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Database: UniProt
Entry: A0A177E3K5_ALTAL
LinkDB: A0A177E3K5_ALTAL
Original site: A0A177E3K5_ALTAL 
ID   A0A177E3K5_ALTAL        Unreviewed;      1054 AA.
AC   A0A177E3K5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE            EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN   ORFNames=AA0117_g12531 {ECO:0000313|EMBL:RYN64372.1},
GN   CC77DRAFT_1015658 {ECO:0000313|EMBL:OAG26348.1};
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:OAG26348.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG26348.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG26348.1,
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:RYN64372.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN64372.1};
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; KV441469; OAG26348.1; -; Genomic_DNA.
DR   EMBL; PDXD01000075; RYN64372.1; -; Genomic_DNA.
DR   RefSeq; XP_018391769.1; XM_018524069.1.
DR   GeneID; 29109663; -.
DR   KEGG; aalt:CC77DRAFT_1015658; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1015658; -.
DR   OMA; NGQEYSM; -.
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; 3.
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; 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   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        53..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        853..880
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        900..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        951..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        984..1003
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..78
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1054 AA;  115344 MW;  50D28F00EEBDB044 CRC64;
     MSLPAHSLTL EQVKTELKTE EWHGLDDAEA KRRVDEYGSN ELGEAESVSP VKILIAQVAN
     AMTLVLIMAM AVSFGIKSWI EGGVVAFVIG LNIVVGFFQE WSAEKTMDSL RSLSSPTARL
     IRSGQQVTVP SAEVVPGDVI EVKVGDTIPA DIRVFDAVNF ETDEALLTGE SLPVRKQEDA
     TFDEKTGPGD RLNVAYSSSS VTKGRAKGIV FATGAYTEIG AIAAQLRETK SKVRPVKRKE
     NGKAKPHRYL EAYTLTTTDA IGRFLGLNVG TPLQKKLSKL AVLLFFIAVV CAIIVLAANE
     FSSRQEVIIY AVATGLSMIP ASLVVVLTIT MAAGTKSMVT RNVIVRNLKS LEALGGVTDI
     CSDKTGTLTQ GKMIARGAWV PGVGTYTIED SNSPQDPTAG HVRFGSAAPS KMDLKAGGDA
     CGERLSVDKL EAHNVEGFGE FLKVASLANL AAVKQNNEGA WEAHGDPTEI AIQVFASRFG
     MNRSHLVKGD SATWEDLVEL PFDSDVKRMS VIMKHASGNY AFTKGAVERV IQSCTTYLAD
     GKEQSQPVTE EFRNEILAHM ASLAGLGLRV LALASKKYPA DVEKGAEVER ASVESELVFR
     GLIGLYDPPR PESAVAVRQC HEAGIEVHML TGDHPDTARA IAIEVGILPS AERYKKISTD
     VAKNLVMTAS EFDDLSDDQV DELPVLPLVV ARCAPSTKVR MIEALHRRDR FCAMTGDGVN
     DSPSLKRADV GIAMGQAGSD VAKEASDIVL TDDNFASILA AIEEGRRIFD NIQKFVLHVL
     AENVAQAGTL LVGLAFKDRT GLSVFPLAPV QVVWIIMATS GLPDMGLGFE RAVPDILQRP
     PQSLKTGIFT LEFLVDMVVY GLWITLLCLA SFVLVVFGFG DGELGTGCNE TYSEQCELVF
     RARACTFACL TWFALFLAWE MIDMRRSFFR MQPGSKRYFT QWMFDVWRNQ FLFWAIMVGF
     VLLFPLIYIP TLNTVVFKHA PIDWEWGIVF IETGIFFAGI EFWKWCKRVY FRRKGAKHGT
     GKVDKNMEIE DRVFGRYYSR DSSTTGNESV QEKA
//
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