ID M0FLL3_9EURY Unreviewed; 925 AA.
AC M0FLL3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cation-transporting ATPase {ECO:0000313|EMBL:ELZ59464.1};
GN ORFNames=C460_06458 {ECO:0000313|EMBL:ELZ59464.1};
OS Haloferax sp. ATCC BAA-646.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1227464 {ECO:0000313|EMBL:ELZ59464.1, ECO:0000313|Proteomes:UP000011677};
RN [1] {ECO:0000313|Proteomes:UP000011677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-646 {ECO:0000313|Proteomes:UP000011677};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELZ59464.1, ECO:0000313|Proteomes:UP000011677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-646 {ECO:0000313|EMBL:ELZ59464.1,
RC ECO:0000313|Proteomes:UP000011677};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ELZ59464.1}.
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DR EMBL; AOLD01000021; ELZ59464.1; -; Genomic_DNA.
DR RefSeq; WP_008573438.1; NZ_AOLD01000021.1.
DR AlphaFoldDB; M0FLL3; -.
DR PATRIC; fig|1227464.4.peg.1271; -.
DR Proteomes; UP000011677; Unassembled WGS sequence.
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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-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; PF12710; HAD; 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 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 90..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 860..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..106
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 925 AA; 97436 MW; 4B2014319CCFE552 CRC64;
MDIRPLVSFG RTVHEQATAH REAEEASGRE DVPWHALEGE AALERLEASR DGLDDDDAAR
RLDEEGPNEL ADEEGVSPLS LLVSQFTGPL ILLLFVAAGL SLAVGLLPGR DPGYTDAALI
LLILLGNGLF GFVQDYRAEQ ALAALREMAT PDATVRRGGS IRAVPATEVV PGDVVVLEAG
DAVPADARIL TAADCRADES TLTGESVPVD KAADPVESDA ALADRNSVLH AGTTVVRGRA
EAVVVATAMD TELGGIADQL GQARQRETPF EIEVDRLGRR IGVGIVALIL LIAAVQLFLT
ATDPVVVLLV AVTLAVAAVP EGLPAVVTLT LALGSRTLME RNALVRNLAV VESLGAVDYI
VTDKTGTLTE NRMTVTRAWL PDDRTVELDG GSGSVSDSSP DPDPALAALL SCGARCNDTK
ELDGGDHRGD PTEVALVTAA ADAGLDGSRD PDDRLREVPF TSERKRMSVV VDDFDAPGDG
PVALVKGAPE EIVARCDRVL VDGEIEPFTD ERRGRVETTV ATFADDALRV LGFAYAPAVD
PDADDETLES GLVFLGLQGM TDPAREGVAE AVTDCRAAGV RVTMATGDTP RTARAIAREV
GIDADSVVTG TEVAAMDDAE LGRVVEETNV FARVAPEHKV RILRALQDAG YTVAMTGDGV
NDAPALGNAD VGIAMGDRGT QVAQGASDVV LRDDNFVTIR DAIAEGRGIF DNIRKFVNYL
LSANAGEVFV VFLGTLLGAA LFPAVFASES ALVITPVALL WLNLVTDGFP ALALGADPKS
DDVMHRPPRP RDEGVLDRRT VASILGIGVA LTATGLGVFF YALSRSGDLV VAQTVLFTFL
VTAELVRTQS VRLRYRLSPL SNPWLLGAVG LSLALHLVLL YTPVADLFGV VPLGLTEWGW
VAGAFVPFLV ANVCLVWLND RLFAP
//
