ID A0A0N1I8I8_LEPSE Unreviewed; 1217 AA.
AC A0A0N1I8I8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative calcium-transporting ATPase {ECO:0000313|EMBL:KPI87958.1};
GN ORFNames=ABL78_2949 {ECO:0000313|EMBL:KPI87958.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI87958.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI87958.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI87958.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI87958.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJSK01000067; KPI87958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1I8I8; -.
DR EnsemblProtists; KPI87958; KPI87958; ABL78_2949.
DR VEuPathDB; TriTrypDB:Lsey_0067_0110; -.
DR OMA; CFTLYFA; -.
DR OrthoDB; 147844at2759; -.
DR Proteomes; UP000038009; 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; 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; PTHR24093:SF531; ATPASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR24093; CATION 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 PRINTS; PR00119; CATATPASE.
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; 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 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 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 960..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1130..1151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..126
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 987..1182
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 1217 AA; 130534 MW; 806569A5C74A45FB CRC64;
MEKCCDAFGG SSRVGSGPVK LAEMVGHKRV DVLTRDYNGP GGLLAELGVR GGPLGAAVDL
SSPEQRSAAL QRREVGIPVS TIPSRQARYG VNVLPEPPKE TIWHFIKESI QGDRVVQILI
GAAVISMVLG MTTPDFRTGE VDLTTGWIEG AAIFASVFIV TAVNAVNDYR KQEQFAEVTR
AEDATRRRIT VWRYVPHHTS TSSDGLVCVA MELPSAEIVV GDVVQVSSGM QLNFDAILLE
SFGPIITDES SVTGENDEVL KQVLTDPFLI SGSSVLDGSA EGMALVCSVG ANSFSGEIAV
SIQTTEKTNT PLQDQLEVMA DIIGKFGVTA AVGSFVSLLL KELFMHFVYG TGLYAMKFFE
NLTTAIAIVV VAVPEGLPLS VTISLAYSMR LMLKDGNLVR HLAACETMGG ATVLCSDKTG
TLTAPTMRVK QVFLGAATYT MDCKSEENSA NFTANSRAGM QAVPRPYAAL PTTLDLHRDV
PTFGRAPHPT GTGQGIVAAV SASSVQLLLD CIVANAVDPE VGRAINKTSE ALLQLCHVMS
CANSIATAQD VEAFRSTKDR MLVALQDPTR CRRFPFSSHS KMSLCMLRQA SPSTGVSSGR
SRTRLYATGA AEVILARCTM YLNDQGSPAP LTAEMRAFYE HNMTQYAESG LRAVCCAYRD
AQGYAESALW NPSPVQQHSG SITATSYEGD FCMIGIVGLE EEVRPEVPGA VAQCFGAGLR
VIMITGDATL TAMSIARRCG LLRHSGSPVS ASATAAAAGW DNCRTPNSSG RLITAGPLPT
ALDTNMSTID SNSDAAVFVN ASPVGYPCTG NGGQACDFSS DIVFGGSAWA VKSPPLHASP
QQLLDGGFVL DGPTFRQISD AELLQQYIPH IRVLARATPM DKKRLLHLLR QLDSNAVIAM
TGDGTNDAPA LKLSDVGFAM NGGSDVAKRA SDIVLLNDNF IGMVKATMWG RNVKDNIRKF
LQFQLTVNFA ACIVSFCGAI LSEQNMSPLK PVQLLWLNLI MDTLAALALA TELPNEAMLL
SRPPEPKDTP IIVPSMWFQV GFQSSFQLVC QLYLLSWGKS LVSRESHGRT ISAGMPISAG
AGAAAEIAIN EAHICFVFNT FVWMQIFNFF NARLLHRNEG FFENWKDSSV LLIIVSIIVV
LQVAIVELGG KVMSTVPLTP AEWFWSVSIA SITLPVGALA RVVYARYSSR HSIRDGCSRG
LMSRIRYRLL DSELKGK
//
