ID A0A5Q4BBT6_9PEZI Unreviewed; 1036 AA.
AC A0A5Q4BBT6;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 Name=Cta3-2 {ECO:0000313|EMBL:TQN64154.1};
GN ORFNames=CSHISOI_11268 {ECO:0000313|EMBL:TQN64154.1};
OS Colletotrichum shisoi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=2078593 {ECO:0000313|EMBL:TQN64154.1, ECO:0000313|Proteomes:UP000326340};
RN [1] {ECO:0000313|EMBL:TQN64154.1, ECO:0000313|Proteomes:UP000326340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2018a {ECO:0000313|EMBL:TQN64154.1,
RC ECO:0000313|Proteomes:UP000326340};
RX PubMed=31527702;
RA Gan P., Tsushima A., Hiroyama R., Narusaka M., Takano Y., Narusaka Y.,
RA Kawaradani M., Damm U., Shirasu K.;
RT "Colletotrichum shisoi sp. nov., an anthracnose pathogen of Perilla
RT frutescens in Japan: molecular phylogenetic, morphological and genomic
RT evidence.";
RL Sci. Rep. 9:13349-13349(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:TQN64154.1}.
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DR EMBL; PUHP01002769; TQN64154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q4BBT6; -.
DR Proteomes; UP000326340; 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; 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:SF12; SODIUM ION P-TYPE ATPASE (EUROFUNG); 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; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000326340};
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 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 788..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..117
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1036
FT /evidence="ECO:0000313|EMBL:TQN64154.1"
SQ SEQUENCE 1036 AA; 112110 MW; 84C0CE438CE0C4FE CRC64;
MGEPAAVRHG EHNTAAAEVN PEQDEPPSIP RPPPIPNPVP QRPAHTVPVT DLGLLWQTNL
ENGLSKAEAS ARLERDGPNR IEGAKGLSVW EIVMRQISNS LTLVLVIVMI LSFAIQDYIE
GGVITAVILL NIVVGFIQDY NAEQTIQSLY ALSAPTCKVI RDGIAETVQA QTLVKGDLVM
IAVGDVVPAD LRLLEGINLS IEEALLTGES LPISKHPEAI FDEDDIPLGD RINMVYSATT
VTRGRARGIV TTTGMETEVG KIAMMLRTTR KRDENASLPV RALTRVKAAF KSILGLEGTP
LQVKLSKFAL LLFGLAILLA IIVFSVSKFD IDDQVLIYGI CVGVAVIPES LIAVLTITMA
VGTKAMASGN VIVRKLSSLE AVGGVTNICS DKTGTLTQGR MITRKVWLAE DTTAIIEGTT
DPYDPTSGKV RWPGSVASSS ASSGASTPTA EKTDDTIHSS SFGAFLKAIA LCNNSSVTDG
KTSTDTESMT TATEVPFAWS AIGEPTEIAL QVFAMRYGKG KNDLISSEKT KMLYEFPFDS
SCKLMSVVYE FPGAPRQVFT KGAVEVMILR LAESEETKAR IIAKADELAS EGLRVLCVAQ
RFLEDTDNAS ERTEAETKLR FLGLAGLYDP PRVETLGAVK QCNTAGISVH MVTGDHIKTA
TAIAHEVGIL RGGEQPTAVM AAGVFDAMSD DEVDALEALP LVIARCSPMT KVRMLEAMHR
RQAYCIMTGD GVNDSPALKK ADVGIAMGKR GSDVSKEAAD MVLTDDNFSS IVTAIKEGRR
LFDNIQKFLL HLLISNISQV ILLLIGLSFK DRSGTSIFPL SPLEILWVNL ITSSFLAIGL
GLEEAQPDIL LRAPHSLRIG VFTFDLIRDK MIYGFFMGSL CLAAFTSVAY GPGAGDLGSF
CNDGWNDTCG VVFRARSTVY ATLSFLLLVT AWEVKHFQRS LFNMNPELWT GPTAVFKTIT
KNRFLFWAVA GGFVMTFPVI YLPVVNRAVF KHDMITWEWG VVIACLVVYI ALIESWKAVK
RHLGLGLTAR IPDQQV
//
