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Database: UniProt
Entry: A0A177DSE0_ALTAL
LinkDB: A0A177DSE0_ALTAL
Original site: A0A177DSE0_ALTAL 
ID   A0A177DSE0_ALTAL        Unreviewed;      1068 AA.
AC   A0A177DSE0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE            EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN   ORFNames=AA0117_g2571 {ECO:0000313|EMBL:RYN81118.1}, CC77DRAFT_1018468
GN   {ECO:0000313|EMBL:OAG22446.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22446.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG22446.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22446.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000291422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   bioRxiv 0:0-0(2019).
RN   [3] {ECO:0000313|EMBL:RYN81118.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN81118.1};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   J. ISSAAS 0:0-0(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}.
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DR   EMBL; KV441474; OAG22446.1; -; Genomic_DNA.
DR   EMBL; PDXD01000003; RYN81118.1; -; Genomic_DNA.
DR   RefSeq; XP_018387867.1; XM_018524630.1.
DR   GeneID; 29110224; -.
DR   KEGG; aalt:CC77DRAFT_1018468; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1018468; -.
DR   OMA; PVQKDCD; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   Proteomes; UP000291422; 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:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02086; P-type_ATPase_Na_ENA; 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; 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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 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; 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   Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT   TRANSMEM        77..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        789..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        826..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        872..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        914..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        965..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        998..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..97
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  116880 MW;  151898B4AC3FE0E6 CRC64;
     MGKKEPSLEG HRSGQANEPL SKPAHALPWK DVVNEIKCNA EDGLTTAEAK SRHEKYGNND
     LGDDGGVSPG KILLRQVANA MTLILIAAMA VSFAIQSWIE GGVVTAIILL NVVIGFVQEF
     NAEKTMDSLR SLSSPTATAA RDGKTVTIPT IEVVPGDLIE LKTGDTVPAD IRIIEALNFE
     TDEALLTGES LPVNKDGDAV FDEETGPGDR LNVAYSSSTV TKGRARGVVF ATGMYTEIGS
     IAMSLRQKGS RVREVKRKPD GKAKPHRYAQ AWSLTAADAV GHFLGVNVGT PLQKKLARLA
     ILLFGVAVVC AIIVLAANSF SNNSEVIIYA VATGLSMIPA SLTVVLTITM AAGTKRMVQR
     HVIVRNLKSL EALGGVTDIC SDKTGTLTQG KMVAKKAWIP AKGTYSVGQS DEPHNPTVGA
     LTFNPKQPRH IDPDVDEKTE TFEELLQDNE HLVDYLKVAS LANLAHVHQT DEGQWNARGD
     PTEIAIQVFA SRFKWNRLEH TGGDSPAWKQ LAEFPFDSDV KKMSVIFEET ASSKKFVFTK
     GAVERVIYSC TRVYNDESEA GVDLDDDYRE EILANMESLA AMGLRVLALA SKEYDGPSPS
     KGEDLDRESI ENGLTFRGLV GLYDPPRPET AGSVRQCQKA GIEVHMLTGD HPGTARAIAI
     EVGIVPSNMS TLPKETTDAM VMTASQFDKL TDDEIDALPL LPLVIARCAP NTKVRMIDAL
     HRRKAFTGMT GDGVNDSPSL KRSDVGIGMG TGSDVAKDAS DIVLTDDNFA SILNAIEEGR
     RMFDNIQKFI LHLLAQNIAQ ACVLLIGLAF KDQSGLSVFP VSPVEVMWII MITSSLPDMG
     LGFEIAAPDI LTRPPQNLKR GVFTLEVIMD MFVYGLWIAA LCLGAFSLVM FGWGDGNLGN
     GCNEGYNDTC DTVFRARATT FACLTWFSVF LAWQMLDMRR SFFAMQPGSK KYFTQWAIDV
     WRNKFLFFSI VFAFVTIFPV LYIPVINDTV FRHKGISWEW GIVFVATFLF FLGIESWKWG
     KRVFFRRRDA KRGVARRGSV DLEQRVFERY LSTAISTDGE DGEKKSSA
//
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