ID F0ZM50_DICPU Unreviewed; 963 AA.
AC F0ZM50;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN ORFNames=DICPUDRAFT_94662 {ECO:0000313|EMBL:EGC34964.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC34964.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000256|ARBA:ARBA00003954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001857};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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DR EMBL; GL871076; EGC34964.1; -; Genomic_DNA.
DR RefSeq; XP_003288489.1; XM_003288441.1.
DR AlphaFoldDB; F0ZM50; -.
DR STRING; 5786.F0ZM50; -.
DR EnsemblProtists; EGC34964; EGC34964; DICPUDRAFT_94662.
DR GeneID; 10501928; -.
DR KEGG; dpp:DICPUDRAFT_94662; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; F0ZM50; -.
DR OMA; WTQEMVI; -.
DR OrthoDB; 1381139at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02077; P-type_ATPase_Mg; 1.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006415; P-type_ATPase_IIIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR01836; MGATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..145
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 107071 MW; CFB3280E04BA2FE8 CRC64;
MGGNSEKKRL LGSDTNITVN DDDGAVSKAQ PYVKPEKDGV FTGILRFLGL REKKKPKKDA
NKEKEFADKF RDLSVLDKQS MLDRIGTPMQ GLSEEEVDRR TKLYGRNVIT QVKASPWYAT
LFFAFTHPFN IVLTAIAVVS ICTDDYATFS VVMFMVIFSA LLCFHEERKS SKAFAHLKSL
VRTTVTVLRT RNGISQEMKI DMDDIVPGDI VPLKAGDVFP GDVRILESNS LFVSQSSLTG
EFLPVEKGPN ASEEPTSIFD TPNICLMSTN IVSGSGIGIV FDTGSRTYIS SISEILTSTQ
TTNAFDIGVR KVAYLLMGFG VVLVPIVIII NGISTRDWKD SALFGLSVAV GLTPEMLPMI
LNTNLAKGAS DMSKKKTIVK QLHSIQNMGA MDVLCSDKTG TLTEDNVKLQ HYIDQDQNES
DNVLSFSFLN SNFQRGLKNV LDVSIISYYG LKRGLITEEE AEKLLLHGHG NGPTDEDNHT
PSGQKKPDPF ADSYSLNDEF PFDFTRRRVS VILNCANEPS TKLLVCKGAV EEVLYCCSYV
ATPNGEAEPL TEQLKKKLLG VMNDLNVDGL RVLSVATKKI ENLPSDYKFD VKVDEFGLTF
HGFLAFIDPP KSDCAGAIRQ LRENNVAVKV LTGDNLAVAR KICRDVGIDV SRVISGPELE
GVDDEDFDQI IEECSLFAKL TPIQKYNVVK ALKRLGHTVG FLGDGINDAL ALREADVGIS
VDTATNIAKD ASDIILLEKS LNVINTAVIT GRITHANTIK YIKMAASSNF GNVFSMLIAS
AWLPFIPLQP IQMLTQNLLY DFSQVAIPWD NVDEEYLKVP HPWSVKSLFK FMVFLGPLSS
IFDVVIFSYM WWKLGWDSET TAQLFQTGWY VEGLITQVFI VHMIRTTKIP FIQRWGSLQL
ILNTLWVAGV CVAIPYIPYV NTFLKMKTLP AMYYPGLAAC FFGYFFLTQI VKKLYMKFFG
EWL
//
