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Database: UniProt
Entry: A0A498IMM4_MALDO
LinkDB: A0A498IMM4_MALDO
Original site: A0A498IMM4_MALDO 
ID   A0A498IMM4_MALDO        Unreviewed;      1078 AA.
AC   A0A498IMM4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=DVH24_032753 {ECO:0000313|EMBL:RXH84470.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH84470.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH84470.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH84470.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RXH84470.1}.
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DR   EMBL; RDQH01000337; RXH84470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498IMM4; -.
DR   STRING; 3750.A0A498IMM4; -.
DR   Proteomes; UP000290289; Chromosome 11.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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   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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
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        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        806..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1002..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1034..1054
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..116
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1078 AA;  118151 MW;  5A84CA89D622BFEB CRC64;
     MTRDHIARRK KKLDPMGKGG QNYGKGESPN PIPIPKADHS FPAWSRDAKE CEDAFRVSRD
     SGLSSEEVDN RRKVYGWNEL EKHEDQSMWK LLLDQLSDTL VRILLAAAII SFVLAWFDGE
     EEKEITAFVE PLVIFLILIV NAIVGIWQES NAEKALEALK EIQSEQAAVI RDGRKVSNLS
     AKELVPGDIV ELRVGDKVPA DMRVLNLVSS TFRVEQGSLT GESEAVSKSV KAVSENSDIQ
     GKKCMVFAGT TVVNGHCVCL VTQIGMRTEI GQVHSQIQEA SQCENDTPLK KKLNEFGEIL
     TMIIGVICAI VWLINVKYFL SWEIVDGLPT NFQFSFEKCT YYFKIAVALA VAAIPEGLPA
     VITTCLALGT RRMAQKNALV RKLPSVETLG CTTVICSDKT GTLTTNQMAV AKLVAIGSRP
     GTLRAFDVEG TTYNPFDGKI QDWPPAGDMD TNVQTIAKIA AVCNDAGVEL SGSHYVANGM
     PTEAALKVLV EKMGVPEVLN TCFSSVGDLL RCSQLWNDID RRIATLEFDR DRKSMSVIVN
     SGSGKNLLFV KGAVENVLER SSSIQLVDGS IVELDQKIRD LILGTLNEMS SSALRCLGFA
     YKDDLPEFAM YNGDEDHPAH QLLLNPSNYS SIENKLVFVG MVGLRDPPRK EVRQAIEDCK
     AAGIRVMVIT GDNKNTAEAI CREIGVFKPS EDISLKSLTG KEFIDHHDQK SYLRQSGGLL
     FSRAEPRHKQ EIVRLLKEDG EVVAMTGDGV NDAPALKLAD IGIAMGIAGT EVAKEASDMV
     LADDNFSTIV AAVGEGRSIY NNMKAFIRYM ISSNIGEVAS IFLTAALGIP EGMIPVQLLW
     VNLVTDGPPA TALGFNPPDK DIMEKPPRRS NESLITPWIL FRYLVIGLYV GTATVGVFII
     WYTHSSFLGI DLSQDGHSLV TYSQLANWGK CPSWEGFSPS NFTAGSQVFT FDTNPCEYFH
     TGKIKASTLS LSVLVAIEMF NSLNALSEDG SLLTMPPWVN PWLLLAMSVS FGLHFLILYI
     PFLANVFSIV PLSLNEWLLV LAAALPVILI DEILKFVGRC TSKLPDSPTI DRSKQKAE
//
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