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Database: UniProt
Entry: D5EBH3_METMS
LinkDB: D5EBH3_METMS
Original site: D5EBH3_METMS 
ID   D5EBH3_METMS            Unreviewed;       909 AA.
AC   D5EBH3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ADE36524.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:ADE36524.1};
GN   OrderedLocusNames=Mmah_1006 {ECO:0000313|EMBL:ADE36524.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36524.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36524.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024}.
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DR   EMBL; CP001994; ADE36524.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5EBH3; -.
DR   STRING; 547558.Mmah_1006; -.
DR   KEGG; mmh:Mmah_1006; -.
DR   HOGENOM; CLU_001771_0_3_2; -.
DR   OMA; GGKFMVC; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 3.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 3.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   NCBIfam; TIGR00003; copper ion binding protein; 2.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 3.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; SSF55008; HMA, heavy metal-associated domain; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 3.
DR   PROSITE; PS50846; HMA_2; 3.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Hydrolase {ECO:0000313|EMBL:ADE36524.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        251..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        498..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        537..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        853..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..68
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          93..159
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          161..227
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   909 AA;  97158 MW;  B0E5DA59B424346A CRC64;
     MAEILLHVSG MSCGHCTKSV HDALEKLEGV KSVEVNLDSG IATINYDPSS TSVETMKETI
     SQAGYSVEDQ EENACEGTCP VSIEEISKQD AEKTLSLNIY GMSCTACAKR IETGLEKVDG
     VREVSVNFAS EKASVTYDTN KLDLREIRDR IESLGYGIRS DRLTLNITGM SCASCVSNVE
     KALKNQPGVL EANVHLSLEK ADIIFDSSIM DPEGLIKVIE NTGYGASIPE DTKNNLKDKQ
     EQERIEQQKN VLIAFALTLP LTLGAMQGML RIDPYVPDIL ANNIVQFTLA TLTLVFPGRQ
     FFTGAFRGLQ HGSADMNLLV ASGTGAAFIA STAAAFLNLG AGYEHTYFDS AAMLITFILF
     GRYLEAKSRG KTSEAIRKLM GLRAKTARII MDGEEKDIPV EEVKPGDIVV IKPGEKIPVD
     GEVIEGDSAV DESMITGESI PVEKSTGDTV IGATINKTGS FRFKATKVGA DTALSQIIKL
     VERAQTSKAP IQRLADIVAG YFIVIVMTIA MLAFFFWFFI GYGTFNVAEL TGVASPFLFA
     LLIAITVLVI SCPCALGLAT PVAIIVGTGM GAENGILIRD GESLETTPKV DTIVFDKTGT
     LTIGKPFLTD VATTGNYEEN YLLQAAASVE KLSEHPLAEA IVEGAKSRKL QLKNISGFES
     FSGKGVAGEW DDHSVIIGTK RLMEEKAIYP GDVANYSNRF EDEGKTAILV AIDGTIAGVL
     AVADVLKEEA PSVIAQLQEI GLGVAMITGD NSKTAQAIAR QAGIDTVLAE VLPADKAAEV
     EKLQKQGKRV AMVGDGINDA PALSQADVGI AMGAGVDVAI ESADIVLIKN DVKDILKALN
     LSKLTMKKIK QNLFWAFGYN TLGIPIAAGV LFPVFGQTLI TPAMAAAFMA MSSVSVMTNS
     LLMKRKRIE
//
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