ID A0A1E7EWR1_9STRA Unreviewed; 1059 AA.
AC A0A1E7EWR1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=P-type ATPase {ECO:0000313|EMBL:OEU10287.1};
GN Name=CuATPase_2 {ECO:0000313|EMBL:OEU10287.1};
GN ORFNames=FRACYDRAFT_247584 {ECO:0000313|EMBL:OEU10287.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU10287.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU10287.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU10287.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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; KV784373; OEU10287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7EWR1; -.
DR EnsemblProtists; OEU10287; OEU10287; FRACYDRAFT_247584.
DR KEGG; fcy:FRACYDRAFT_247584; -.
DR InParanoid; A0A1E7EWR1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000095751; 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; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; 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; 1.
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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
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:UP000095751};
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 276..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 319..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 569..593
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 605..627
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 953..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 982..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 49..118
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 141..222
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 115242 MW; 17E002AFB8879730 CRC64;
MMMDSSSLEL SSVVIAVGGH VDDGDDIETG GSNDDVNVSN KNENENHKRI VDFSVGGMTC
SMCSSSVLKL LTEMPGITYA TVTLATNIAH VEYIESPEYE LTAEIIADEI ECIGYDINDI
MKKKTQQQPK KEIAVVSRIL KTVELAVGGM TCSMCSSAVH KALSEMPGVE SVDVSLSTNI
ARIHYYDYND LQNQDEEIDD AEPYNYPHDL SELVEDIGYD VNDVIIVPTS SSSQQQQQQQ
HNFDDEYNNN TEEEVPEDRL ERILRQQDSQ LKKRKIAFLW SATGTIPILT ITMLIPHILN
ENNIVRSFLE QTIQIVGCTL LVQAIIVWLL TTPVQFWCGY SFYKTSYHGI RRGVLGMDVL
VVIGTTSSYI YAFMAMLSND PGYRFFETSA VLITFVLLGK WMNAMAVRQT SKALTQLMKL
QAKTAIKITP LTETKNKSWD PLTDFYSEKV VPIQNVYPGD IVKILRGSNI PADGIVLHGE
LTVDQSMITG ESIPVLKSPG DDVLGGTICS ETGTTMSTTE GDHALTAAAF VRVTGVGADS
ALSQIVQMVQ DAQSRQVPIQ NYADGIASIF VPVVVIFSTV TFIAWYACCM LGIVPSGWYG
EENPVAFSLL FGIASLVISC PCALGLATPT AVMVGTGVGA SHGILMKGGE TLEVASKANV
VVFDKTGTLT RGKPAVTDFT RLASDEFLRG FMNNNNSNNN SLDSSQHVDD YLVWLLGSLE
RNSEHILASA IVNFAEKKID NLLQTKPFAQ PSDFVAITGR GASGIINGDT SVAIGNRSFA
ERENMEISSE VEACMQKMEL DGKTAIIAGI NGTACAVLGI ADEIKEEAPD TIQYLKKLGI
EVWMVTGDSN RTAYAIARQL DLPAEHVIAE ALPNSKVEKV KELQQEGKIV CMVGDGVNDS
PALAEADVGI SMGTGSDIAA EASDMVIVGG NIAKTCTALH LSRAIFRRIQ LNFVFSLVYN
IIGIPLAAGV LFPIFHTRLP PTLAAVAMAL SSVSVVFSSL ALKLYNPPDI LATKSNAFRR
LGPPNILRLG QKRKPKQEYE MVVHKDPYHD LDSFRDEPV
//
