ID GET3_MALGO Reviewed; 331 AA.
AC A8Q0M1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 77.
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 {ECO:0000255|HAMAP-Rule:MF_03112}; ORFNames=MGL_2053;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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; AAYY01000006; EDP43840.1; -; Genomic_DNA.
DR RefSeq; XP_001731054.1; XM_001731002.1.
DR AlphaFoldDB; A8Q0M1; -.
DR SMR; A8Q0M1; -.
DR STRING; 425265.A8Q0M1; -.
DR GeneID; 5855361; -.
DR KEGG; mgl:MGL_2053; -.
DR VEuPathDB; FungiDB:MGL_2053; -.
DR InParanoid; A8Q0M1; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 3135429at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
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; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..331
FT /note="ATPase GET3"
FT /id="PRO_0000388213"
FT ACT_SITE 61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 273
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 276
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 331 AA; 36710 MW; 9907AAADC2F24733 CRC64;
MATTTTVDDA QPPTLQNILD QKSLKWIFCG GKGGVGKTTT SCSLAIQLAK VRESVLLIST
DPAHNLSDAF GQKFGREAVK VNGFSNLSAM EIDPTSSMQE MIEQSEQRGG ALAPFMQDLA
FAIPGVDEAM GFAEIMKLVK SMEYSVVVFD TAPTGHTLRF LSFPSVLEKA LTKFSSFGKS
LGPMFQQFQS MMGGGANAQE DMFAKLEGMR QVITEVNSQF KDETKTTFVC VCIAEFLSLY
ETERLIQELT QYGIDTHAIV CNQLLYPPPG SQCEHCRVRK AMQDKYVHEM MDLYAEDFNV
VKIPLLTEEV RGPEKLSSLS EYLMHPYQPP Q
//
