ID A0A1V6S4U6_9EURO Unreviewed; 1252 AA.
AC A0A1V6S4U6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=PENVUL_c008G03754 {ECO:0000313|EMBL:OQE08739.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE08739.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE08739.1}.
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DR EMBL; MDYP01000008; OQE08739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6S4U6; -.
DR STRING; 29845.A0A1V6S4U6; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000191518; 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; 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; 2.
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:UP000191518};
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 428..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 535..552
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 757..779
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1110..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1139..1159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 77..143
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 164..230
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 255..321
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 336..402
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 927..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 132571 MW; F02A76030B61EE15 CRC64;
MSYLIQALGV LSLAPSELIR PSARLSPSLR PRVGGSSSKT PPYAIVSPFL AVFASRFTVE
MVSTNPHAGG AGQPTMATTT IKIDGMTCGA CTSAVESAFK GIAGAHDVSV SLIMGRAAVQ
HDLSLLPPAK IAELIEDCGF DAAVLSTEEQ KNPDSASLPA TRLSVTTLAV EGMTCGACTS
AVESGLNDVS GVNSVDVSLL SERAVVEHDA KIITPEQIAE LIEDRGFEAR VLDTSLMGSK
EQSASVDSEE KSGLLVTTIA IGGMTCGACT SSVEGALGSV DGVIQFNISL LAERAVVVHD
PTRLPASKIP DLIEDAGFDA SIVSSEAQAA ISKKTQQVNL SLHGLRDGVS ATALEANLLQ
QPGVHSASIK MATSRMVIAF DPSMIGVRSV VEVIEAAGYN ALLVDSDDTN AQLQSLSKTK
EIQEWKRSFI IAASFAVPVF LISMILPMYL PAIDFGSFAL LPGLYLGDLI CLALTIPVQF
GIGKRFYVTS FKSLKHRSPT MDVLIMLGTS AAFFYSCFTM IMALCSMEHR RPSTVFDTST
MLITFITLGR WLENRAKGQT SAALSRLMCL TPSMTTIYED PIAAEKLAER WNSKPIPDTP
EQPTMADDMT VNQKCIPTEL IQVGDIVILH PGDKVSADGV VIRGESYVDE SMLSGEALPI
HKKKGSQIVA GTVNGTNSID FKVIRAGKDT QLSQIVKLVQ DAQTSRAPIQ RMADIVAGYF
VPTIIGLGLI TFFGWMVLSH VLPHPPTIFE MAGNGGRVMV CLKLCISVIV FACPCALGLS
TPTAVMVGTG VGAEHGILVK GGAVLEAATK VTHVVFDKTG TLTTGRMSVA HTRIEPQWTM
NDWRRRLWWL IVGLAETGSE HPIGRAIFSA AITESGHAGE DGLPGSMGDF DNCVGRGISA
IVEPTSSGQR IRHHVLLGNA NFLRSKDVPV PADADPDSAE PTEDPEADVP KPGATACGIT
RIHVAIDNRY AGTISLRDTV KATAVAAVAA LHRMGISTSM VTGDTLSTAM SIATAVGIPT
ASIHASVSPS EKRTIVSALQ AEGEYVAMVG DGINDSPALA TASVGIALAS GTDVAVEAAD
IVLMRPDDLL SVPASLSLSR TVFKRIKMNL IWACMYNVIG LPFAMGLFLP FTGFMLPPMA
AGAAMALSSV SVVVSSLLLK FWRRPSWMDV ERLEKELRSG AVSAASAARR RHARKVSWWA
TTTIFEGSPR SLRRRVRNSV SSLWSLVTGK GPMPAGQGDE GYVPLQMVEP PV
//
