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
//