ID A0A1Y1YKS1_9FUNG Unreviewed; 1137 AA.
AC A0A1Y1YKS1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=P-type cation exchange, alpha subunit of ATPase {ECO:0000313|EMBL:ORX98582.1};
GN ORFNames=K493DRAFT_313597 {ECO:0000313|EMBL:ORX98582.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX98582.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX98582.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX98582.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX98582.1}.
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DR EMBL; MCFE01000111; ORX98582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YKS1; -.
DR STRING; 1314790.A0A1Y1YKS1; -.
DR InParanoid; A0A1Y1YKS1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000193498; 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; 2.
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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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; 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:UP000193498};
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 132..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1082..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..159
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1137 AA; 125124 MW; 647AA72AEFBCCBFA CRC64;
MSANNSNNNN LSSNPNDDDL ISTATHHSKV VFQDSEKPLR PSDITPVSYV PPSSNEPAAE
AFDEKTPHSK QKKNVDIIEH LMGFEEVCHK YNTSADIAKP GNSQGLTTDQ ATRGLQEHGP
NILTPPKKKS PLFLYLECLA GLFNVLLVVA GILQYVLLAI DPVNNQANIY LGAILIGVAL
VNAFIEFYQL QKSASILASF LNMIPAKCFA IRDGRLNQMA AADLVPGDIV LARMGDKIPA
DLLIFASSDM KVDNSSLTGE SEPQERTKAN THKNPLEASN IAFNGTLVVS GEGYGIVIRT
GDNTVLGQIA GLTQGEKKRK SPLTTEIDNF VKIIASVAFL TAVIFFIVGQ VIYGKIQFTL
NFAIGVFVAW VPEGLPATVT MLLTIAAKRM ADAKVLVKDL KGVETLGAIT LLATDKTGTL
TRNQMTVTNV WSGLVMYTAF PSAGNPEVPL TADAPGVNEI MYISTLNSKA KFDRVDIPVE
ERQILGDATE SGLVRFAAKN LPNFDNAANN FPKVFEIPFN SDNKWALTIH QKRHANGPLT
LYIKGAPERV LRLCSSILIN NEAVPLSGEH QALYDQTYEY MASKGHRVLA FAQLLLPGDQ
YPEDFQFTKE AQNYPTSNLC FVGLASLEDP PKHGVREAIG RCRSAGIQVM MVTGDHPLTA
EAVGRKINLV LSETKIQVAK RTGRPVESVQ EHEYSAIVIH GEQIDSLSDD DWDIIFSKNE
IIFARTSPRH KLEIVKRAQA MGHIVGVTGD GVNDSPALKK ADLGIAMNES GSDVSKEAAA
MILLDDNFAS TVKGVEEGRL IFANLKKSIQ YTVTHSTPEI LPNLLYIIVP LPLPLSAILI
LVIDLGFEIF AALSYAWELP ETKGGLMKLP PRKPVTARSV TRLRNQMARR PVASVDVESG
EESRPSKMTL FKHSVSEKFT SYYWRELFEE TDDEVLVDAG VLSWAYVEAG LIEFAAAMTA
YFVVLYREFG ITPSQARHMQ EGNQYFLNDS PSYTLPSGRV LTNEDQKEAL AQAQSIFYLS
IMICQCFNLF ACKCLIRLPF GKYMFRNKKT FYGMFCGAAL AMMIVYIPPF NIAFGTSHRL
SPLYWLIPLA FGAFLILYST VRRIIIRKRK PINWNPEIAG LQMYPTVRTV KSTGAGK
//
