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Database: UniProt
Entry: W2S636_9EURO
LinkDB: W2S636_9EURO
Original site: W2S636_9EURO 
ID   W2S636_9EURO            Unreviewed;      1044 AA.
AC   W2S636;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:ETN44085.1};
GN   ORFNames=HMPREF1541_10950 {ECO:0000313|EMBL:ETN44085.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN44085.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN44085.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN44085.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) 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; KB822716; ETN44085.1; -; Genomic_DNA.
DR   RefSeq; XP_008713841.1; XM_008715619.1.
DR   AlphaFoldDB; W2S636; -.
DR   STRING; 1220924.W2S636; -.
DR   GeneID; 19978289; -.
DR   VEuPathDB; FungiDB:HMPREF1541_10950; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_0_0_1; -.
DR   InParanoid; W2S636; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000030752; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
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; 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; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR46594:SF4; 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   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; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
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:UP000030752};
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        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        420..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        641..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        675..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        991..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1016..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          243..310
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          80..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1044 AA;  111325 MW;  8C3B7BC358DCE058 CRC64;
     MSNSAEKPEA ECLGDCCGHA QATPSTAASS ASTLPQYCDQ DEKCDEACIK AAAALECKLA
     CETATKECAG QDCHSDADKL EEKHGHAHAN ADGHPHDHEH DEVGLHGSEA CDNHILAAME
     KYSAYLETAR CICRSVLAST SKIEKGCAGS MLPIAPPMPH GVSSGHLYRK DRSTVGRRHT
     AKTTRTLNTE GHEHRHHGHN HGHDTGKHAC DHDHDQEQDP DTSKERTAAS LSHGDVEKGA
     TTEHFLLNVT GMDCSGCANN LTRAFQNVPG VSNVQVIFIN NTAEIDVDTK ITSFENAIRL
     AQRATGYQLV PFSADSQSID LVLDTRTAKS FQDSLPYGVD SCTKVLKNVF EVYYDPCLIG
     ARELVDRSGG QLAPPRNDRT LDAGHRRLVW VASLTFAAFV FTMPVVVMEW GDFQTIPHRT
     VLIISLVLAT VVQTLAYPEF YKPAISALIY NRVLEMDMLV VISITAAYGY SVVAFGLIFD
     GRDLETSPFF ETSTLLITLV LLGRLLAAWA RKRAVSKVSL RSLQASTAML LDPATDITNE
     IDARLLQYGD TIIIPPHSQI VTDADVSQGT SEVDESMLTG ESLPVLKTVG SSVISGTVNG
     AGSLKAKVTR LPGKNTITDI ANLVEQAQSS KPRIQDLADK VASYFIPVVC TAAVIVFVVW
     LIVGLRGRRD SVDGAIGTAI GYCIAVLAVS CPCALGLAVP MVLVVAGGIA AQGGIIIKTA
     DVTERGHKVT DVVFDKTGTL TEGNLDVVHE EVFAHGDLAP GTDVYSIALA LVKDNKHPVS
     QAVASVLSKR PCHPVNLQDV VSVPGCGIDA AYNNLSLRAG NPRWLEVDAH PKVLALKQQG
     STLLCITLNG QPLAIFGLKS TLRANAPNVI RELVRRKIAV HILSGDIIPA VQAVASTLDI
     SPENAHAECS PALKQEYIRG LMEQGKTTMF IGDGTNDAVA VAQADVGVQI GESASDVTRG
     TADVVLLGGL DGVLGLLDVS KAAYRRIMFN FGWSATYNVL AVLLAGGAFV KIRIPPAFAG
     LGEIVSVLPV VVAALTMPKV KKTM
//
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