ID F0VRG2_NEOCL Unreviewed; 1341 AA.
AC F0VRG2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=P-type Ca(2 )-ATPase, putative {ECO:0000313|EMBL:CEL71072.1};
DE SubName: Full=Putative P-type Ca(2+)-ATPase {ECO:0000313|EMBL:CBZ56310.1};
GN ORFNames=BN1204_067350 {ECO:0000313|EMBL:CEL71072.1}, NCLIV_067350
GN {ECO:0000313|EMBL:CBZ56310.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ56310.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|EMBL:CBZ56310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ56310.1};
RA Aslett M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBZ56310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ56310.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {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).
RN [4] {ECO:0000313|EMBL:CEL71072.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL71072.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FR823393; CBZ56310.1; -; Genomic_DNA.
DR EMBL; LN714487; CEL71072.1; -; Genomic_DNA.
DR RefSeq; XP_003886335.1; XM_003886286.1.
DR GeneID; 13445533; -.
DR VEuPathDB; ToxoDB:NCLIV_067350; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; F0VRG2; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
DR GO; GO:0016020; C: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 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; 2.
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:SF128; CATION_ATPASE_N DOMAIN-CONTAINING PROTEIN; 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; PR00119; CATATPASE.
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 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: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 233..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1264..1282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1294..1312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..258
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 144754 MW; 13F6CC68C4C0CDC8 CRC64;
MAAPAPDNDV PSSAGQDPTP TGSAAVPEVS AGGNEHSKSA DGAVREDTQA GSAVAEGTAA
GQDGDSPHRE FHHHRTVSRR LSSKRDSASA PNGAGHMHLG KSISSVSQCH REEHARLLPV
GSSMSLAPGM GYENVETEVI DRLSKSHVSL KELVETARKT DPEAFRMAVT LTEQSHPTSG
KNRFASLSIE ELAKEFGLKD LNNGLTEEQV QENRRIYGPN ILEKDKSEPV WKIFIQQFLS
PVVLLLLIAS IASLALQEWV EGAAILIIVT LNASLATYME KSASNALAKL ASMAAPGCVV
VREGKVQTVG AVDVVPGDVV VLATGNSVAA DMRCIESVEL KTNEALLTGE SEDISKTLRA
KDYDTPFATN LCFASTIVTN GSGRGLVFAT GMETQVGRIA QQLKKAGEGS RLTPLQRGLN
RLGGMIGLIA ICVLIVVVVV AILTGYKDPA HPDADPVFTI VLVAVGFAVS SIPEGLPMVV
TICLSLGARD MVKRKANVRK LPAVETLGCC SVICSDKTGT LTEGKMTAVR LVTVCRQGKV
VNADGFTKSF GFYPTKGFDP NGGIFDLNKL DEKTKNNLMI QYRDGAFQDY DAICHNYGNP
ANKDPTTKLV RSVMLSGYLN SHATTLERDP DTNRWLAKGN MSEGAIVVGA AKARFGSPLA
GKSERAGMHD AKLDYPRVAD LEVPFNSSRK MMMTVHQLPS ANFFGDICLN SDGNKYTHCA
IVKGAPDRVL QHVRYTVREG LSGPSVDWDT PVTPEEIQSV EAVNLDLSQQ ALRVLALTFR
PLTDADVAAL RKQDGADLRL RFALGETREE LCLLGVIGSV DPPRPGVREA IERCGEAGIR
VIMITGDQRP TAVAIAKDIG LLTSHDDSEQ ASIQCSGLHI DDDPMNEHLP EAQLDEIIAR
VKVFSRAQPE DKIAIVEALK RQGHTVAMTG DGVNDAPALK AADIGVAMGI AGTDVAKGAS
EMVLLDDNFV TIVAAVEEGR KIYSNIQKFV CFLLGTNIGE IIYLTIAIAA SMPLPLEALQ
VLFLNLMSDG CPAVALAKEP SDDENMKIPP RPRKQPIMTR DWWLYGNLPH TVFEAGCVLM
SLALGLYLCT GVVQLTPLHD QCSYYTAIDV SNNKEIDYRY FCRSFEYRVT QDYTGWVTHI
DFWNPETQTM EQVLGAIAGK HPDVTVRTPG LAEYITEAMS DGCPSDVATD PKTGFCMPAA
GTTVSSSSET PKGAAPRDYF DVSARGAKMG RTCSFITAVW CEMLRAYTVR SWHWFFLVFN
RNPWMHLACS ISATLTSLLT IVPGIQSAFS TCALPWYLYL FAIGCGFVNL ILDELIPKPL
YRWKNARETR AALASKASAV A
//