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Database: UniProt
Entry: A0A091G509_9AVES
LinkDB: A0A091G509_9AVES
Original site: A0A091G509_9AVES 
ID   A0A091G509_9AVES        Unreviewed;       900 AA.
AC   A0A091G509;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE   Flags: Fragment;
GN   ORFNames=N303_10121 {ECO:0000313|EMBL:KFO76259.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76259.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO76259.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76259.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC         Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC         Evidence={ECO:0000256|ARBA:ARBA00024272};
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 IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR   EMBL; KL447693; KFO76259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091G509; -.
DR   STRING; 55661.A0A091G509; -.
DR   Proteomes; UP000053760; 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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02085; P-type_ATPase_SPCA; 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; 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; IPR006413; P-type_ATPase_IIA_PMR1.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF23; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 2; 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   Calcium {ECO:0000256|ARBA:ARBA00022568};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
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:ARBA00022568}.
FT   TRANSMEM        263..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        770..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        839..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        870..890
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..95
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO76259.1"
FT   NON_TER         900
FT                   /evidence="ECO:0000313|EMBL:KFO76259.1"
SQ   SEQUENCE   900 AA;  98748 MW;  DEBB1EDE6F74DC6F CRC64;
     EDCELKIIEQ EKEVTVLPPK DACKCHKEDL AKALNVDLQT GLSEFSVLQR RLKHGWNEFS
     VENTEPIWKK YLDQFKNPLI LLLLASALVS VVTKEYEDAA SITMAVLIVV TVAFIQEYRS
     EKSLEELNKL VPPECNCLRE GKLQHLLARE LVPGDIIYLS VGDRVPADLR LIEVTDLLVD
     ESSFTGEAEP CNKTDSVLQE AGDITTLSNV VFMGTLVRYG KGKGVVIGTG ENSQFGEVFK
     MMQAEETPKT PLQKSMDRLG KQLTLFSFGI IGLIMLIGWL QGKRLLSMFT IGVSLAVAAI
     PEGLPIVVTV TLVLGVLRMA KKRVIVKKLP IVETLGCCNV ICSDKTGTLT ANEMTVTRLV
     TSDGFQAEVS GVGYNGEGNV YLLPSKEILK EFSNVSVGKL VEAGCVVNNA IIRKNSVMGQ
     PTEGALIALA MKMELADIKD IYVRKKEIPF SSEQKWMAVK CTLKTQDQED IYFMKGAFEE
     VIRYCTLYNS GGISLSLTPQ QKAFYQQEEK RMGSSGLRVL ALASGPELGK LTFLGLVGII
     DPPRAGVKEA VQVLFESGVS VKMITGDALE TAVAIGQNIG LCNGKLKAMS GEELDQLSDA
     ELSSTVKNVS IFFRTSPKHK VKIIKALQRG GAVVSMTGDG VNDAVALKSA DIGIAMGQAG
     TDVSKEAANM ILVDDDFSTV MNAIEEGKGI FYNIKNFVRF QLSTSISALS LITLSTVLNL
     PNPLNAMQIL WINIIMDGPP AQSLGVEPVD RDTIKQPPRR ITDTILSKSL ILKIFMSAII
     IISGTLFVFW KENPKSGITP RTTTMTFTCF VFFDLFNALT CRSQTKLIFE IGFFRNRMFL
     YSVLGSFLGQ LAVIYVPPLQ KVFQTENLRV LDLLFLTGLA SSVFIVSELV KLCEKRCCRP
//
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