ID A0A067NLM6_PLEOS Unreviewed; 948 AA.
AC A0A067NLM6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cu-transporting P-type ATPase {ECO:0000313|EMBL:KDQ28988.1};
GN Name=CTR6 {ECO:0000313|EMBL:KDQ28988.1};
GN ORFNames=PLEOSDRAFT_1037970 {ECO:0000313|EMBL:KDQ28988.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ28988.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL198007; KDQ28988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NLM6; -.
DR STRING; 1137138.A0A067NLM6; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1037970; -.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; A0A067NLM6; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000027073; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 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; 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; 2.
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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
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 192..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 236..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 290..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 495..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 537..565
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 887..909
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 921..943
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 13..78
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 948 AA; 102780 MW; BC4573012B53C46C CRC64;
MTPASDDTPN GPFNVVLSVG GMTCSSCTNS ITQMMSQMPG VTDISVSLIE KSAKAVVDRR
ELAQEIADTI DDCGFESQVV SVHPVRLQEE DEKGTRTVTL KVDGMFCKNC PPKVSAALER
FGSRVEILKP LNDHTDPIIT IRYTPDVPDF TIRHIIAALA SAKSPPFNVY IHHPPSLEQL
SRALQRQEQR RLLFRLVLSI VIAIPTFIIG IVYMTLVKDG DATKEYLMQP IWSGNASRIE
WSLFFLATPV MFYCANLFHT RSIKEIRALW RRGSKVPIWK RFVRFGSMNL LVSAAVTVAY
FSSVGLLATA ARQSPTHSNM GETTTYFDAV VFLTMFLLAG RIIEAYSKAR TADAVSALGS
LRPSEAYLLN RRSDTKERFS IDDDGFGVEK ISAELLDIGD VVRVPHGATP PADGVLVMLP
TRSEGAFDES SLTGEAKLIK KQAGDRVFLG TINKGNMVHV RIDSIGGETM LDRIVNVVRE
GQTKRAPIER IADMVTGYFV PVITLIAILT WIIWLSLGLT GSLPEDYLDI QTGGWPVWSL
GFAIAVFVVA CPCGIGLAAP TALLVGSGLA AKFGILARGG GEAFQEMAQV DLVVFDKTGT
LTQGGEPKVS DAHILPAAET RWSRETILGF ASELEFASSH PLALAIRAYC KAAKARNMTG
EDFDEVSGRG MKAHFPSMKC TAIIGNEAWM EAHEAAIDVG VSQQLGAWRS EAKSVVLMAL
REEGTSEAGF HLAAIFAVAD PLREEAPQVI SWLRTQGIQT WIISGDNATT ATAVAHAAGI
PTGNVIAGVL PHEKAEKVQW LQLHASKRQP STLRKFDAKP RLNQRCIVAM VGDGINDAPA
LTAADIGIAI GSGSDVAISS ASFILLSSNL RSLITLYDLS RNVFNRVLFN FFWAVIYNVA
AIPIAAGVVY PAGHTRLDPV WASLAMALSS VSVVCSSLLL KLYKEPKM
//
