ID D6PJK7_9ZZZZ Unreviewed; 760 AA.
AC D6PJK7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Heavy metal translocating P type ATPase {ECO:0000313|EMBL:ADD95908.1};
OS uncultured organism MedDCM-OCT-S01-C5.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=743601 {ECO:0000313|EMBL:ADD95908.1};
RN [1] {ECO:0000313|EMBL:ADD95908.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20393571; DOI=10.1038/ismej.2010.44;
RA Ghai R., Martin-Cuadrado A.B., Molto A.G., Heredia I.G., Cabrera R.,
RA Martin J., Verdu M., Deschamps P., Moreira D., Lopez-Garcia P., Mira A.,
RA Rodriguez-Valera F.;
RT "Metagenome of the Mediterranean deep chlorophyll maximum studied by direct
RT and fosmid library 454 pyrosequencing.";
RL ISME J. 4:1154-1166(2010).
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DR EMBL; GU943109; ADD95908.1; -; Genomic_DNA.
DR AlphaFoldDB; D6PJK7; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
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; 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 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; 1.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 95..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..72
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 760 AA; 80628 MW; 530DF7F5AF498E6D CRC64;
MEKNQLNLSV SGMTCAACVA SVERVLSNVE VVEAVSVNLP LEKAVISLRE SASQTHRAAC
IAAVERAGFG ASELLPALTT RQVNEDRVAQ QRRRVALAFV LAIPVFVLSM LLDDLGSAGP
LDARLTLAML AAWPVYVISG AEFHRQAWAS LRRGTANMDV LVHLGTTVAM VWSTLVTLAP
VLPSLPAFVG QAQHVFFDGA AFIIAFVLLG NYLEAKAKLK ATDAVHGLMR LQPKEAWVVV
EEGTVATPID EIPRGTLLKV RAGETVPLDG VVEDGTAMLD ESMMSGESFP VRKREDDTVS
AGTTVLDSTL LVRTTALVGD TMLAKVIELV DEAQMGKAPI QRLVDRISAV FVPVVLVAAL
VAASVWWFMA ETLAPNSDMA PSEMAVMVLV STLVIACPCA LGLATPTALV VGTGRGANFG
LLIKGIEALE QAHATSTVVL DKTGTITVGS PRVSHIELLD SDVQELLCLA SALELESTHP
LASAVHTAWE NIGYARPEVA DVRTFPGLGL VGSLDGEPVA VGNLELMEER LGTLPDDLEE
KIALRARRGT TVVLVAKGPR LLGWLEFSDR IRETSEAAVR RLKQTGIRIV MLTGDREEVA
QTVADAVGIT EIVAGVKPDE KAERIRALQE EGVVAMIGDG INDAAALTVA NVGIAMGAGS
EIALESADIV LVRNDLADAV AALDLGRATM TRIRTNLAWA FVYNLIGLPL AMGLLFPWTG
WLLPPAFAAA AMSLSSVSVV SNSLVLRWWQ PGASLRSGEF
//
