ID A0A2X0MDN6_9BASI Unreviewed; 1176 AA.
AC A0A2X0MDN6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=BZ3500_MvSof-1268-A1-R1_Chr1-1g01094 protein {ECO:0000313|EMBL:SCZ89305.1};
GN ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR1-1G01094
GN {ECO:0000313|EMBL:SCZ89305.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ89305.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMWP01000013; SCZ89305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MDN6; -.
DR STRING; 289078.A0A2X0MDN6; -.
DR Proteomes; UP000249723; Unassembled WGS sequence.
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 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; 2.
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; 1.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; 2.
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:UP000249723};
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 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1051..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..186
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 128092 MW; 381FEC7D7A7ADF26 CRC64;
MTAPNPSGLP TTFDEKASTP ARRLSTSSTA DSELKKEGVH TTGVTFPDTP LKRIPTLPRT
NTLGIRRELT LNRELTQEVK DRAAAGYQDA NEKTKESASQ FIEIVDHHLT VAEVAKKFDT
TFDVKNPANS KGLTSAVAAE RLQTNGPNAL TPPARKSGLR KYLESLSSLF NILLIVAGIL
EYILLGVDFE DNKPNEYIGG ILIAVAFVNA GIDYYQIAKA EAVLAGFLSL VPATCTVVRD
GQISQIPAAD LVLGDCVLIR MGDKTPADVF IFSAVSCSVD NSSLTGEAEP QKRVVVPEGD
KAKRAAEAQN LLFNTTLVVS GEAWGVCIRT GDNTFIGSIA SLTSNQSEKK SPLATEIDRF
VKLLSSVAIF TAILFFIVGI TTVYKGQAAA TVTFAITILV AWIPEGLPAT VTLLLSIAAQ
RMAKRQVLVK DLQGVEVTYR KSGTLGSLTM LATDKTGTLT RNQMTVTNVW TGEVFYTDNA
VHAESSERTL VPQDIGIAET ISICALNSKI KFNRTDVPFS ERELLGDATE TGLTRFSAKH
LASYDDTRAE FPQVFAIPFN STDKAATVVV KKQHATGHLT LYLKGAPERV LARCSTYLGS
DGSLRQVDDA FKAAYTVSYD AMAHKGHRVI GCAQLQLADA DVREGFDFEE NKSMFAHGLT
FVSLVSLEDP PKHGVREAVG TLRRAGIQVM MVTGDHPATA EAIARKINLI SGETKADVAK
RTGRLVDSID EDEYDAVVVH GDDIDGLQGY QWDQIFSHSE IVFARTSPQH KLAIVRHAQD
LGHIVGCTGD GVNDAPALKQ ADLGIAMNIS GSDVSKESSK MILLDDNFAS ITSGVEEGRL
IFQNLKRSIR YTVTHSIPEV IPQILYVLVP VPLPLSALLI LLIDLGFELA VALSFAFDPA
ESADAIMRAA PRKPVSDASI GRLKARALRR IKTRNFDPET NQTIEPTRMS KYIDSAKAPF
TRQFWVDAFE PSDDETLVDR NLLSYSYLEA GMIELIGALT GYFVVFYKSG FTPRDLYLAQ
KSANPKYFLD NSPNYISVSG RVLTASEQVD AWAKATSIMY LSIFLIQCFN IFASKAKFLP
PFGKHVVSNY YNFAGILGGA VVAMFVIYTP PLHAAFGGTY KLSPLYWLIP IAFGCFLLAW
STARVYLTRR ALEKTHVKPL PKLMMHPTMY STGGGK
//
