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Database: UniProt
Entry: A0A1Y1YU47_9FUNG
LinkDB: A0A1Y1YU47_9FUNG
Original site: A0A1Y1YU47_9FUNG 
ID   A0A1Y1YU47_9FUNG        Unreviewed;      1133 AA.
AC   A0A1Y1YU47;
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:ORY01095.1};
GN   ORFNames=K493DRAFT_312586 {ECO:0000313|EMBL:ORY01095.1};
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:ORY01095.1, ECO:0000313|Proteomes:UP000193498};
RN   [1] {ECO:0000313|EMBL:ORY01095.1, ECO:0000313|Proteomes:UP000193498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY01095.1,
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:ORY01095.1}.
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DR   EMBL; MCFE01000074; ORY01095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YU47; -.
DR   STRING; 1314790.A0A1Y1YU47; -.
DR   InParanoid; A0A1Y1YU47; -.
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   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: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        128..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        947..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1046..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1079..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..155
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  124721 MW;  2591AF40AEF8F3D7 CRC64;
     MSSENHNGAL SAHTEDDPMS TATHHSRVVF QDLEKPARVN ETFNPVPAAS PQKPESPPPT
     SEKATSKSKN VDITEHLMTI DEVSQKYSTL VNTTKPADST GISQAQAAKG LVEYGPNVLT
     PPKTKHPIIL YLECVAGLFN LLLILAGILQ YVLLAIDPVE NQANIYLGAI LIVVALLNAF
     IEFFQMLKSA AILASFLNMI PAKCFAIREG KLAQMSAAEL IPGDVVFTRM GDKIPADLLI
     FHSSDMKVDN SSLTGESEPQ ARVPFNDQRS PLEASNIAFN GTLVVAGEGY GIVIRTGDNT
     VLGQIAGLTQ GEKKRKSPLS LEIDNFVKTI AGVAAFTAIV FFIVGQVLYG KISFTLNFAI
     GVFVAFVPEG LPATVTMLLT IAAKRMAAAN VLVKDLKGVE TLGAITLLAT DKTGTLTRNQ
     MTVTNVWSGL VMYTAFPSSG NPEIPLTADA PGVDEIMHNA SLNSRAKFDR VDVPIEERQI
     LGDATESGLV RFAAKNLNDF DNIAATYPKV FEIPFNSDNK WAMTIHEKVH ANGDLTLFIK
     GAPERILRLC STILINGEAI PLTQEHKDLY DQTYAYMAGK GHRVLAFAQL LLPRDQYPLG
     TEFTKEKKNY PTSELCFVGL TSLEDPPKHG VREAIGSCRS AGIQVMMVTG DHPLTAEAIG
     RKINIMLSET KEMVAKRTGR PIESIQEHEY SAIVIHGEQI DSLTEQDWDI IFSKNEIIFA
     RTSPKHKLEI VRHAQAMGHI VGVTGDGVND SPALKKADLG IAMNQSGSDV SKEAAAMILL
     DDNFASTVKG VNEGRLIFTN LKKSIQYTIT HSTPEILPNL LYIIVPLPLP LSAILILVID
     LGFEMFAALS YAWEYPETKS GLMKLPPRKP VTVRSVARLR RQLSRRPQSH TDIESGAEFK
     PSKFSLFKHS ITEKFTSQYW VEMFEETDDE VLVDAGVLSW GYLEAGMIEF VGAILSYFLV
     LWFEFNISPS EARNMQKNNC FQKDSDPYTL TNGTVLDATQ QKEALSQAQS IYYLSVMIMQ
     CFNLFACKCR IRLPFGKYMF KNKMSFIGLT IGAAIALLVV YVPPFNVVFG TSYHLSPKWW
     LVSVGFGILL FFYSCVRRII ARKRKPISWN PDIVGLQMYP TVRTVKSTGT TGK
//
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