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Database: UniProt
Entry: A0A0F5YCZ3_9CYAN
LinkDB: A0A0F5YCZ3_9CYAN
Original site: A0A0F5YCZ3_9CYAN 
ID   A0A0F5YCZ3_9CYAN        Unreviewed;       727 AA.
AC   A0A0F5YCZ3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 38.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:KKD36779.1};
GN   ORFNames=WN50_17925 {ECO:0000313|EMBL:KKD36779.1};
OS   Limnoraphis robusta CS-951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX   NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD36779.1, ECO:0000313|Proteomes:UP000033607};
RN   [1] {ECO:0000313|EMBL:KKD36779.1, ECO:0000313|Proteomes:UP000033607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-951 {ECO:0000313|EMBL:KKD36779.1,
RC   ECO:0000313|Proteomes:UP000033607};
RA   Willis A., Parks M., Burford M.A.;
RT   "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT   robusta strain CS-951.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
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:KKD36779.1}.
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DR   EMBL; LATL02000165; KKD36779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5YCZ3; -.
DR   PATRIC; fig|1637645.4.peg.3281; -.
DR   OrthoDB; 438550at2; -.
DR   Proteomes; UP000033607; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07550; P-type_ATPase_HM; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM/ZINC-TRANSPORTING ATPASE HMA4-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF19991; HMA_2; 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   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   727 AA;  79014 MW;  4DAD154E0231FCA0 CRC64;
     MESERFIEPA PYIVHAVPGR VRFRVYRLSS DEYYAQNLEQ VLQSEPGVIQ VRINRSAASV
     AIHYQHLDFP DIEIYSRLST LIQQAGISIT VEDISDSPQP EPNEPDNEGE WSSLLAPTGA
     TLLALLSSST RLAWLRPLAW GSLALVTFPV AQRAFYSLFV KQKLNIDCLD LLALSLGGAQ
     GKLVTPALVL TLHELGDVIR EQTARSTEHQ TADLLDTIGR FAWVERNGEK QSIPSDQVQP
     GEIVFVYPGE QIPVDGVVTE GKAVVDQQQL TGESMPIVAE NGTFVYASTL VRSGNLHIKA
     ERIGKKTRAA ASLELLQKAP VHDTRMANYA ANLADRLITP SLILAGIVFA ATRDPARAAS
     ILTLDFVTGI RVSIPTAFLG ALNHTTRHGI LVRSGRTLEQ LAELDTIVFD KTGTLTQGNI
     SVVNVKTISG RMSAKEVIKY AAATEQRITH PVAEAIVRYA QEQVIEIPPR VDWNYEVGLG
     IRAEIEGQKV LVGSGRFLTQ EGISLEGLDQ SETAENSAWM SLIYVACNGK LQGAIEYADP
     LRPESLDLIE ELQNRYGMEI HLLTGDSRQR ADLVADELNI PSKRVHAEAF PEQKAKIVRD
     LHRSGRTVAF VGDGLNDSVA LAYADVSVSF EDGSDVARET ADVVLMNNDI SSLLQAIAIA
     KQTRTLIDQN TLLVIGPNLV ALGLASAVGL NPLIATVIHN GSAIAAGLNS LRPLVQHQLE
     RGSSTES
//
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