ID A0A0L1JF63_ASPNO Unreviewed; 1180 AA.
AC A0A0L1JF63;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:KNG90439.1};
GN ORFNames=ANOM_001053 {ECO:0000313|EMBL:KNG90439.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG90439.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG90439.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG90439.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG90439.1}.
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DR EMBL; JNOM01000014; KNG90439.1; -; Genomic_DNA.
DR RefSeq; XP_015411362.1; XM_015546311.1.
DR AlphaFoldDB; A0A0L1JF63; -.
DR STRING; 1509407.A0A0L1JF63; -.
DR GeneID; 26802857; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000037505};
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 372..394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 447..471
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 477..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 661..682
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1046..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 19..85
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 110..176
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 199..265
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 280..346
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 124507 MW; 6F1B177CD81F1A99 CRC64;
MLGAQVDGAS AARSPAHMAT TTVNVEGMTC GACTSAVEGA FKSVDGVGEV SVSLMMGRAV
VHHDPKVLSP DKVAEIIEDS GFDATVISTD SPPGPPGGTT TVKEKESMVS TTTLAIEGMT
CGACTSAVEG GLKEVAGVKS VNVSLLSERA VVEHHVSTVT PDQLAEIIED RGFGAKVLDT
TTPQSGSSQE TTETTSRLMV TTVSIDGMTC GACTSSIENV FNGVEGLVQF NISLLAERAI
ITHDPVALPS KSIVNMIDDA GFEAAILSSE PQAPVSNAVG RVMLSLHGLR DAPSAGALEE
SLLQKAGISS ASVDIATSRI TVSYDSSVIG VRSIVAAIEA AGYNALLADT DDTNAQLESL
SKTKEVQEWK RSFLFSVSFA VPVFIINMLL PMYLRSLDFG KVQLIPGLYL GDLACLLLTI
PVQFGVGKRF YISSYKSLKH RSPTMDVLVV LGTSAAFFYS VFAMVMALLI APHKRPSTVF
DTSTMLITFV TLGRWLENRA KGQTSAALSR LMSLAPSMTT IYDDPIAAEK MAEEWEASRT
DNGEQKSTSD NERPGPGHQV IPTELIEVGD IVILRPGDKV SADGIVIRGE SYVDESMITG
EALPIHKAKG SAVVAGTVNG TSSVDFKVTR AGKDTQLSQI VKLVQDAQTS RAPIQRMADI
VAGYFVPAII SLGLITFFGW MVMSHLLPHP PKIFLADDNG GKLMVCLKLC ISVIVFACPC
ALGLSTPTAV MVGTGVGAQQ GILVKGGAIL EAATKITHVV FDKTGTLTTG KMSVAEAKIE
RHWTSNEWRR KLWWLIVGLA EMNSEHPIGK AIFLAAKTES GHSDDGGLPG SLGDFDACVG
KGISALVEPA SSAERVRYRV LIGNATFLRS RDISVPESAE DTDSDTTTSK IPAGITRIHV
AIDSQYTGTL LLRDTVKVTA VAAVAALHRM GLSTTLITGD TYATAVSIAN AVGISPEAVH
ASVSPSDKQS IISSLEASGE RVAMVGDGIN DSPALATASI GIALASGTDV AMEAADIVLM
RPDDLLSVPA SLSLSRAVFN RIRLNLVWAC MYNVIGLPFA MGLFLPFGGY MLPPMAAGAA
MAASSISVVV SSLLLKFWRR PRWMDAEKLE KQVEMGNLSF RGSRKSWWEA ALSVSGSSGR
GGPLRWIKGT KVWSILTGKP SGRLDSDEGY VPLQTVEPAV
//
