ID A0A2J5HHH2_9EURO Unreviewed; 1167 AA.
AC A0A2J5HHH2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Heavy metal translocatin {ECO:0000313|EMBL:PLN76402.1};
GN ORFNames=BDW42DRAFT_188703 {ECO:0000313|EMBL:PLN76402.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN76402.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) 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}.
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DR EMBL; KZ559619; PLN76402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HHH2; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000235023; 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; 3.
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; 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; 4.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
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 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 428..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 459..477
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 639..660
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 680..702
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1037..1060
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 89..155
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 180..246
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 261..327
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1167 AA; 122314 MW; F4109C8C990E4C6B CRC64;
MATTTLNVEG MTCGACTAAI ESAFHSVAGV GEVSVSLIMS RAVVHHDPAV ISPAKVAETV
EDCGFDATVV STDMPTAPNA VDEDGPPMCI TTYAIEGMTC AACTSGVESG VRELPGVESV
SVSLLSERAV VDYDGSRITA EQIADAIEDR GFGAKVLETT APPRSGGRPS QVAEASARLS
VTTVAITGMT CAACTSAVEN QFRDVDGLVQ FNISLLAERA IVTHDATRLS PKQIVDRIED
AGFEAAIVAQ DTQAAGARGL AHVTFNLHGV RDAVDAAALE EALLQRRGIC LAAVDLTTAR
IAVSYDPRAI GVRSLVTTIE ELGYNALLTD THDTNAQLDS LAKTREVHEW KRAFRFALAF
AIPVFLLNMV LPMYLPALDV GRFRLCPGLY LGDLAACLLT IPVQFGVGRR FYVSSFRSLR
HRAPTMDVLV MLGTSAAFFY SVFTMLFALF TAARKRPSTV FDTSTMLLTF VTLGRWLENR
AKGQTSAALS RLMSLAPSMT TVYDDPIAAE KQAEAWHAAS APTPAGEAAA AAGPGRRVIP
TELLEVGDVV ILHPGDKVSA DGVVLRGEGY VDESMITGEP RPIRKAAGSA VIAGTVNGTT
ALDFRVTRAG RDTQLSQIVQ LVQTAQTSRA PIQRMADVVA GYFVPAIVSL GLVTFFGWMF
ISHLLPNPPM IFMAEDNGGR VMVCLKLCIS VIVFACPCAL GLSTPTAVMV GTGVGAQQGI
LVKGGAILEG ATKITHVVFD KTGTLTTGRM TVADARLAPS WQASEDRRRL WWQMVGLAEM
NSEHPIGRAV LAAAQVESGH PGEGALPGSL GDFDACVGQG IAALVEPTTA AEERVRARVL
IGNADFLQSR DAPVPDDEVA AAESPELAGA AAAAAAAPGA KEPAGVTTIH VAIDGQYAGT
LRLRDTVKPT ARGAVAALHR MGLATALVTG DARPTALAIA AAVGIPPEAV HASVAPADKQ
AIIATLEDRG HRVAMVGDGI NDSPALATAS IGIALASGTD VAVEAADIVL MRPDDLLSVP
ASLCLSRAVF NRIRLNLVWA CLYNLIGLPF AMGLFLPFGG VMLPPMAAGA AMAASSISVV
VSSLLLKFWR RPRWMDADTL AYEGPAGPDP RAATKTRWDV LTLAPRRGPA RLVHQAVGRL
RALFLGKPAG GLDTDEGYVP LQTVEPV
//
