ID C4YB42_CLAL4 Unreviewed; 465 AA.
AC C4YB42;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Copper-transporting ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CLUG_05334 {ECO:0000313|EMBL:EEQ41206.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ41206.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ41206.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ41206.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH408082; EEQ41206.1; -; Genomic_DNA.
DR RefSeq; XP_002614556.1; XM_002614510.1.
DR AlphaFoldDB; C4YB42; -.
DR STRING; 306902.C4YB42; -.
DR GeneID; 8495260; -.
DR KEGG; clu:CLUG_05334; -.
DR VEuPathDB; FungiDB:CLUG_05334; -.
DR HOGENOM; CLU_001771_10_1_1; -.
DR InParanoid; C4YB42; -.
DR OMA; IEIVFAE; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..465
FT /note="Copper-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002946312"
SQ SEQUENCE 465 AA; 50005 MW; 0F578422771FA76A CRC64;
MCIKLSISVV VVACPCALGL AAPTAVMVGT GVGATHGALI KGGDILEKAS KINVILFDKT
GTLTSGEMSV SRSRQICKSN NLKTAQWWHL IGALEVHSEH PVGRAITREA KSNLGLHFED
DTFQALVKNF KVNTGMGVQA QITLDNVTYD VAIGNSRMVV RDYPGARLVL ADMLDTDLKD
SVSSVSHVVI DGEYCGYLEL MDSIKPNARK VLDYLRYAQG YQVGIVTGDN KEAAHMVGQQ
LGVPKGNIFS EVTPINKGEV ISNLREKFGG SSNISIAFVG DGINDAPALV QADIGMAIST
GTDIAIDSAE VVLMSQSSEQ ANDLAGVITA LQVSSATFRK IKWNFVCATV YNMAMLPFAM
GCFLPLNLML PPGAAAAAMA CSSISVVVNS SLLKNWKPPK VDKYSIPEDE IGISDFSLKE
SSRAEFDQIK RGRGLRLKRS IWAVFARKAR QSKNHAQYEM LPNEA
//
