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Database: UniProt
Entry: M0NEX3_9EURY
LinkDB: M0NEX3_9EURY
Original site: M0NEX3_9EURY 
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
//
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