ID A0A137PF90_CONC2 Unreviewed; 1371 AA.
AC A0A137PF90;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Copper-translocating P-t {ECO:0000313|EMBL:KXN73663.1};
GN ORFNames=CONCODRAFT_77240 {ECO:0000313|EMBL:KXN73663.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN73663.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN73663.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN73663.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KQ964433; KXN73663.1; -; Genomic_DNA.
DR STRING; 796925.A0A137PF90; -.
DR EnsemblFungi; KXN73663; KXN73663; CONCODRAFT_77240.
DR OMA; GGKFMVC; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000070444; 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; 5.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 6.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 4.
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; 5.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 6.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 4.
DR PROSITE; PS50846; HMA_2; 6.
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:UP000070444};
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 574..592
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 643..667
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 679..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 830..849
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 869..891
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1203..1225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 6..73
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 146..211
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 216..282
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 294..360
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 408..474
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 482..548
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1324..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 149079 MW; E05626B3ED8BFA48 CRC64;
MTQIVTYLEL KVIGMTCQSC VKAINKSLSK LDHLTSYSVD LETEIAKVTY PSSVINFEAD
IITCIEDCGF DVYQLVNYKI PELIQVNTNL IKENYKEEVV YSVEFNEATR YLSIWKSLSL
SNENLLQKLE ELELQPITVK QNNTANYIQL NVEGMTCQSC VRSIQNALKP LEGLVDCEVS
LENNKVSAVI LPSLSKSLVA ETIENAGFDV IQDSSNIVTL SVEGMTCQSC VKSIQSSLKK
QSGILNSTVS LAENQAQVIY SPSEISAKTI ATTIEDCGFD VSIISDLLNA PSNNELVLSV
EGMTCQSCVK AIKSASQKVN GIISIDVSLA DDRATIVYDS KIVSSSDLVN MVEDCGFDAK
IISNNSSSST LVPNSVRQRS TSIAKSNSKQ VESDLTITVN NFESGEIITT NISVHGMTCS
SCTGLVEGEL KDRQGIESVV VSLMSERATI KHYPNVISAQ QLADIVTGLG YPSEVQKPSS
KNTLTINLYG LVDGQMALKV ENELGSLNGV QSVEIDPTGQ ILIVEITPGE IGPRQIISAL
KEFGIDGLIE QKSANSQLES LNKTREILQW KRQLKLSLLF TVPIFIISKV FMNIPYTRSF
LEYQILKIPI DTWIQCILTI PVQFGVGWQF YTNSYKALSH RSANMDVLVA IGTSAAFFFS
VFTMLWAMFL GDSTHPECFF ETSATLITFI VLGRYLENKA KGKTSSALSQ LISLTPSSCV
LVTKGDDGNL IEEKIPSELV IPGEKIPVDG IVREGSSTID ESMVTGEPIP VSKKIGDNVI
GGTVNGMGML VIEADKIGEE ATLSKIVKLV EDAQTSKAPI QYFADLVAKY FVPVVVALAI
ATFTLWIILG SFFADHVPDN VMLKHKGAFI TALTFAISTI VISCPCALGL ATPTAIMTGT
GVGAQLGILI KGGVPLEAAK SLTKVLFDKT GTLTLGKLQV TEIRMMVDFE IRSKYQLTQD
NFTKIIAAAE SSSEHPLGRA IVVHAKENLK LDVESVKMDE FLATAGRGVH CRVTCEPTNQ
SMNIRIGNGK FLQENSISLP ESFTQTKEQY ESEGNTVVMV AIDNFFAGFV ALSDTLRPES
LMTVRALKKM GLSVAMVTGD QQLTAEAIAK QCEIEEIYAG VSPQGKSKTV ERMQRDGHSV
CFIGDGINDS PALAKSTVGI SMGGGTDIAI EAASVVLMKT DLMDVVGAIH LSKRIFNRIR
LNFLLASIYN IIAIPLAMGL FAWIGFTMHP IVAAAAMGLS GLSVVLSSLA LKLYRRPYFS
METNSFYYQP YTEDNLPSFL LSPFNAYVSF TQKLSSKIRG RPSTVGYANI NESESQVQIT
VTSPGALESG NATSSRNKLW SKSSTQQDDE IELINHSFNQ FTIDDSDSES D
//