GET3_ASPCL
ID GET3_ASPCL Reviewed; 340 AA.
AC A1CKN5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ATPase get3 {ECO:0000255|HAMAP-Rule:MF_03112};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenical pump-driving ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenite-stimulated ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Golgi to ER traffic protein 3 {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Guided entry of tail-anchored proteins 3 {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=get3; ORFNames=ACLA_039240;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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:0000255|HAMAP-Rule:MF_03112}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}.
CC Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; DS027056; EAW09709.1; -; Genomic_DNA.
DR RefSeq; XP_001271135.1; XM_001271134.1.
DR AlphaFoldDB; A1CKN5; -.
DR SMR; A1CKN5; -.
DR STRING; 5057.CADACLAP00003886; -.
DR EnsemblFungi; EAW09709; EAW09709; ACLA_039240.
DR GeneID; 4703578; -.
DR KEGG; act:ACLA_039240; -.
DR VEuPathDB; FungiDB:ACLA_039240; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0043529; C:GET complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR GO; GO:0010038; P:response to metal ion; IEA:EnsemblFungi.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR10803; PTHR10803; 1.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..340
FT /note="ATPase get3"
FT /id="PRO_0000388187"
FT ACT_SITE 63
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ SEQUENCE 340 AA; 37620 MW; FE0E69740BEA7F8F CRC64;
MSSAAVVHHD DLMEPTLQSI INQKTLRWIF VGGKGGVGKT TTSCSLAIQL AKARKSVLLI
STDPAHNLSD AFGQKFGKEA RLVDGYSNLS AMEIDPNGSI QDLLASGEAQ GEDPMAGLGM
GNMMQDLAFS IPGVDEAMSF AEVLKQVKSL SYEVIVFDTA PTGHTLRFLQ FPTVLEKALA
KLSQLSSQFG PMLNSILGAR GGLPGGQNID ELLQKMESLR ETISEVNTQF KNPDMTTFVC
VCIAEFLSLY ETERMIQELT SYSIDTHAIV VNQLLFPKKG SECEQCNARR KMQQKYLEQI
EELYEDFNVV RMPLLVEEVR GKEKLEKFSE MLVHPYVPPQ
