ID A0A1H4DF20_9FIRM Unreviewed; 928 AA.
AC A0A1H4DF20;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ca2+-transporting ATPase {ECO:0000313|EMBL:SEA71019.1};
GN ORFNames=SAMN04515656_12316 {ECO:0000313|EMBL:SEA71019.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA71019.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA71019.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA71019.1,
RC ECO:0000313|Proteomes:UP000199394};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNRK01000023; SEA71019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4DF20; -.
DR STRING; 81409.SAMN04515656_12316; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000199394; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF506; CATION-TRANSPORTING ATPASE PMA1; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
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 SMART; SM00831; Cation_ATPase_N; 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 731..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..76
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 928 AA; 100521 MW; AA3AB3AB86DE2B38 CRC64;
MQAFRESAKA VLSRLGVDPG RGLTPEEAEE SRAVNGANTF TKAKAKSVWK KIWDATTEPM
IIMLLTAAAI TLGVNFIRLF TGGETEFIEC VGIFAAIFLA VGVTVIMEGR SEKAFDALNK
INEDVQVKVL RGGGITLISQ KELVVGDIME IATGDMISAD ARLLETQELR VDESSLTGES
NPVKKDGNLI FDNPKTPVAE RVNMLYSGCF VTGGSGVAVV TAVGDATEFG SIARELSVEG
DGKTPLQEKL DRLGKLITIL GATAAAIVFT IQCIIFLSSG TFNLDTVSEA FITSIVLIVA
AVPEGLPTIV AVSLSLNIIK MARQNALVKK LIACETIGCI NVICSDKTGT LTENRMTVTD
MVIASHKNNC GRACVSSEDW PEGVCQRRIP ASEINDVHLI ENFILNSTAD IEMDGETVRF
IGNPTECALI TAYEKYNGGE GTDATLPRKT YDAIRKDATV SFVFPFSSET KNMTTIIEVD
QGFMAYSKGS PEKILSQCAF VEVDGVNEPM NADYKAQIEA AMAGFERKAK RVLAFCHRPL
TQEMPITALE ERRASIESDM VFDGFVAIAD PLRGDVYESV ARCRAAGIEL KMLTGDNSLT
AQAIAEELGI LKDGEQVVEA VSLEDLTEDE LKACLPQIRV IARSTPTVKM RVVSALKELG
NVVAVTGDGI NDAPAIKKAD VGIAMGITGT EVSKEASDIV LLDDSFSTIV KAVQWGRGIF
ENFQRFIQFQ LTVNLSSVIV VLTSILLGMA SPFSALQLLW INIIMDGPPA LTLGLEPIRE
DLLGRRPIPR DASIVNGSMM TRIASNAVYV SIIFMLQALF NILGGTPGEQ YTILFTLFVV
MHLFNAFNSR ELTPTSIFKN FFNNRLMLLV FGLTFLLQVI ITQYGGIFYG TIPLSLTMWL
KIIGLGLSVI VVSEVVKAIQ RGFQRKKG
//
