ID D2VEQ9_NAEGR Unreviewed; 907 AA.
AC D2VEQ9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC44644.1};
DE Flags: Fragment;
GN ORFNames=NAEGRDRAFT_33544 {ECO:0000313|EMBL:EFC44644.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC44644.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC44644.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG738867; EFC44644.1; -; Genomic_DNA.
DR RefSeq; XP_002677388.1; XM_002677342.1.
DR AlphaFoldDB; D2VEQ9; -.
DR STRING; 5762.D2VEQ9; -.
DR EnsemblProtists; EFC44644; EFC44644; NAEGRDRAFT_33544.
DR GeneID; 8848574; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_33544; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; D2VEQ9; -.
DR OMA; KMHACET; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 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; 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:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
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 44..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 699..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..61
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFC44644.1"
SQ SEQUENCE 907 AA; 99213 MW; A5972543BDB739E1 CRC64;
ETDINIGLTE KEARRRLDIL GPNELKEEEE ESLFSKFIEK FKEPMILLLL GSAAISLLLG
QYDDAISISL AVFIVCTVAF IQEWRSDKAL DSLKELTTHK ATVIRDGNPQ VISASDIVPG
DVVVFSSGDR IPADVRLVEI SRLGVDESVF TGEVNPASKT IERADLPFHQ SEESSSNPFP
KSTHVSDCKN IAFMGTLVSV GNGKGVVVST GQKTEIGKIS DLLKSIEEKN TPLQDAMDDL
SQKISYLSFG VIGVIFLIGG LTGKPWLEMF QMGISLAVAA IPEGLPIVVT VTLAMGVIRM
SKKKAIVRKL PSVESLGACN VVCVDKTGTL TKNEMTLVKA FTLAEQDAVI NVTGLGYQAY
EGSFHKASIS SLKNRYDHNL GEAIKPTEVS HLHTLLKVGV VCNNASVDFA TSKIVGQPTE
AALITAAQKG GLDVADIRSK HKRVEEIPFS SEHKWMAVKS KNIETGKEMY YVKGAIENIL
GNCTHYCIGT ENQKKPLNDQ LRREIENTSS LFAESALRVM ALCVGDKPSS ELTFVGVVGI
YDPPRPGVKE AVSALYKGGV KVVMITGDSM KTAVAIAKEL NIVPEDGDEK EYALSVEDLS
TSDFEDKIYK ARVFYRMAPV HKMKIVSAYQ KAEYVVAMTG DGINDAPALK MANIGIAMGK
SGTDVSKEAS EMILADDNFP TILSAIEEGK GIFRNIKSFL RYQLTTSVSC MFIIIFCTFM
GYPLPLNPMQ ILFINIIMDG PPAQSLGVEP VDEDVMNQPP RDTKKPITSG KIVMSVALSA
LIMVIGTLYV FIREMAHDGV VTAHTTSITF TTFVFFQIFN AFNCRSEKKS VFQVGWLTNI
PLALSVGGCL LGQLSMLYVP VMRGIFETEP LSLSELLYVT LVSSSVWLIE EVIKFFERRV
ESKYQYN
//
