ID A0A091VLV6_OPIHO Unreviewed; 1222 AA.
AC A0A091VLV6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=N306_13564 {ECO:0000313|EMBL:KFR03398.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR03398.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR03398.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR03398.1};
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; KK734076; KFR03398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VLV6; -.
DR STRING; 30419.A0A091VLV6; -.
DR PhylomeDB; A0A091VLV6; -.
DR Proteomes; UP000053605; 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; 1.
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:UP000053605};
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..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 406..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 929..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 963..982
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1003..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1070..1088
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1100..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1138..1155
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 168..222
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 1199..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 137860 MW; 512CB928E36F391E CRC64;
MEKEEKKFVN KAEEDEMEIY GYDLCRWKLV LVTVGVICSG GFLLLLLYWM PQWRVKATCK
RTTLKDCEVV LLRTTDEFKI WFCAKVRIMP SLGASPLQNP NALVHKVSNG HVVRFCESAT
EECKNDSKIY LPVRYFTHHS VKYFWNDSVQ SFDVLRGLDE SIFCSSIHNE HSTGLTKEMH
DYRKAFYGVN EIAVKVPSIF KLLIKEVLNP FYIFQLFSVV LWIIDEYHYY ALAIVIMSVI
SIVSSLYTIR KQYVMLHDMV AAHSIVRVSV WRGNQEIEEI LSTDLVPGDI VLIPSNGTIM
PCDAVLLSGT CIVNESMLTG ESVPVTKISL PNPSEYPKAM GDEIYSPEVH KRHTLFCGTN
VIQTRFYTGE LVKALVVRTG FSTAKGQLVR SILYPKPTDF KLYRDAYLFL LSLVVVAGIG
FLYTVVNSIL NEVPAHTIII ESLDIITITV PPALPAAMTA GIVYAQRRLK KIGIFCISPQ
RINICGQLNL VCFDKTGTLT EDGLDLWGIQ RVENARFLLP EERACSENLL KSEFVACMAT
CHSLTKIEGV LSGDPLDLKM FEAIGWILEE ATEEETALHN QIMPTVVRPS KQLFPESKQA
TDQEMELFEL STSYEIGIVR QFPFSSVLQR MCVITRVLGE KRMDAYMKGA PEVIASLCKP
ETVPVDFECV LEEYTKQGFR VIALAHRKLE SKLTWHKVQT INRDAVESNM DFMGLIVMQN
KLKQETPAVL EDLHKANIRT VMVTGDNMLT AISVARDCGM ILPQDKVIIA EALPPKDGQA
ARINWHYADT LAKCTSSSPA INSEDIPVKL VHESLEDLQM TRYHFAMNGK SFAVILEHFQ
DLVPKLVLHG TVFARMAPDQ KTQLVEALQN VDYYVGMCGD GANDCGALKR AHGGISLSEL
EASVASPFTS RTPSISCVPK LIREGRAALI TSFCVFKFMA LYSIIQYISV ILLYSILSNL
GDFQFLFIDL AIILVVVFTM SLNPAWKELV ARRPPSGLIS GPLLCSVLSQ IIVCLAFQVF
GFFWVKQQSW YEPWTTESDA CNVLDASNIS SAHHGNETLD EHNIQNYENT TLFFISSFQY
LIVAIVFSKG KPFRQPCYKN FLFVTSVIVL YVFIFFIMLH PVESIDAFFE LVCVPYEWRL
RILIIVILNA IVSVLTEEAV DRYRVCFLSS LFGCREKTPK AKYMHLAQEL LVDPEWPPKP
RTTTEAKVPS QGNGSYQNIT IT
//
