ID A0A1I7Y0Y4_9BILA Unreviewed; 1261 AA.
AC A0A1I7Y0Y4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g11528.t2};
RN [1] {ECO:0000313|WBParaSite:L893_g11528.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
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DR AlphaFoldDB; A0A1I7Y0Y4; -.
DR WBParaSite; L893_g11528.t2; L893_g11528.t2; L893_g11528.
DR Proteomes; UP000095287; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
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; IPR022141; ATP_Ca_trans_C.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 351..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 389..419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 875..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 918..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 956..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1026..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 32..106
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 310..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 137709 MW; DAE2B142189C12B7 CRC64;
MSGSKEYGCT VEELRTLMEY RGSEAREKIE SDYGGVEGLC QRLQSNPSDG LPANKEELDR
RRAVFGANEI PPHPPKSFLQ LVWEALQDVT LIILLVSAIV SLALSFYKPP DDGKTAGGDA
SEHDTGWIEG VAILISVVVV VLVTALNDYT KERQFRGLQA KIETEHKFAV IRGGQQIQIV
VNELVVGDIA QIKYGDLLPS DGVLIQSNDL KIDESSLTGE SDLIRKSPDH DPMLLSGTHV
MEGSGKMLVT AVGVNSQTGI IMTLLGAAKT AVEEERKAAK REGDVQSANA LEDGTAQALL
TEDHIKADGF NNGAVAGGSE AGDTKKGDEE EEGRKERSVL QAKLTRLAIQ IGYAGSFVAG
CTVLILVIRF CISKYAIGGE EFTLADFQYF INFLIIGVTV LVVAVPEGLP LAVTLSLAYS
VKKMMHDNNL VRHLDACETM GNATSICSDK TGTLTTNRMT VVQSYINDVH YKETPKFEKL
DPKTRDLIIN LISINSSYAS QVIPPKQAGE QMTQLGNKTE CGMLGFVLGL GQSYQDIRDR
HPEETIFKVY TFNSVRKSMS TVISMDSPSG TTYRVFCKGA SEIVLKKCRW FLGKNGQVTK
FSSKDCDRLV KDVIEPMASD GLRTICLAYK DYVPGNAEEN QVNFAGEIDW DNEDAIVNDL
TAVAIVGIQD PVRPEVPEAI RKCQRAGITV RMVTGDNINT ARSIATSCGI LKPGEDFIAL
EGKDFNAKIR DENGEVSQAK LDAIWPKLRV LARAQPSDKY TLVKGIIDSR ITDNREVVAV
TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FTSIVKAVMW GRNVYDSIAK
FLQFQLTVNV VAVVVAFVGA CAIEDTPLKA VQMLWVNIIM DTLASLALAT ELPTENLLRR
KPYGRTSPLI SRTMSKNILG HAIYQLVVLF VLVFYGEVLF GIPCGRRVEL HAPPTQHFTI
VFNTFVLMTL FNEINARKIH GERNVFEGIF SNPIYYIIWI GTMVSQVLIV QFGGRWFSTA
ALNLEQWLWC VALGVSVLLW GQLVTSIPTR GLPENMAIGS GEVESTEHIL NGEYEDPETH
EKRSGQILWI RGLTRLQTQL RVVKAFRSTL EDFDERRSIA STQSCQSMRG GWSSFFLGGM
SNNQPTSTSP TEQPLSGVRG AVASLMQRTS GPQPYPYYHW QQARTPSPQP PVSPQAIVVE
NGRGSANAAI VRGDKVEKVP LVQRWSPSSG AASSTTTSSA AAAHRMGKSI SLDTPISIAH
V
//
