ID A0A1I8CVA9_9BILA Unreviewed; 1328 AA.
AC A0A1I8CVA9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000850900.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000850900.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000850900.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR WBParaSite; RSKR_0000850900.1; RSKR_0000850900.1; RSKR_0000850900.
DR Proteomes; UP000095286; Unplaced.
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 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; 1.
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; 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:SF253; CALCIUM-TRANSPORTING ATPASE; 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; 2.
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 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 143..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 448..471
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 491..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 956..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1064..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1105..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1134..1157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 85..159
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 146534 MW; 2FAE83F9AFCE3029 CRC64;
MGKDHLNLHD VTDQSKTQVG ETKGGIANGK SPEPCNKVIK EKDVDGNEHD FFEVKIHNDK
PVTVENLKTL MTFHGIESVN KINEDYGGTA GFCSALRTDP NKGLVNDVEV INGRKSKYGA
NTLPATKSKS FFTLLYNACK DPTLIILIAS GFLSLLLSFY EPGQVETNNL NATMASALTD
VSIKLLNNDT KGINYTISNN NINSLNLTLP STDPEPQEEH NTAWIEGAAI LICVIVVVLV
TAINDYSKER QFKLLQAQVE TGHTFSVIRD EKESNIPVSD LVVGDLCRVK YGDLIPADGI
LVQSSDLKVD ESSLTGESDH VKKSLANDVA LFSGTYIMEG SGLMVVTAVG IHSQSGIIMA
LLNGGHRPGH TSSSSGSSSV SDDDSDKKSN SSINFETQTG KPFYKRRRRR SSSSSTSSSS
SSSSSTSTAS SSSGQLSKSI LQAKLSKLAM QIICCGTVMA VLALLILIVR YCVEQYVFDQ
KSFEFSDVHR FIKFFIIAVT IVVISIPEGL PLAIALALTY SVRKMMKDNN LVRHLDACET
MGNATTICSD KTGTLTTNKM AVVQSFINNS YYTSQETQPK THDLPPSTRK KLAQVISINS
AFNSMIEKPT IVGEQVKQLG NKTECALLGF LENIGEDYQL VRKEHPEKEL VKVYTFNSSR
KCMLTIINLI ERGRIVGYRV FCKGASEIIL AKCKFISDDD GQPIEFKSDQ LNAINQDIIE
NMAELGLRTI CVAYKDYILH DARPANFNEV QVDKLEDVDI HNEEEMNKDF DCLGIFGIQD
PVRPEVPSAI ETCQRAGITV RMVTGDNINT ARAIAMQCGI IKPGDDFLIM EGKEFNTRIR
DEHGVVDQEK LDEIWPRLRV LARAQPADKF TLVKGIIEST NSVNREIVAV TGDGTNDGPA
LKKADVGFSM GIAGTDVAKA ASDIILMDDN FTSLVKAVMW GRNVYDSISK FLQFQLTVNI
VAILTAFFSA CFISDSPLKA VHMLWINLIM DTLASLALAT EMPTKDLLTR KPYGRKKSLI
SRTMIRNIVC QALYQLIVLF TILFKGTEIL NIPSGLDAKI HSPPSVHFTI IFNTFVMMTL
FNEINSRKVH GERNVFKHIL DNPMFCCIWI TTFICQIIIV QFSGAWFQAA PLDFNQWSVC
LILGVSVLPL GQLIAFLPSK KLPKSITVGR DVPEITYTSP TGMCGFGSGG LLHPSASGAT
GIQKGVEIFG IHNRVVNGIL IERNNLEDTA PMQQAHAVKL WRRSLRHHQH RRMTNKRLHH
VRKSIDNHFD FGSMTSIEKA NKTKKSHLDR VMKTAGLQRA VSLDAPSRDD REVTAKDSTD
FTPSRPQI
//
