ID A0A4T0W188_9PEZI Unreviewed; 1137 AA.
AC A0A4T0W188;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=CH35J_006407 {ECO:0000313|EMBL:TIC99004.1};
OS Colletotrichum higginsianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=80884 {ECO:0000313|EMBL:TIC99004.1, ECO:0000313|Proteomes:UP000305883};
RN [1] {ECO:0000313|EMBL:TIC99004.1, ECO:0000313|Proteomes:UP000305883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TIC99004.1,
RC ECO:0000313|Proteomes:UP000305883};
RX PubMed=31028389; DOI=.1093/gbe/evz087;
RA Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA Shirasu K.;
RT "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT Pathogenic Fungus Colletotrichum higginsianum.";
RL Genome Biol. Evol. 11:1487-1500(2019).
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:TIC99004.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWPZ01000004; TIC99004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0W188; -.
DR Proteomes; UP000305883; 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; 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; 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; 1.
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:UP000305883};
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 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 998..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..82
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 401..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1137 AA; 125193 MW; 941069BE22E08B36 CRC64;
MSGDYPKHPF LLSVQETAQA LGVDPDKGLS SQQVQQAQEK YPANEFEVGE SVPWYTILSK
QLFNAMVLVL VFAMILSFAI NDYIEGGVLA FVIVANVTIG FWQEYRAEKQ MDALRTLSAP
SANVLRDGKT KVIPNAEVVP GDIILLKMGD TVPADMRIFE AMNLSCDEQS LTGEAQPVDK
ISEANITVPG SDKLATEEGE VGIGDRLNIA YATTIVRKGR GRGIVVATGM QTEVGKIAAS
TQKKVRKPGR SMNYKKYGKR QPVVGLTKRV YDAVGKFLGL TEGTPLQRKL AALAYVLFGC
AIILAIIVFA AHKFDVTGEV IIYAVSLGIA IIPESLVAVL TITMVVAVTV MRKSNVVVRD
LSALEALGGV TNICSDKTGT LTQGAMIVRK AWLPFSHTYT VRDSQSPNDP TKGRVTYSET
KEQEDKIEEA PKRDYDQERS AAVLKFDVPE EKLQNKQPAK EPEAENEAEM TPRLKAFLLS
SALCNLATVR YDEEEAKWQT TGEPTEIALQ IFSHRFKLGK KSLEGLGWKQ LAEFPFDSSI
KRMSVIYDLP ETSEASDIWG PGNSLVFTKG AVERVLDLCS HIGFGDDKIE LTEELKEEVL
NQMNNLASQG QRVLAVGYRD WNGRFTTKQA DVSQEKENAL RTEVEQGLTL LGLAGIYDPP
RRETKPSIAE CSSAGIKVHM LTGDHPETAK AIAKEVGIIP KNLGVLPDAL AKSIVQKATD
FDKMTDEEID AMPELPLVIA RCAPDTKTRM IDALRRRNAF MAMTGDGVND APSLARADVG
IAMGSGSDVA KSASKIVLTD DKFNSIVSAI RQGRRMFDNI QKFILHLLSS NVGEVILLCC
GLAFRDGADL SVFPISPLEI LWINMVTSSF PAFGLGREQA AADVMRKPPQ NKKRGVFTNQ
IIVDMIVYGI IMGALTLATF IIVVYGANGG ALGQECNKTF TEACRPVFRA RAAVFAELTW
IILISAWEFK NLRRSMFRLN PDSESKFPFF KDIYDNKFLF WAVIIGALSV FPVIYIPTLN
TTLFKHIGIT WEWGIVVGFT LLYVVGVEAW KFVKRTFNLL DDHQVVKGAF SQGGEDEGRD
FKKTMTFSSF KSWHSFGRKD TGESTGRRSR SQHRTNTNLS GDTRTGEGSP NNSNEKV
//
