ID K3VLD5_FUSPC Unreviewed; 1070 AA.
AC K3VLD5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=FPSE_04413 {ECO:0000313|EMBL:EKJ75394.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ75394.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ75394.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ75394.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EKJ75394.1}.
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DR EMBL; AFNW01000088; EKJ75394.1; -; Genomic_DNA.
DR RefSeq; XP_009255806.1; XM_009257531.1.
DR AlphaFoldDB; K3VLD5; -.
DR EnsemblFungi; EKJ75394; EKJ75394; FPSE_04413.
DR GeneID; 20363031; -.
DR KEGG; fpu:FPSE_04413; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_0_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000007978; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0000139; C:Golgi membrane; IEA:EnsemblFungi.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:EnsemblFungi.
DR GO; GO:0140613; F:P-type manganese transporter activity; IEA:EnsemblFungi.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0030026; P:intracellular manganese ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
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; 2.
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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 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:UP000007978};
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 929..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 963..979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1000..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 61..135
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 116109 MW; 7D6348A3972151F5 CRC64;
MQLPWGGRDG PGNDTLLPTS NIPSITGHIG DNTTSKDGDH SHRPRHHART TSSDARNVAD
HFSYMTPSEA AANLRTSLTL GLTPNEALTR LGDYGPNEIP HEPPEPLWLR FIKQFQEPLI
LLLLVSAGTS LLLGNTDDAI SITVAVTIVV SVGFVQEYRS EKSIEALNHL VPNHAHLVRG
QGKVSPTGKT PTWPPRVDDE DSSLTPGSVT PVGDILDATS SKVMASQLVP GDLVLFTTGD
RIPADIRVTK AADLTIDASN LTGETEPVRV TAEARSRGFG GYGLDKNELP RPASLAPAEH
GDSHGDGIHN IAYMGTLIKS GHGQGIVFAT GGHTHFGTIA TSVSGTESPR SPLQLSMDDL
GSQLSKASFV VIGLISIVGW LQGKKLLEIF TISISLAVAA IPEGLPIIVT VTLALGVHRM
ARHNAIVRRM PKVETLGSVN VVCTDKTGTL TTNHMTTTRM WYFGAQEPVE VESDNEDVGS
SMESNQATLR VLRIGNIAND ARLAQKYTEH GQAATAVLSS TLGRDQVSTY TRWVGQPTDV
AMLDLLDRFK EHDVRTSIGP RVSETPFSSE RKWMGVTIGS ETKSDKEYAY MKGSIEKVLA
ACDTYLEKDG REIVLDSSRR QEALQAAEAM AVKGLRVLAF ASGHVSRTAR NKSTARSTPG
FDRSESPSSH APEDIYKHLT FAGLVGMRDP PRPGVGRSIR RLMRGGVKVI MITGDAETTA
LAIGKQLGMT IAAPIGHTGS QNSVKPVLRG DEVDRMSEAD LAQAMEHTTI FARTNPDHKL
KIIRALQSRG DIVAMTGDGV NDAPALKKAD IGISMGRHGT DVAKEAADMI LTDDDFSTIL
RAIEEGKGIF NNIQNFLTFQ LSTSAASLAL VFICTCFGFK SPLNAMQILW INIIMDGPPA
QSLGVEKVDP DVMTKPPRRR GDPVLTRKLI QRVLTSAAII TVGTMLIYRR EMVADGQVTR
RDTTMTFTCF VFFDMFNALS CRSESKSILR GEVGVFSNNL FNWAVALSIA GQLLVIYFPW
LQETFQTEAL GFFDLVRLVF LCSTVFWADE LRKYLKYGKR RFGNGYSQAV
//
