ID M0NEX3_9EURY Unreviewed; 916 AA.
AC M0NEX3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:EMA56103.1};
GN ORFNames=C451_04034 {ECO:0000313|EMBL:EMA56103.1};
OS Halococcus thailandensis JCM 13552.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227457 {ECO:0000313|EMBL:EMA56103.1, ECO:0000313|Proteomes:UP000011680};
RN [1] {ECO:0000313|EMBL:EMA56103.1, ECO:0000313|Proteomes:UP000011680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13552 {ECO:0000313|EMBL:EMA56103.1,
RC ECO:0000313|Proteomes:UP000011680};
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:EMA56103.1}.
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DR EMBL; AOMF01000092; EMA56103.1; -; Genomic_DNA.
DR AlphaFoldDB; M0NEX3; -.
DR STRING; 1227457.C451_04034; -.
DR PATRIC; fig|1227457.3.peg.726; -.
DR eggNOG; arCOG01578; Archaea.
DR Proteomes; UP000011680; 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; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 820..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 887..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..95
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 375..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 99586 MW; 098A9B601CF79DAA CRC64;
MLFNKPFDSM TRYDLDTIRS EPWHATPTNE IFSALATDEK GLSPDEADRR LSEYGTNDIH
DAERTSVLEL LFSQFRDPLI YLLVMAALLS LGVGFIPGGE PNYTEAAFIG LIIGANGLFG
FIQDYQATRS VEALRELASP EATVVRDGQK QVIDAEQVVP GEIIHLEQGD AIPADARVLT
ADELRTNESP LTGESTPVQK TTGTVDEDTL LAERHNMVYK NTTVVKGRGR AVVVETGMET
EVGGIATQLG GADEQQTPFQ AEVEQLGKQI GGLVVALIVL VVAVQFLFTA TDPVAILLVG
ITLAVAGVPE GLPAVVTFTL ALGAREMVDR NALVRRLPVV ESLGSVDVIV TDKTGTLTES
RMTVTRLYAS GSVTDLSDST AQSEGEVPER RQIDDDGNER SRSSVTPLLR CGALCNNVDR
TDDEYRGEPT EIALQRIADE ADIESLGERV REIKFSSERK RMTVLVEYGE LTAYMKGAPE
VVLDRCDSIL EDGDVHELTD EKRREILDQT TSFAGDALRV LGFASKAIED PSADADQIED
EMVFLGLQGM IDPPREEVEE AISDCQSAGI RTILATGDNL TTAKAVGEQI GLDPDGAHPG
TDVDEQSDDQ LTRTIEEVDV FARVTPDHKV RLLNALQDNG HTVVMTGDGV NDAPALTQAD
VGVAMGQRGT DVARQASDMI LRDDNFSTIR DAIREGRGIF ENVRKFVNYL VSTNTGEVLV
VFLGVLFGSL LFPGQFSATS KALILTPILI LWINLAADTL PALALGADPH ADGLMNRPPR
PTDEGVINAR VLVSILTIAI LLAVIGLGIF FYALDRTGSL LRAQSLLFTF IVVVELIRIQ
VIRSRYDQTL RSNLWLVGAI GVSLLVHLAV LYTPLHDFFQ VVPLAPVEWV WIVVGFVVFL
LLNVVVSRLN TRVFES
//