ID A0A091HZA6_CALAN Unreviewed; 1224 AA.
AC A0A091HZA6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=N300_13317 {ECO:0000313|EMBL:KFP00483.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP00483.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP00483.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP00483.1};
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 = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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DR EMBL; KL217930; KFP00483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HZA6; -.
DR STRING; 9244.A0A091HZA6; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 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; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF12; POLYAMINE-TRANSPORTING ATPASE 13A3; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 207..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 407..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 930..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 964..983
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1072..1090
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1102..1120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1140..1158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 13..146
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 163..222
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
SQ SEQUENCE 1224 AA; 137937 MW; 3C287176DC6CBFB4 CRC64;
MEKEEKKFVN KAEEDEMEIY GYDLCRWKLV LVTIGVICSG GFLLLLLYWM PQWRVKATCK
RTTLKDCEVV LLRTTDEFKI WFCAKVRIMP SLGASPLQNP NPIGHKLSNG HAVHFCESDA
EENKNDLKNY LPIRYFTHHS VKYFWNDTVQ SFDVVRGLDE STFCSSIHNE HSTGLTKGMH
DYRKAFYGVN EIAVKVPSIF KLLIKEVLNP FYIFQLFSVI LWITDEYHYY ALAIVIMSVI
SIVSSLYTIR KQYVMLHDMV AAHSIVRVSV CRGGDQEIEE ILSTDLVPGD IMLIPSNGTI
MPCDAVLLSG TCIVNESMLT GESVPVTKIN LPNPSEYPKA MGDEIYSPEV HRRHTLFCGT
NVIQTRFYTG ELVKALVVRT GFSTAKGQLV RSILYPKPTD FKLYRDAYLF LLSLVVVAGI
GFLYTVVNSI LNEVPAHTII IESLDIITIT VPPALPAAMT AGIVYAQRRL KKIGIFCISP
QRINICGQLN LVCFDKTGTL TEDGLDLWGI QRVENARFLL PEESACSESL LKSEFVACMA
TCHSLTKIEG VLSGDPLDLK MFEAIGWILE EATEEETALH NRIMPTVVRP SKQLFPESKQ
EANEEMELFE LSTGYEIGIV RQFPFSSVLQ RMCVIARVLG EKRMDAYMKG APEVIASLCK
QETVPVDFEC VLEDYTKQGF RVIALAHRKL ESKLTWHKVQ TINRDAIESN MDFMGLIIMQ
NKLKQETPAV LEDLHKANIR TVMVTGDNML TAISVARDCG MILPQDKVII AEALPPKDGQ
AARINWHYAD TLAKCTSSSP AINSEDIPVK LVHESLEDLQ MTKYHFAMNG KSFAVILEHF
QDLVPKLVLH GTVFARMAPD QKTQLVEALQ NVDYYVGMCG DGANDCGALK RAHGGISLSE
LEASVASPFT SRTPSISCVP KLIREGRAAL ITSFCVFKFM ALYSIIQYIS VTLLYSILSN
LGDFQFLFID LAIILVVVFT MSLNPAWKEL VAQRPPSGLI SGPLLCSVLS QIIICLAFQT
FGFFWVKQQS WYEPWTTESD ACNVLDNTNT SSAHHGNETL HDEHYIKNYE NTTLFFISSF
QYLIVAIVFS KGKPFRQPCY KNFLFVTSVI ILYVFIFFIM LHPVESIDTF LELVCVPYEW
RLRILIIVVL NAIVSVLMEE AEDRCGVCFL SSLFGYREKT PKAKYMHLAQ ELLVDPEWPP
KPRTTTEAKV PSQGNGSYQI ITVT
//
