ID A0A2C5YWT9_9HYPO Unreviewed; 1418 AA.
AC A0A2C5YWT9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN ORFNames=CDD80_4838 {ECO:0000313|EMBL:PHH72000.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH72000.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH72000.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH72000.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000256|ARBA:ARBA00003954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001857};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000256|ARBA:ARBA00006886}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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:PHH72000.1}.
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DR EMBL; NJES01000457; PHH72000.1; -; Genomic_DNA.
DR STRING; 2004952.A0A2C5YWT9; -.
DR OrthoDB; 1381139at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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 HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_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; 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; IPR008220; HAT_MetX-like.
DR InterPro; IPR006415; P-type_ATPase_IIIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01524; ATPase-IIIB_Mg; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR32268:SF16; SERINE O-SUCCINYLTRANSFERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 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; PR01836; MGATPASE.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 880..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..121
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 967..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 154601 MW; 1DD86E1B85FA4E4C CRC64;
MSVMSVMSSF LARILPGHTK MRSNWPDTAS WARPPSARDE SPEAILYAFA SAPMDHALAH
LMTDVDGLTE AEAAMRRGIK GLNVLPTQKP PSWFRTLIGA IPNPFNILLI FLAIINAVVP
DRNWASVIVL LVMVFISIVV RFWQEYRSSL AVFRLQSSIT NLLKVRRPLY SGGSEKTSRE
RDEVTVTEKN LVPGDVVWLT PGCVVPADCL ILEASFLRIS QSSWTGENEP VAKIANPSVD
KEASLFDLPN IVFMGTSVVS GNGVALVLRT GGDVLVANMA NELTKKRVPN AFQIGIRHVS
YMLIGFMCVM VPIVLCISGK TTGDWNAAAL FSVSVAVGLV PEMLPAIVNA NLARGAFLLS
GLKAIVKRLD SIQNLGAMTV LCSDKVDGLF LLRVHIEADS WSVQTGTLTK DEITLCRYID
LSGNDNEAVL KLASVDAKVQ GSNGNNIDQA ILQHRLADGT TISIAQYEKL AAIPFTFERR
RSSCIVRGAT GEKLLISKGA FDEVLSLCST VRQGGVTVTL DADRKRQLAE RAEALNRQGY
RVLLVAEKQL SAVDVEDEEG LNGLESRMTL EGILTFIDPP KDDAAMSIAS LKMLGVEVKV
LTGDSLPVAL NVCQGLGLLG PDDETVDDVQ ATTGPQLAAL EGTDEFDDRV RCCSVFAKLT
PQQKALVVGS LRKAGHCVGM LGDGINDCMA LRRADVGISV DSGASVAKEC ADLILTEKGL
GIMVASVKTG RITHGNTIKY IKMVASSNFG NVFSVLAASA WLPFQPMLGL QLLAQNLLYD
ISQIAIPWDR VDDDYVLTPK QWNTWDLLRF VVVLGPTSSV IDILTYLIGY FYYGVRTADS
PDVGMFQAHW FLQGLLTQTL IVHLLRTAKI PFVQSRSTKP LAFSTAGIMA IGFAIPWIPP
FRRALGMGMP APSLAITIPT LSLVRFITSF SLGLVSKDDA LAFPCLDALD SRSARLRESV
SWTRSAAAIP SPSPSSSSPQ IGSEPSYTSG ATQMFHSETP LRLDWGGLLP EFDIAYETWG
RLNPDRSNAI LLHTGLSASS HAASTPENGQ AGWWERFIGP GAPLDTDRFF VICTNVLGGC
YGSTGPSSLD PANGERYATR FPILTIEDMV RAQFRLLDHL DIPVLYASVG ASMGGMQALS
AGLVNPHRVS RIATISGCAR SHPYSIALRH AQRQVLMMDP NWNRGFYYGR VPPHAGMKLA
REIATVTYRS GPEWEMRFGR RRAEPGRVPA LCPDFLVETY LDHAGEKWCL EYDANSLLYV
SKAMDLFDLS LENQTLASTR RNLTQPPQPS PCGLTLPETP YKEQQQHQQQ HQQQQHQQQH
NPQSQPQPQP QPTLGLPPQD LISGLRPLSS TPTLVMGVAT DILFPAWQQR EIADALRLAG
NRTVEYVELD EGKSLFGHDT FLLDIENVGG ALGRFLRG
//
