ID H9NIE6_PLAVN Unreviewed; 1136 AA.
AC H9NIE6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=SERCA-type calcium-translocating P-type ATPase {ECO:0000313|EMBL:AFF59220.1};
OS Plasmodium vinckei petteri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=138298 {ECO:0000313|EMBL:AFF59220.1};
RN [1] {ECO:0000313|EMBL:AFF59220.1}
RP NUCLEOTIDE SEQUENCE.
RA Tripathi A., Puri S.K.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JQ678694; AFF59220.1; -; mRNA.
DR AlphaFoldDB; H9NIE6; -.
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; 2.
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; 3.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF4; CALCIUM-TRANSPORTING ATPASE 1, ENDOPLASMIC RETICULUM-TYPE-RELATED; 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 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 2: Evidence at transcript level;
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 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 858..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 920..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1087..1111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..81
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 543..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 129192 MW; 8EAFFE969251639C CRC64;
MENILKYAHI YNVEDVLRAV KVDENRGLSE NEIRKRIMQY GFNELEVEKK KGILELILNQ
FDDLLVKILL LAAFVSFALT LLDMKDNEVA LCDFIEPVVI LMILILNAAV GVWQECNAEK
SLEALKQLQP TKAKVLRDGK WEIIDSKYLT VGDIIELSVG NKTPADARII KIFSTSIKAE
QSMLTGESCS VDKYVEKLDE SLKNCEIQLK KNILFSSTAI VAGRCTAVVI KIGMNTEIGN
IQHAVIESNN EETDTPLQIK IDSFGKQLSK IIFIICVTVW IINFKHFSDP IHESFLYGCL
YYFKISVALA VAAIPEGLPA VITTCLALGT RRMVKKNAIV RKLQSVETLG CTTVICSDKT
GTLTTNQMTA TVFHIFRESN TLKEYQLCQR GDTFFFYETN QDDENDSFFN KLKESPNNES
SYKKKISKNI IDDDDDDTDY EREPLINMKS NVNTIISRGS KIIDDKINKY IYSDFDYHFY
MCLCNCNEAS ILCNVNNKIV KTFGDSTELA LLHFVHNFNI LPNNTKNNKM SMEYEKINNI
TKQNSDINGG HDSSTYKKNK ISDKKSEPTF PSKCVSAWRN ECTIMRIIEF TRERKLMSVV
VENSKNEYIL YCKGAPENII NRCKYYMSKN DIRPLTDSLK NEILNKIKNM GKRALRTLSF
AYKKVKSNDI NIKNSEDYYK LEHDLIYIGG LGIIDPPRKY VGKAISLCHL AGIRVFMITG
DNIDTAKAIA KEINILNHDD TDKYSCCFNG REFEDLPLEK QKYILKNYQQ IVFCRTEPKH
KKNIVKILKD LGETVAMTGD GVNDAPALKS ADIGIAMGIN GTQVAKEASD IILADDNFNT
IVEAIKEGRC IYNNMKAFIR YLISSNIGEV ASIFITAILG IPDSLAPVQL LWVNLVTDGL
PATALGKRRP TLITTFLPRF SPRFCSVFAP FSLLTTSHHF SLLRIQPPRA RRNEVQAPTQ
KRQFNKRANP AKIHSHRNIY MDNHTLINFY QLSHYNQCKT WSNFNVNKVY DMSEDLCSYF
SAGKVKASTL SLSVLVLIEM FNALNALSEY NSLFVLPPWR NMYLVLATIG SLFLHCLIIY
FPPLAGIFGV VPLTLHDWFL VFLWSFPVII IDEIIKFYAK KQLNKELGYG QKLKTQ
//
