ID A0A2B4S0M5_STYPI Unreviewed; 1400 AA.
AC A0A2B4S0M5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cation-transporting P-type ATPase C-terminal domain-containing protein {ECO:0000259|Pfam:PF00689};
GN ORFNames=AWC38_SpisGene12859 {ECO:0000313|EMBL:PFX22599.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX22599.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX22599.1}.
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DR EMBL; LSMT01000234; PFX22599.1; -; Genomic_DNA.
DR EnsemblMetazoa; XM_022939689.1; XP_022795424.1; LOC111334009.
DR OrthoDB; 125283at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 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; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR039720; TMEM94.
DR PANTHER; PTHR13219:SF6; TRANSMEMBRANE PROTEIN 94; 1.
DR PANTHER; PTHR13219; UNCHARACTERIZED; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1167..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1280..1297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1309..1331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1351..1371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1161..1373
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 157566 MW; E985208313D7B39B CRC64;
MEGRGMKMSG YPKDSSAASE KRRSWSWRRR EGLGESEGEI DMDTLEILCE VQEKTNDGSS
GLSSQEALKR LFDAIGDELA TFNAANQCTW RSDIWSTLRD NHHLPISFIS LTFLVFEFLV
MVMSYVFNDK TRSLPLIEGI IVLLLTAINL TLCVREERLR RTEMIRSTQE LLNSCDSCCS
WMPSDYIDPC TPPSLSISLV HAYRDNAMVS VPSNLLVQGD VVVLGPGHTA PARVQQLSTE
FPNRGPSFIL EEGQVYHPVT QSSSTDGNKG TGVQPSQPHP REKFLVTESP FKQNLRTILN
NSLKRPISII GNEMHYITST IIDKKLLFVI LVLSLTVNIL RTIFLKSESG HWSEMILLLQ
GYAILPLLPI SFPIVWICLN LYGTARIKVL FTQLKEKEDP ANEITLKEVL HCFCKNFLGD
PSSLPRTASL LEILGSVTVW CCVDKEGILS LPNPCAEKVF FLKSRKHKTK EDLAGQGKER
KESVCTWESE ISRISSSQDG QESSDEEDDD DVSASLEDSE SVEKNWNTCF KGHREVLNLS
SDPESQFGLR FDDIRWQNHI NSLKPLGLNI LLNSCCKSPV RCLRFADHTG LLSLSYNSVP
LPFFRRCLCL LGKEIGFMER ALQLFSKQKY IFAVQSPINS SLRVPIHSHS FLSISKEKPI
PTMVCLITKE ENSGSLQLLT QGSADVVLDA CTDYWDGSSL CPVTAFERKK VLDFYQRNSM
SAYCVAFSYR PVTEQIPDEK SEDVYLELPS TAQWICSESD EMESASEISE AESENSDKDS
AFNCFELLEA DMEAASLLER VNIAENVESY QRILGGQIFI GVVTLQFQAK KDILPLIEDL
NNAGIRFVYF SAENELRSRV FAERMGLETG WNCHISLREG GHLLEDRGSS ATVSDRNTES
LYDIQDDANV SGQDGDEKHV SWRVTHTEST EKISHKAEAV EMDPLLESQS DGGTLLGSSQ
ISAPEDYWFF ANRAKLPRGI QNIRPHLESV DNVPLLVPLF TDCTPSAVQE MIAIMQDFGE
VVCCVGSSFN SANPAIFIQA DIGIAVEPLF PQLCLKGLPK DFRSGTPQLG HENIREKLRQ
RFSEEQSIED ENELSPLELS AFLNALPCSL AFHRDTNFKF LSLIKEARRI CFGLKNCFSF
MLSCQLVLSA TMLLSACFVL PPPLTGLHLL WLSCLIVPLL SLSLIGSPAD PNLMTMMTGK
NDKNFKDITY TVCFFFSVCF FPSLCICCLL LFPLNLHGFC ISVNKKSTNC HYLLGFRNTT
ELWNGLRESH IQALAMAQDI NAFFLVLIFV FLSSSYVHRL HLLWRKSPFV NRSWIISAVI
ILILQVIYFT LSQVGWSQDA PLVFHLTDVP VPSMIIIFLW PIVALGICEL FKRRYIKERI
RFQKRAKLKF GTKLGMNSPF
//
