ID V5FM58_BYSSN Unreviewed; 1128 AA.
AC V5FM58;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=PVAR5_7765 {ECO:0000313|EMBL:GAD99059.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD99059.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD99059.1}.
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DR EMBL; BAUL01000275; GAD99059.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FM58; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR InParanoid; V5FM58; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000018001; 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:0030001; P:metal ion transport; IEA:UniProt.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 3.
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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF85; CALCIUM-TRANSPORTING ATPASE 3; 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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
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 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..923
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 242..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 122945 MW; 37E1F2BBF9160ECB CRC64;
MGGSKKNASR KQGFERHPFL ISVEEMTSLL QTDIEKGLSD TKAQELQQQY GLNRLEGEGG
VSWYSILGKQ ISNAMIMVLI LAMALAYGVS DYVEGGVITA VIVVNVLIGF FQEFQAEKKM
DSLRSLSSPS ATVIRNGQTA TIPSGEVVPG DIVLVKTGDT VPADLRIFEC MNLECDEKIL
TGEAVPVAKE GDFDTTDKDE LSTGVGDRLN MAYSSSTVTK GRGRGIVVFT GMFTEIGKIA
QSMQGKQRKP NRSLSRKKGG NLQPVKGVSL RIWDGIGKFL GLTEGTPLQI KLSKLAYSLF
GCAIILAIIV FGVNKFNVTN EVAIYAISTG IAIIPESLIA VLTITMVVGM TEMRKKRVVV
RQLSALEALG GITNICSDKT GTLTQGQMIT RKAWIPGVGI YSLSNADDAN DPTRGTVSLG
QAPASKKEAE EEQERQRSER DQSRSAAALK FEIPPEKQEK DQRHADGQFD EEENASNGDS
PLPEVVPELE SFLHAAALCN LATVRHDAES NKWKTMGDPT EIALQVFAHR FSFGKKVLET
QKGWKQLAEY PFDSTVKRMS VIYNRDGEDK AVVFTKGAVE RIIDLCTTVG TGEHKQDMTA
EMKEQVLEQM SFLADQGLRV LAVAHKPAPG GESIPRDDVE SDLTLLGLAG LYDPPRLETK
GAVKECTTAG IRVHMLTGDH PSTASAIAKE VGIIPRNTGA MSAEEAASLV KTAAEFDGMT
EEEIDAMPTL PLVIARCAPD TKTRMIAALH RRKRYCAMTG DGVNDAPSLQ ASDVGIAMGM
GGSDVAKSAA DIVLTDDNFA SIVNAIEEGR RMFDNIQKFI LHLLTSNVGE VVLLVVGLAF
QDRQGISVFP LSPLQILWIN MLTSSFPAFG LGREKASASV MHRPPHDTKK GVFTWQIITD
MLVYGLIMGT TTLLTFVIIV YGVGSGQDDL GIDCNGSLDS CNIVFRARAA VFAELTWQIL
ISAWEFKHLR NSIFNLDPLR DRSEDHGLQA FPFFHDVWEN QFLFWAVIIG AISVFPAIYI
PGLNTSVFKH QGISWEWGLS FGGLIIFFLG IEAWKTVKRY TGWFAEGEDY GHGSESHRKI
GHELGLRQGF FTIARTLTGT SGKSLGMDSV KSPSTRKNNG NSQLTEHV
//
