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Database: UniProt
Entry: J3LA07_ORYBR
LinkDB: J3LA07_ORYBR
Original site: J3LA07_ORYBR 
ID   J3LA07_ORYBR            Unreviewed;       904 AA.
AC   J3LA07;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB02G14740.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB02G14740.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB02G14740.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB02G14740.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR   AlphaFoldDB; J3LA07; -.
DR   STRING; 4533.J3LA07; -.
DR   EnsemblPlants; OB02G14740.1; OB02G14740.1; OB02G14740.
DR   Gramene; OB02G14740.1; OB02G14740.1; OB02G14740.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_0_3_1; -.
DR   OMA; MVCPRIH; -.
DR   Proteomes; UP000006038; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.
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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR46594:SF6; HMA DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00942; CUATPASEI.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        242..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        273..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        301..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        456..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        500..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        838..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        867..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          34..100
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   904 AA;  97756 MW;  32C39B8C4B1FBAB7 CRC64;
     MQEEDIIEAI EDAGFEAELL PDSSVSQPKS QSTLSGQFRI GGMTCAACVN SVEGILKKLP
     GVKRAVVALA TSLGEVEYDP SVISKDEIVQ AIEDAGFEAA FLQSSEQDKV LLGLTGLHTE
     IDVDILHDIF NRMEGLRQFS VNLALSEAEI IFDPEVVGLR LIVDTIKMES NGRLKAHVQN
     PYIRAASNDA QEASKMLRLL RSSLFLSIPV FFMRMVCPRI HFMRSLLLMH CGPFHIGDLL
     KWILVSIIQF GVGKRFYVAA YRALRHGSTN MDVLVVLGTT ASYVYSVCAL LYGAFTGFHP
     PIYFETSAMI ITFVLFGKYL ELLAKGRTSD AIKKLVELVP ATALLLLKDK EGKYAAEKEI
     DASLIQPGDV LKVLPGSKVP ADGIVVWGTS HVDESMVTGE SAPISKEISS IVIGGTMNLH
     GILHIQATKV GSGTVLSQII SLVETAQMSK APIQKFADYV AGIFVPIVVT LSLVTFIAWF
     LCGSLGAYPN SWVAETSNCF VFSLMFSISV VVIACPCALG LATPTAVMVA TGVGANHGVL
     VKGGDALERA QNVKYVIFDK TGTLTQGKAT VTSTKIFSGI DLGDFLTLVA SAEASSEHPL
     AKAILDYAFH FHFFGKLPSS KEDIKKRKQE IFSQWLLEVA DFSALPGKGV QCLINGKKIL
     VGNRTLITEN GINIPEEAEN FLVDLELNAK TGVLVAYDSK LIGLMGMTDP LKREAVVVVE
     GLKRMGIYPV MVTGDNWRTA RAVAKEVGIE DVRAEVMPAG KADVIRSLQK DGSVVAMVGD
     GINDSPALAA ADVGMAIGAG TDIAIEAADY VLVRNNLEDV ITAIDLSRKT FSRIRWNYFF
     AMAYNIIAIP VAAGALFPFT GLQMPPWLAG ACMAFSSVSV VCSSLWLRRY RKPRLTTLLQ
     ITIE
//
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