ID A0A1P6C3Q8_BRUMA Unreviewed; 1149 AA.
AC A0A1P6C3Q8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=Bma-mca-2 {ECO:0000313|EMBL:CDP95672.1,
GN ECO:0000313|WBParaSite:Bm5210a.1};
GN ORFNames=BM_Bm5210 {ECO:0000313|EMBL:CDP95672.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm5210a.1};
RN [1] {ECO:0000313|EMBL:CDP95672.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP95672.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP95672.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP95672.1};
RG WormBase Consortium;
RA Ghedin E., Paulini M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm5210a.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) 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 EMBL; LN856947; CDP95672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P6C3Q8; -.
DR SMR; A0A1P6C3Q8; -.
DR STRING; 6279.A0A1P6C3Q8; -.
DR EnsemblMetazoa; Bm5210a.1; Bm5210a.1; WBGene00225471.
DR WBParaSite; Bm5210a.1; Bm5210a.1; WBGene00225471.
DR InParanoid; A0A1P6C3Q8; -.
DR OMA; CFTLYFA; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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; 3.
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:SF451; 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 Reference proteome {ECO:0000313|Proteomes:UP000006672};
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 84..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 316..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 361..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 812..831
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 885..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 927..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 966..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 997..1019
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 31..105
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1149 AA; 126485 MW; 8BBC887F0AD9FE49 CRC64;
MTAREFGCTL SELRALMDLR GAEALAQVNK KFGGIEGLCA KLKTDPVNGL PNEKASLEER
RRIFGRNEIP PAPSKSFLRL AWEALQDITL IILLVSALVS LGLSFYKPPE NSETGGHDAN
EREAGWIEGA AILLAVIVVV LVTALNDWSK EKQFRGLQAK IETEHKFSVI RNGEALDTVV
TELVVGDIAR VKYGDLLPAD GLLIQSNDLK VDESSLTGES DLIKKSPEGD PVLLSGTHAM
EGSGKMVITA VGVNSQTGII MTLLGAAKGT TSKKSPNTVA PEEQINGTTS EIERKHSVDS
AEYDCKLPKS VLQGKLSALA IQIGYMGFVV AGATVVILIV RHCITHYGIN HESFQPSDFS
YFVNFIIVGV TVLVIAVPEG LPLAITLSLT YSVKKMMKDN NLVRHLDACE TMGNATAICS
DKTGTLTTNR MTAVQSFING KFYKEYIPKF EQLDKKTRQI LIEGISVNSG YNSQVILPEK
HGIQRTQLGN KTECALLGFV LDLGQSYENI RKEHPEESLF KVYTFNSVRK SMMTVKRLPN
GYRVYAKGAS EIIMSRCSYM FGPEGKVKPF DSEQQQEMTR DVIEPMASDG LRTIGLAYKD
YILIGKPAAE NDTVYEGEID WEDEEAVRME MTVIAIIGIK DPVRPEVPAA IERCQKAGIT
VRMVTGDNIN TARSIATSCG ILKPGSGFLA LEGREFNERI RDANGKVNQA KFDAVWPRLR
VLARAQPSDK YVLVKGIINS KFSKNREVVA VTGDGTNDAP ALKKADVGFA MGIAGTDVAK
EASDIILTDD NFTSIVKAVM WGRNVYDSIS KFLQFQLTVN VVAVTIAFIG ACAINDSPLK
AVQMLWVNLI MDTLASLALA TELPTENLLE RKPYGRTKSL ISRTMVKNIV GHATFQLTVL
FAILFWGDKF IPDLENGRWA PLNSPPSKHF TIIFNAFVLM TLMNEINSRK VHGERNVFKG
LFTNPLFCII WILTLISQVL IVQFGGAWVS TAPLNEIHWA VCVACAFGTL LWGQILATIP
SKVLPKFFSF GGGEVQPTSV LVTGEYDTSD GLVKGMSKED QKRPGQMLWL LGLTRLQTQM
RVIRAFQTNA CTTHPTSLTT STAERLRASY RRLQLARERE EQRRIHSARL DEEIGIDSMS
KDKGVIKFV
//
