ID Q57VN8_TRYB2 Unreviewed; 1102 AA.
AC Q57VN8; D6XMU5;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=Tb08.29O4.290 {ECO:0000313|EMBL:AAZ12887.1};
GN ORFNames=Tb927.8.1160 {ECO:0000313|EMBL:AAX70320.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:AAX70320.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:AAZ12887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12887.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [2] {ECO:0000313|EMBL:AAZ12887.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12887.1,
RC ECO:0000313|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [3] {ECO:0000313|EMBL:AAX70320.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX70320.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT ".";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAZ12887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12887.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT through 8.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; AC159438; AAX70320.1; -; Genomic_DNA.
DR EMBL; CP000071; AAZ12887.1; -; Genomic_DNA.
DR RefSeq; XP_846953.1; XM_841860.1.
DR AlphaFoldDB; Q57VN8; -.
DR STRING; 185431.Q57VN8; -.
DR PaxDb; 5691-AAZ12887; -.
DR GeneID; 3659093; -.
DR KEGG; tbr:Tb927.8.1160; -.
DR VEuPathDB; TriTrypDB:Tb927.8.1160; -.
DR eggNOG; KOG0204; Eukaryota.
DR InParanoid; Q57VN8; -.
DR OMA; GIMWRNI; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000008524; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IBA:GO_Central.
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; 2.
DR PANTHER; PTHR24093:SF369; 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; 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 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}; Hydrolase {ECO:0000313|EMBL:AAX70320.1};
KW Ion transport {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:UP000008524};
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 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 315..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 354..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 806..827
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 914..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 984..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 69..141
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1102 AA; 121242 MW; 54893A1371CFC2A9 CRC64;
MISPKDTSNY GTLAGRGRER QAFLSTGLTR SDGSVAVEVE LEDRIGIGIK GELHTLFSCV
GDAKPLYEEL GGVEGIAERL GTSITDGIDS FSVENRRAVY GRNELPEEAP LTFWKIFKAA
WSDRMIILLT LAACVSLILG LTVPEPGHEK VDYKTGWIEG TAILMAVIAV TSASSIQDYR
KELKFRALVE ENSAQPISVI RDGHKVTVDV TEIVVGDLVS LSPGLVIPVD GLYVRGLSVV
VDESSVTGEN DLKKKGAEHP ILLSGTVVST AEDAYILACA VGESSFGGKL LMESRLDGEP
RATPLQERLD ELAGFIGRIG IGAAVILMSL LSLFYILLVL RGKEELRAKK FLDIFLLCVT
IVVVAVPEGL PLAVTIALAY SQSQMQKDNN QVRRLCACET MGNATQICSD KTGTLTQNRM
TVVQGYIGMR RFRVSNPGDP SSTVNLEGVS SDAQSLLMLG LALNSSSEKE LLPGNVGAES
DLLSRWTWRT DKGNKTDQAI LDFVDRVLIS VPGSCNDKEL PHQKLRMTNR SRGFAIFPFT
SERKFMTAVV AGADGVVMQY VKGGSDRVLG MCNRYLSSEG REEPLTEEVT EMITAQIRSI
AGDANRTIGV AYGRIGTDGA VPEEEPEGPF VWLALLGIQD PLRPEVVDAV RMCQRAGVTV
RMCTGDNLDT AVAISRQCGI YNRLRGDLAL TGKDFRNLVY DTYGDEANME KFWPVLDRMM
VMGRSQPLDK QLLVLMLMLR GEVVAVTGDG TNDAPALRLA NVGFVMRSGT DIAVKSGDIV
LLDDNFRSVQ RAVVWGRTVN DNIRKFLQLQ LSINIASIVV VFVGSFLSAH DMSPLTTVQL
LWVNLLMDTL AALALATEQP TEDCLNRGPS SPRAPLVSRR MWLTILTATV VQVVSVLLLT
QYGGKWLKAK GKELPTVVFN VFIFFTIFNM FNARKVYDEV NVFEGLFIRS KSFLVIVVCC
VGFQVLAVEV LKEFMSCVPL RAEQWIASIL IASLTLVFVS VSRLIPVSEP SFEKGAELED
MEPGARRIAV KLAEDVEHHS SASNNVGSYM RFGQRLVARA QWQRVREHVT MRGVSQFWWS
RHSHPRERGW RRMSAWCEER IR
//