ATX1_PLAFA
ID ATX1_PLAFA Reviewed; 1956 AA.
AC Q04956;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable cation-transporting ATPase 1;
DE EC=7.2.2.-;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T9/96;
RX PubMed=8421054; DOI=10.1083/jcb.120.2.385;
RA Krishna S., Cowan G., Meade J.C., Wells R.A., Stringer J.R., Robson K.J.;
RT "A family of cation ATPase-like molecules from Plasmodium falciparum.";
RL J. Cell Biol. 120:385-398(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; X65738; CAA46646.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04956; -.
DR VEuPathDB; PlasmoDB:PF3D7_0516100; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000135300; -.
DR VEuPathDB; PlasmoDB:Pf7G8_050021300; -.
DR VEuPathDB; PlasmoDB:PfCD01_050022400; -.
DR VEuPathDB; PlasmoDB:PfDd2_050021000; -.
DR VEuPathDB; PlasmoDB:PfGA01_050020500; -.
DR VEuPathDB; PlasmoDB:PfGB4_050022000; -.
DR VEuPathDB; PlasmoDB:PfGN01_050021000; -.
DR VEuPathDB; PlasmoDB:PfHB3_050021100; -.
DR VEuPathDB; PlasmoDB:PfIT_050021300; -.
DR VEuPathDB; PlasmoDB:PfKE01_050020500; -.
DR VEuPathDB; PlasmoDB:PfKH01_050021400; -.
DR VEuPathDB; PlasmoDB:PfKH02_050021600; -.
DR VEuPathDB; PlasmoDB:PfML01_050021000; -.
DR VEuPathDB; PlasmoDB:PfNF135_050021600; -.
DR VEuPathDB; PlasmoDB:PfNF166_050021200; -.
DR VEuPathDB; PlasmoDB:PfNF54_050020300; -.
DR VEuPathDB; PlasmoDB:PfSD01_050021000; -.
DR VEuPathDB; PlasmoDB:PfSN01_050021200; -.
DR VEuPathDB; PlasmoDB:PfTG01_050021200; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 3.
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; IPR001757; P_typ_ATPase.
DR SUPFAM; SSF56784; SSF56784; 2.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1956
FT /note="Probable cation-transporting ATPase 1"
FT /id="PRO_0000046354"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..1818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1819..1837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1838..1845
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1846..1863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1864..1881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1882..1905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1906..1928
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1929..1952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1953..1956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 901..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..933
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1760
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1764
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1956 AA; 230286 MW; AE708AAE99009335 CRC64;
MHLMCTGLRN EKLINDRKIL YGECNLNIKS DSFIILLFKE IMNPFFIFQI FAMIVWSLDN
YIEYTISILF ITSISIILEL KNTIKNQKKI KNMLNYTCPI NVYRYNTSYI ISSSELVPGD
IYEIKNNMTI PCDTIILSGS VTMSEHMLTG ESVPIHKERL PFEGNAIINK NNKYDSNDEK
DDYLRIYNNH ASINMIKRNH LIEETLGKKD REYKSNTHDL CSMNKLCYIN NTYDDVHMKN
NKMDYNNNNN NKKKKKINNL NFVKGTYINS NDLLYDDKIG VNIFEDDVNN MKHKFNQRNI
NYYNKDTNNL EYNNKHRYIY DCLLKKVEAI SQKNKIIYSN EDINKYMLYG GTYVLSLYNI
NKIKYNNKEE NRILGLVIKT GFITTKGKIV NNILYHKKKE LNLINDSYKF LIILIIYALF
SVFILLYITL SNNEYTNHII IKCLDIITDA IPPALPTTLT VGISIAISRL KKKFSISCLC
PHKINIAGQI NTMVFDKTGT LTENNLQFIG IITQNKKNKN MLSDFIHIKE MNTESYIHSK
DDNMIHNKNS IISEYYIKDN MKNLHTSSKK KSITKERSNF LVQTIKSCLL KDHYIKEKKK
EYYTNNTYCN DLHINDSTCS SYLLNSETKD AYCEYYNIDH LCDINKKNMD INSKNELMGK
YSKNELMGKT IKNELMGKYS KNELMGKYSK NELMGKYSKN ELMGKYSKNE LMGKYSKNEL
MGKTIKNQVG VDTNIYHMNC DNDYNYDYPC DYNCNNCNDT YHRLEYHNIN KDNSFNIPPE
KNKSYNNISE HIKINYPLLF EALACCHTLS KVNNKIMGDV LEILMFNFTN CDMLINNNSF
IIKEKKKNCS YDFQKIDGDK NIGANDERCH LNNNLVSYNI LKRFEFQSRL QRMSVIVKST
YGNNNDDNND DDNNNDDDNN DDNNNDDNNN DDNNDDNNNN NYYYNIFCKG SPEKIKELCL
KSKIPNNYDE ILNKYTKQGM RILSISYKRV KSKNINLLNV KRSFVESNLH FLGFLIFTNN
MKKNAPDIIH NLQTSGCQCI MSTGDNVLTS IHVAKKCGII NSNVESIIIG DVIPVVGKNN
KQKKKLVWYN HKNDTYLKGH DKTCIDNEFT SIQSQMNSDN ICGDNICGDN IYGDNICGDN
IYGDNINGDN INGDNIYGDN INGDNINGDN INTYDNIYGD NYNLDYCPTE YHKCTYNNSI
LYRNNFLYKK ENKKDKNYKN ISTLYEHRTN DIQFDKLCDI LINKDPRNVN IVLTGKAFIF
LKKKFYSFHL PYYEECKNIV HYIMKKKHKK IKNIINNHNS NLYYHYNIID TFVKRMNKEY
MCFNKLLYKI QQKLLYNLIH NLYKKKKYMN NYYDIDEVHL IGNNNNNNNK NNSKEKKLPL
KNKMKHIRKN ESNDNITFNT YTSNNIHLSK YKYVHHKNYY YPDSCTNLRK KKNSLFYNLK
KYIYYEKKKY LQHCLLKHDN YKKVELPRIK DINYSYQMES IKTRNFIHSL SEQFAFSNLI
LSFYIIKNDD NNVYNKNYIY NKNYIYNKNS ICNKNYICNK NYIYNKNNIY NKNNIYNKKN
ILTHAKSVLL SGSSKKFLKF FSNIIRRHKL KEKKNKKNIK RYKMNHVNNT SKGHIILNMC
THGFKKDYSS LKNKYRIVNN KRYMLKNDNV YDRHMYNLTD MYRGTQYGCS KKKNKNIYMN
NNNNILKNKI NRFLEHLLVD KCKRNICHKY TDIKNIKLSI YEYILRTCTV YARMKPKDKS
DLILSLKKLP NNSYVGMCGD GANDCLALSC ADIGISLCNN NESSICSSFT SNKLCLHSIV
HILIEGRASL VNSFQLFKFI SLYSIMQCSQ VLILYSISNK LTDNQYIFID IVTILPLSIF
MCWTSASEKL SKNIPIGKLF SFPILISIYG QIIIQLFFVM ISLVVLMNLS FYKYDKNKVM
KEKSDDTYLY KAQKYTLIYS LLFSKFVYVY IFKYKE
