
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 metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q95022 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 82AECB973C207D8B	FASTA	1,528	168,875
	10 20 30 40 50 60 MIGSDDSFEP NIQNQTVQSS MATKSSNTFH SIFNKDEKLL EMSSQSSLKD VNSYSPNIAT 70 80 90 100 110 120 YNCIGNNSSP SSRIVSPISS ASFFVDMTPN GRHLLHAEVA DEEPNPETCS PNPQKFLQNR 130 140 150 160 170 180 LNLLASRNLL NHYVNSNENN YFGKQLSSDV ISSIPDLQYN ETAVQDMVIN KLSMSTQMLP 190 200 210 220 230 240 DTIEEARKRD PEFVSKALEQ TLEYSEAQKP IHYWSQIELD MLINELSANI IDGIDEGKAI 250 260 270 280 290 300 ELMEKKYGPN KLQKEKHEPI WRIFLSQFTS LVVSLLLVAG IVSLAFQEWV EGIGILFIVL 310 320 330 340 350 360 INASLATYME NNASNALAKL ADLSSPKCTV IRSGIINIIP AYNLIPGDIV LLRTGDSVPA 370 380 390 400 410 420 DVRLIEATEI KCNEALLTGE SEDVSKHLVS PDPNNPFPTN ICFASTAITN GTGKAIVVLT 430 440 450 460 470 480 GMNTQIGRIA QQLKLASGGS NSGTPLQIGL NRLGGFIGFM SLIVLVIIVI VALLTNYKDP 490 500 510 520 530 540 SHPNSNPVFG IILVAVGFAV SSIPEGLPMV VTICLSIGCS EMCRRKANIR KLPAVETLGC 550 560 570 580 590 600 CSVICSDKTG TLTEGKMTAV KLATFSRNNT KTLNISPTGN EQSPSFVEYQ ESNSCVFSFY 610 620 630 640 650 660 PTRGSDPNGG IFLSSSLTQN IKEEIMNLIH FNKNKTIEMT ENHFLESNFE MPPDDKIPYK 670 680 690 700 710 720 FINYNSICKD FGDPLNSHLP QTKYVRSALL AGYLNSYGTA LVYDNESNSW KTRGNMSEGA 730 740 750 760 770 780 IVVAAAKASY GIKNKIFDSR KQDIESKQSS TKKSGHLIRS KLNDQNFKTI NNGNNPATEV 790 800 810 820 830 840 ATSGSSPTQC ALDSNSTDSN KLKNYIIDGV NTENKTNLVI EDEIEYLRVP SVEVPFTSSR 850 860 870 880 890 900 KMMMTVHSLS TPNKFGDIFF SNTDSKSNKQ TNLQNKVSNS NSQRYSKTVD NLDSGVYTHV 910 920 930 940 950 960 AILKGAPDRI VKHIGFMLNT DWKNEEPMVH IDYSEKINPQ EIFEIENTNK VLSGEALRVL 970 980 990 1000 1010 1020 GIAILPLTSE DFFDLVTEEC SDKRLQYVLD KNELTLLGLI GFLDPPRPGV EKAITKCCEA 1030 1040 1050 1060 1070 1080 GVRVIMITGD QQPTACAIAR SIGLLADEYE YKNSYEGSAD LHNATSGSII CNQLHENGDA 1090 1100 1110 1120 1130 1140 SRPHLSNELF DKIVSSVSVF CRAQPEDKIA IVRSLQRQGE VVAMTGDGVN DAPALKAADI 1150 1160 1170 1180 1190 1200 GVAMGISGTE VAKGASEMVL LDDNFVTIVN AIEEGRKIYS NVQKFVAFLL GTNIGEIIYL 1210 1220 1230 1240 1250 1260 SIAIAAQLPI PIAALQILFL NLMSDGGPAV ALSVDPPDPN MMKVPPRPKK SPIMTRDWWI 1270 1280 1290 1300 1310 1320 FGNIPHAIFE AICVLSVLII SMYTSLGVFQ RNAIESLCLH DSNNRYFCQT NEWRLNLIDL 1330 1340 1350 1360 1370 1380 EKTGWVTNID FYNPLTNSME QILGVTKGKL NSTLPPSEIP YVKGLYEKAE RLGISCVAGK 1390 1400 1410 1420 1430 1440 HGWCIPQQKI TNDEYIDLVA FGTIRGRTAS FIAAVFCEML RAYTVRTWDW FTKPLFNNPW 1450 1460 1470 1480 1490 1500 LHFACSLSAS STLIVTFTPG LQQIFGTHTI YWWLYILAIG AGFLNMAFDE LVPKPLYRRI 1510 1520 VERRRIRAKL LAERDVNWIT RSEQFENT

References

[1]	"Molecular analysis of a P-type ATPase from Cryptosporidium parvum." Zhu G., Keithly J.S. Mol. Biochem. Parasitol. 90:307-316(1997) [PubMed: 9497052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: KSU-1 EMBL AAC47833.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U65981 Genomic DNA. Translation: AAC47833.1.
PIR	T37308.
3D structure databases
HSSP	HSSP built from PDB template 1SU4 based on UniProtKB P04191.
ProteinModelPortal	Q95022.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	KOG0202.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 3 hits. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 4 hits.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q95022_CRYPV

Accession

Primary (citable) accession number: Q95022

Entry history

Integrated into UniProtKB/TrEMBL:	February 1, 1997
Last sequence update:	February 1, 1997
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)