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Database: UniProt
Entry: A0A0S7DY44_9EURO
LinkDB: A0A0S7DY44_9EURO
Original site: A0A0S7DY44_9EURO 
ID   A0A0S7DY44_9EURO        Unreviewed;      1188 AA.
AC   A0A0S7DY44;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM40221.1};
GN   ORFNames=ALT_008708 {ECO:0000313|EMBL:GIM40221.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM40221.1};
RN   [1] {ECO:0000313|EMBL:GIM40221.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM40221.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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}.
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:GIM40221.1}.
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DR   EMBL; BCLY01000009; GIM40221.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DY44; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_5819; -.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 4.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 4.
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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
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; 4.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        486..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        669..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        710..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1052..1075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1081..1104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   1188 AA;  125558 MW;  43A0CFCD41B5E293 CRC64;
     MAASDLIRAH DSGSSAGRSP AHMATTTVKV DGMTCGACTS AVEGAFKGLD GVGQVSVSLM
     MGRAVVHHDP TIIPAETIAE KIEDSGFDAE IISTDGPSIQ TDSHRNAQDP TPRFSTTTLA
     VEGMTCGACT SAVEGGLKEV RGVKSINVSL LSERAVVEHD ASVITPQQLA DIIEDRGFGA
     TVLETSTPQD GPRGSQEDAD AKSCLMNTTV SIDGMTCGAC TSSVQSAFDG VDGVVQFNIS
     LLAERATIVH DPTVLSAQQI TTIIEDAGFD AAIISSEPKL STSSSTNSVT LSLHGLRDVV
     AANDLEDSLL RRPGIHSASI NMGTYKLAVS YDSAKIGIRT IVEAIEAAGY NALLSESDDT
     NAQLESLSKT KEVQEWRSAF LFSLSFAVPV FVLNMLLPMS LPKLDFGKLR LCAGVYLGDV
     LCLLLTIPVQ FGIGKRFYVS SYKSLKHRSP TMDVLVMLGT SAAFFYSVFI MLVAMCTMAD
     KRPNTVFDTS TMLITFITLG RWLENRAKGQ TSAALSRLMC LAPSMTTIYD DPIAAEKLAE
     EWETAKVYTD EKKPASSSAD RSGPGHRVIP TELIEIGDVV VLHPGDKVSA DGVVIRGESY
     VDESMITGEA LPIYKKKGST VIAGTVNGTS SIDFKVTRTG KDTQLSQIVK LVQDAQTSRA
     PIQRVADIVA GYFVPAIISL GLITFFGWMF VSHVWSHPPK IFVAEGSGGK VMICLKLCIS
     VIVFACPCAL GLSTPTAVMV GTGVGAQEGI LVKGGAVLEG ATKINHVVFD KTGTLTTGKM
     TVAEARIERQ WHEGRCRLWW LIVGLAEMNS EHPIGKAILS AAKAESGHSE GDGLPGSLGD
     FNAHVGQGIS ALIEPAFNGD RTRYRAVIGN AAFLQSQGVS VPESVEAEDQ PTGSPKPTAG
     ITQIHVAIDQ QFAGTIFLRD TVKSTAVATI AALHRMGLKT SLITGDTRST ALSIASAVGI
     SPEFVHASAS PSDKQSIIAS MQESGDRVAM VGDGINDSPA LATASIGIAL ASGTDVAIEA
     ADIVLMRPDD LLSVPASLSL SRAVFRRIKL NLMWACVYNV IGLPFAMGLF LPFGGFMLPP
     MAAGAAMAAS SVSVVVSSLL LNFWKRPRWM DVEKLEKEAQ LGGVGSRASR KNRWPAALFV
     SGPGSRTGPL GWARRTGAKV WSTVTGRSPR TVDTNDGYVP LQTVEPVV
//
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