ID A0A0D2WSB9_CAPO3 Unreviewed; 1020 AA.
AC A0A0D2WSB9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Copper-transporting ATPase, variant {ECO:0000313|EMBL:KJE94313.1};
GN ORFNames=CAOG_004972 {ECO:0000313|EMBL:KJE94313.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94313.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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; KE346367; KJE94313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2WSB9; -.
DR EnsemblProtists; KJE94313; KJE94313; CAOG_004972.
DR Proteomes; UP000008743; 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 CDD; cd02094; P-type_ATPase_Cu-like; 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:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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 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:UP000008743};
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 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 745..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 855..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..59
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 824..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 110429 MW; 750A502B6091AC51 CRC64;
MTCSSCVNTI ESNLMDNPKG VTFATVSLAT NKGRFDYNPD LTGPRDIIAA IEDLGFEASL
VDSKASDETT REMLSHESEV RTWRRRIFIC LVFSLPAMIC MIILTRIPET NAKLMMQPIP
GLSWMNALMI TFAFPLQVLV GRHFYRSAFG ALLHKSANMD VLIVLGTTLA LLYSLFVVAI
AIFSGIMASS DSMASPMLTE PHTFFEAAPM LLTFVCIGRY IENKAKGRTS SALAKLLTLK
ATTATLLTLD PASGHVTSEK AIHPDLVQRG DLLKIVAGER IPVDGTVESG RAFVDESMLT
GESIPVTKNE GSTLFGGTML QSGTLRMRAT NVGQDTALSK IARLVEQAQM SKPPIQQLAD
RLAGRFVPFI VCLSIVTFFV WLILCLCKAV QPTDDMTDVG FALLFAISTL VIACPCALGL
ATPTAVMVGT GVGATLGILI KGGSALELAA KVDSVVFDKT GTLTTGVLSV SRVEMLVPES
QCSQRELLEL AGLAEADSEH SIAVAIVKHA REMTNLPLLS GSASEFEMVP GLGVKCRVTP
SRPIAVSAVK PQQQQQHQQQ FAKTLSANLV LVGNRAWMAQ NGIFVTPTAE DHMAAFERQG
KTAVLVAADE ILVGILVVHD GIRPEAPAAI EALRRMKVEV CMITGDNHRT AKNIAARVGI
TKVWAEALPA SKAELVRRLQ QQGRSVAMVG DGINDSPALA QADVGIAIGH GTDIAIEAAD
IVLVRNNIAD VSVALSLSRI TLRRIWLNFG WALVYNMLCV PIAAGALMPL GFWLHPVYAS
AAMALSSSSV VLSSLMLRTF KRPAFAADDV DYRESDSWDA LEALGPATDD DFDDTDDESG
SPAPKRMERM SWRTLWRDGV LVGVVSLLVF GCFFAIDLPL RVTRWTCGTT WRFPSESNSP
RSYAIRRKVA RRTKNGFSAL KTEDDDENDE AVVVNSDSST KLRRRVVDQQ GGDSDDEDTA
WMNDKGKKNK QSQLQLKSFG KKRSASRSAS ASSLLEKTSD DDDDDDDADE SVLFSVNVRR
//
