ID F0VFP2_NEOCL Unreviewed; 1886 AA.
AC F0VFP2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Heavy metal translocating P-type ATPase, related {ECO:0000313|EMBL:CBZ52536.1};
GN ORFNames=NCLIV_023240 {ECO:0000313|EMBL:CBZ52536.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ52536.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
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DR EMBL; FR823388; CBZ52536.1; -; Genomic_DNA.
DR RefSeq; XP_003882568.1; XM_003882519.1.
DR GeneID; 13444695; -.
DR VEuPathDB; ToxoDB:NCLIV_023240; -.
DR eggNOG; KOG0207; Eukaryota.
DR InParanoid; F0VFP2; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000007494; Chromosome VIIa.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.30.70.100; -; 2.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 3.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 2.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494};
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 532..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1150..1179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1725..1744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1750..1773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..231
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 247..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..1859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1886 AA; 197778 MW; A97681282089EB3E CRC64;
MDEPAIGEPS EAAYVPLSSA STSQHPRTDV WEFQVGGMRC GNCARKIENR LRQTFTSSIL
SVDVDVRGGR VKVSATRSPG ASDTAGVVTH AEIAGAIAVL GLDVSLLSSG SPVAASCVAS
VDFSASTSLA TTVETGKQAE RGAEENRGNP EASLKEQLRY AELRVEGMTC ASCARHIEKH
VQKLPGVLSV AVNLILESAT VEYRASCHAS SPTVTVEDIR RHVEDLGYRT SVGLDRPLYT
SSAASVFPKR ASPSGDGGGA AGSATESTGE KTRRASSSAL LAPCTPPAAT LHLCLLPPFP
SRALESCSPQ ADLPTFSSSS RGASRASSSL LNPNTQPLLQ SASTQAEPRP TPPLPARPFA
RARAVPQAHA RPSSSAADAS GPRCSAAPSE SVAAFVSWLE KQQGIIAVAS ASDAGAAERA
RRRSQVFFSL LRSATSRGED DAALSRGPSA YPPSLASSAL CAPHETRWER RDFQLGLPGI
RVTYSPDQIG AREILERARE AGWSVEWDST GKKKFGDLQQ AAHAENALGK QFVCALLPSI
VVFAVMMIIP MDAFPEWMNL RVLPGISARL LVVLLLTTAV MYGPGWRFHR AAYEAARRGM
TDMNVLVSLA TNIAFLYSLV AVIFTIYVSV TVPPGGRLAA STGSLALSSH GTPFRSPSSA
SLTSPPLRSS PLASFSLSPG AVVDPAGPAY SSSAVEIVTR GAGLGEPRKQ LLDAVQELSL
SEESVEQEWN FKFSILPSHA RRFSPLPRFL AAVSTAFPDA TTDHPEAGRD VSGRRGADGQ
RSDSRLLTRD EVHVNSFSGR APGHSVDASN LQMPPSLSLR VVHSQSPASS FARPPPSTRA
LGSDASEFSD VPSSSSAASH ASAEPADPPT FFDLSAVLIC VLLLGKLLEV KAKRRAVAAL
DELSAAQPEF ALLVRNQSSS SVTSGRCVIR RCENTPSAGG AKLQSGESHS GAAEETDADP
SEFVGVRPSE KASGNRADSD NDRPVRTEKR YKGDAGQEEA RRRPHRPRTE NFEELIPVEL
LQLGDVVRVP PGATVPADGE KINEEESLLS EALLTGESVP VSKQKGDSVL GGSLVVGGHT
GAPSLHRSAP AGPSADFGAD RTTREGRVGA SLLLVRVQKL GTASVLGQIF RLVKDAQGTK
TKTQQFIDNV AGYFVPGVLL ISAVTTVVWL ILLFGGFVTP SFRDVDADTL NAFPVASRIL
FALQFGIGVL SIACPCALGL AAPTALMVGT GVAARLGILV KSGQAFELAT KLKALVLDKT
GTLTTGKFEV QEVVLLGSSF ARLAALAKSS DWRDVLSPAA LAPHVCAPNS SSSSPLAPCA
DVRVALAQAA ESPSASHSVS AWGLSVRDLS SPGRPGGLAR SHLSLGPTES EAAKGDTRGH
GPCLSPSLPE KAGRLEKAIN PTASPNTSSA PAQGCSVSSF REMVSAFVWI LGVAERHSEH
PVAASLMEFV LAWKDLAPLA SPSLFKALPG RGLSCRIGKH LAVEVISLTS AETSRAPRRS
FEFPAVCASA AFGSSDGAGS SSPSSPVSSG CCSKSERRDA REERTEAREE GEPRGAGEAW
AEDQQRGGAT VALLVVNQVC LGALALRDAV KLESREAVSL LESHFGLDVW MCTGDSLHTA
MAIADAVGLP RSRVVAEALP SAKVAFIEKL QRPDETQTYR PVGMAGDGLN DAPALAHADL
SMAIGAGADL ALTAADVVIL KSRIADLVTF LELSRAVLFT IRLSVVWACI FNAAGIPLAA
GVLYKFRVFV PPTVAGAMMA LSSVLVISNA LLLRRFRPSL LPRLSSSSSL VCGSLSAFWS
SLSCSFSSAF FQGSVDRRGR RVYAADARPP RESSLRAASS DSGATEPERT ANCPENRTRV
GLAAEVASPR AQDFTLPLVS RQCTDA
//
