ID J9HRH4_9SPIT Unreviewed; 1147 AA.
AC J9HRH4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Ca++-ATPase {ECO:0000313|EMBL:EJY66794.1};
GN ORFNames=OXYTRI_12914 {ECO:0000313|EMBL:EJY66794.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY66794.1};
RN [1] {ECO:0000313|EMBL:EJY66794.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY66794.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY66794.1}.
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DR EMBL; AMCR01020341; EJY66794.1; -; Genomic_DNA.
DR AlphaFoldDB; J9HRH4; -.
DR EnsemblProtists; EJY66794; EJY66794; OXYTRI_12914.
DR OrthoDB; 213167at2759; -.
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; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
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 Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 4: Predicted;
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 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 870..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..139
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 890..1073
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 635..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 128919 MW; FF059960E919CC0D CRC64;
MQMEHTLDAP LLNKQSEFNL SKTDLKSIFD CYCQRQEKTD QDTKRGSSGQ VVVSAKDQEK
ERQLTVLNKY GGAKTIVGSL KSDLQNGLNS KDQRDMDKRR LLFGENKKKD IPPVSILALI
IEQFEDEILR LLLLAATVSL AIGIWKEGLG KGWYEGVTIY FAILIIVSVT AMNDYVKDKQ
FRKLNDVRKE RYILARRNGH TQSISTFDIV VGDIIELKQG DLVPADCLLI ESDDLQTDES
SITGESEHIK KFPQNGSLEQ EELKRKKYMP NPFLLNDSQI VLGKGLAVVC AVGVNTQTGE
VEEKLFQDDD EGTPLQQKLE RVASFIGKVG MYVALATFIA MCLNLVINRI LNNQPILDIA
VTRGVVNAVI VAITIIVVAV PEGLPLAVTI SLAYSVNQMR KENNLVRRLE AAETMGGANE
ILTDKTGTLT QNKMSVIQVY TEGKTHNALE EVTQNTQDLI IKACSLNSNS HLIIDDKTYQ
EKRVGNQTEC ALLDFVNRTL LKLDKQDKTY ESIRKNNKIL KMYPFNSTTK KMTVVVEIEH
MKTVRIYTKG ASENIIDDCD RVIEGGSQTT NSYGGMGGAA SGLGAGEVRD FDNSMKTHVK
DTVIRNMAMN ALRTIAVGYK DMSYDKFREI QERLEDRGED DENSEEFKSQ DDFNNSNLGE
HEEQLDKNLI LIGVFGIRDI LRPEIKEAIQ KCHQAQVTVR MVTGDNQDTA MAIAREIGII
PQLGHDNEGD KYAAKFRCMT GADFRKHFGG LRMDLQNGEQ KEVINDIHAF REIVKELRVL
ARSTPMDKYI LTLGLKQLGS VVAVTGDGTN DAAALKKADV GFAMGKAGTE VAKEAADIIL
LDDNFGSLVT SIKWGRNVYD SIRKFLQFQL TANLVAMFMA LVGGIFLGDS PMNSIQMLWV
NLIMDTFAAL ALATEPPKED IIKGKPHPKN ESIVTPVMWR NVLGQSAFQI TILSLFLFQG
EYILNTEYRR PDEPWTYENG LQTTIIFNTF IFMQVFNEIN CRKILPSEFN VFDGFFNNPQ
FLFVMFITVL TQILLVQYGG EAVKCSPLSF NQHLFCITVG ALSLIVGFFV KFLPLELFSI
FQFNEQPLSI EEKEHAFKAS LRKSRSLYRM SSRNLNLSKD SKGNHRIIDE KVQRIKNLRK
QSSKKML
//
