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Database: UniProt
Entry: U5DG59_AMBTC
LinkDB: U5DG59_AMBTC
Original site: U5DG59_AMBTC 
ID   U5DG59_AMBTC            Unreviewed;       353 AA.
AC   U5DG59;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Anion-transporting ATPase-like domain-containing protein {ECO:0000259|Pfam:PF02374};
GN   ORFNames=AMTR_s00069p00163470 {ECO:0000313|EMBL:ERN19413.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN19413.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- FUNCTION: ATPase required for the post-translational delivery of tail-
CC       anchored (TA) proteins to the endoplasmic reticulum. Recognizes and
CC       selectively binds the transmembrane domain of TA proteins in the
CC       cytosol. This complex then targets to the endoplasmic reticulum by
CC       membrane-bound receptors, where the tail-anchored protein is released
CC       for insertion. This process is regulated by ATP binding and hydrolysis.
CC       ATP binding drives the homodimer towards the closed dimer state,
CC       facilitating recognition of newly synthesized TA membrane proteins. ATP
CC       hydrolysis is required for insertion. Subsequently, the homodimer
CC       reverts towards the open dimer state, lowering its affinity for the
CC       membrane-bound receptor, and returning it to the cytosol to initiate a
CC       new round of targeting. {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03112}.
CC       Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SIMILARITY: Belongs to the arsA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00011040, ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03112}.
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DR   EMBL; KI392069; ERN19413.1; -; Genomic_DNA.
DR   RefSeq; XP_006857946.1; XM_006857884.2.
DR   AlphaFoldDB; U5DG59; -.
DR   STRING; 13333.U5DG59; -.
DR   EnsemblPlants; ERN19413; ERN19413; AMTR_s00069p00163470.
DR   GeneID; 18447797; -.
DR   Gramene; ERN19413; ERN19413; AMTR_s00069p00163470.
DR   KEGG; atr:18447797; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   HOGENOM; CLU_040761_0_0_1; -.
DR   OMA; MDAPYEF; -.
DR   OrthoDB; 3135429at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0043529; C:GET complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0048767; P:root hair elongation; IEA:EnsemblPlants.
DR   CDD; cd02035; ArsA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_03112; Asna1_Get3; 1.
DR   InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR   InterPro; IPR016300; ATPase_ArsA/GET3.
DR   InterPro; IPR027542; ATPase_ArsA/GET3_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00345; GET3_arsA_TRC40; 1.
DR   PANTHER; PTHR10803; ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE; 1.
DR   PANTHER; PTHR10803:SF3; ATPASE GET3; 1.
DR   Pfam; PF02374; ArsA_ATPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03112};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03112}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112}.
FT   DOMAIN          15..308
FT                   /note="Anion-transporting ATPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02374"
FT   COILED          322..349
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   353 AA;  40005 MW;  8F621B87FA152829 CRC64;
     MESSVRNILE QEELKWVFVG GKGGVGKTTC SSVLSILLSR VRSSVLIIST DPAHNLSDAF
     QQRFTKSPTL VHGFSNLYAM EVDPNVEKDE LPNVEGMDSF ISELTNAIPG IDEAMSFAEM
     LKLVQTMDYS VIVFDTAPTG HTLRLLQFPS TLEKGLAKMM SLKNKFGGLI NQVTRMFGVD
     EEFGEDAILG KLEGMKDVIE QVNRQFRNPD LTTFVCVCIP EFLSLYETER LVQELAKFEI
     DTHNIIINQV LFDEEDVESK LLKARMKMQK KYLDQFYMLY EDFNITLLPL LPEEVCGVEA
     LKKFSAHVLT PYQPSTTPKG TVEELVKRIS TLRLQLKEAE TELERLRKGK DKI
//
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