ID A0A1X2GYC8_9FUNG Unreviewed; 1011 AA.
AC A0A1X2GYC8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
DE Flags: Fragment;
GN ORFNames=DM01DRAFT_1379583 {ECO:0000313|EMBL:ORX63022.1};
OS Hesseltinella vesiculosa.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX63022.1, ECO:0000313|Proteomes:UP000242146};
RN [1] {ECO:0000313|EMBL:ORX63022.1, ECO:0000313|Proteomes:UP000242146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX63022.1,
RC ECO:0000313|Proteomes:UP000242146};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate;
CC Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00035079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate;
CC Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00034989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC Evidence={ECO:0000256|ARBA:ARBA00034989};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IID subfamily. {ECO:0000256|ARBA:ARBA00035017}.
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:ORX63022.1}.
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DR EMBL; MCGT01000001; ORX63022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2GYC8; -.
DR STRING; 101127.A0A1X2GYC8; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000242146; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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; IPR006414; P-type_ATPase_IID.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01523; ATPase-IID_K-Na; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-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; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242146};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..137
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ORX63022.1"
SQ SEQUENCE 1011 AA; 110248 MW; 9BA09607AF2645A2 CRC64;
MTMSGAISFA NNEKKEKQGI TMTRSSTVQS TISDSAKSIR STMMRKMKLV KKKQEVARVE
GPPYHTMTLD TVAQLVKTDM EDGLTEAEAK ERQAQAGYNE LEGEGGVNPF KLLFKQFFNI
LVLILIAAMA VSFAFKDWVE GGVICAIMFL NAGVGFAQEY KAERTMESLR QMASPTVNVI
RGGEQKTIAT RDLVVGDLIV MKSGDVVGAD CRVLHRSFNM DVDEALLTGE SVPVNKVKDV
IEGELVPLGD RVNMGYSSTT LTKGRGRAIV TAIGMDTEIG KIAKRLMDGG DSSRTPLQKS
LDRMAVALLI VAIVSIIIVF AANKFQNIDD QIILYAISTG IAVIPEGLIA VVTLTQAFGV
HAMAKANALV RRMAALEMLG AVTNVCSDKT GTLTQSKMVL TRLWQPDEGF CKVTGLGFSI
DGQVEREQDN AEPLVVANLS TGFQQLVQNA ALCNMSELRK DKEGDSYHGI GDPTEIALQV
FAHKMTMGKP ALMDAGWNVA VEFPFDSTIK RMSVIAQTKD GNNVAYLKGA TERVLSCCVG
VQKKDGIESM TIDQLEALVL PHVETLARGG LRVLSLATRP IKTDGPLDPE TVKREDIEQG
MIFLGLVGIY DPPRIESKGA VEKCHRAGIT VHMLTGDHVA TATAIAREVG ILPGDYGLSP
TDNNAVSVGK LVMPATEFDQ LTESQIDALP DLPLVIARCS PDTKVKMIEA IHRRKRISAM
TGDGVNDSPS LKESDVGIAM GQNGSDVAKQ AADIVLVDDN FATIVSAIEE GRRVFANISR
FVVHMVSVNV AEVTPLLLGL IFADSTGQSV FPLSPIQILF NNVVTSAPPA MALGLEPVHP
RQMQVPPRDN NEGLFSRSNI IDILFYGIMM GLICLADFCY VMFTWGEGNF GTDCNLSYGP
DCYWVYRARG CLFATMTVLL LIHGYTCRDL KHPAYSLRVI FGPQNYYLHA SIAFGLAIMF
VALYVPVLNT QVFRHEGITI EWVVVFISSI VYIILAEGWK YLRRKTFLRH L
//
