ID C5K736_PERM5 Unreviewed; 958 AA.
AC C5K736;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Calcium-transporting ATPase 1, endoplasmic reticulum-type, putative {ECO:0000313|EMBL:EER19371.1};
GN ORFNames=Pmar_PMAR012347 {ECO:0000313|EMBL:EER19371.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER19371.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG671079; EER19371.1; -; Genomic_DNA.
DR RefSeq; XP_002787575.1; XM_002787529.1.
DR AlphaFoldDB; C5K736; -.
DR EnsemblProtists; EER19371; EER19371; Pmar_PMAR012347.
DR GeneID; 9039632; -.
DR InParanoid; C5K736; -.
DR OMA; PLWNNMM; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000007800; 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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF4; CALCIUM-TRANSPORTING ATPASE 1, ENDOPLASMIC RETICULUM-TYPE-RELATED; 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:UP000007800};
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 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..95
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 451..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 105082 MW; 12E50737AD996B8E CRC64;
MKTKTSRAGD KKLDDDTIRR LAYARNYQET LDFFNVTLEK GLSDAQVQAQ AAKFGPNELD
KTEGKSLLAL ILEQFDDLMV KILLVAAFIS FLLAYFDDEN NDEGMLAYVE PLVILLILIA
NAIVGVWQET NAEAALEALK SLQPSYAHVL RNNGTWVTQD STSLVPGDIV EVRVGDKVPA
DIRLCRLRTT TLRVEQSQLT GESVTVSKDV DAVDDDDEGT CEIQGKVNML FSSTAVANGC
GIGVVVGTGM NTEIGDIQKA VTDAAEEDQQ TPLQMRLEEF SELLAKIIFI ICFIVWVINY
KHFFDPVYGS WFRGCIYYFK VAVALAVAAI PEGLPAVITT CLALGTRRMA KRNCIVRRLP
SVQTLGCTTV ICSDKTGTLT TNEMCAVKFA TPSASSAGVL NVYNVDGVSY TPLGQIRPSL
APPESNNTGL AEFAKCAALC NQSRLRYSDD LGDGDVDDTI ESESEEGGNK KPKIRRTGEP
TEAAIRVLAE KIGCPDKELN RRCLQVGGKQ VRSMFMAVCF QSEERSAKDL QAFSHYWSSR
CKLVATLEFS RDRKSMSVLV KENERDENTL YVKGAPEVIL ERCTSIMTPD GSVKPLNKET
KKVILDDYVE KMAGEEALRT LGLAVRKELD PRLAHFKGID VDPENGSLLK DPANFVKVEQ
EMTFLGLVGL MDPPRPECRP AIDSCRDAGI SVIMITGDNK LTAEAIAKDL GIISAGKNAV
SLTGREFDQL SDNEKTAVLR KCMDEQGGVF SRTEPRHKQV IVRILKSLGE VTAMTGDGVN
DAPALKAADI GIAMGISGTE VAKEASDMVL TDDNFSTIVA AVEEGRSIYS NMKAFIRYLI
SSNIGEVASI FFTAALGIPE SLTPVQLLWV NLVTDGPPAT ALGFNPPDLD VMKRPPRRIP
LDLHDWALVL YFSFPVILID EVMKTFGRIV VDKEIEKMHE HQSELMHHAV ESSDDKME
//
