ID A0A2A9MR07_9APIC Unreviewed; 400 AA.
AC A0A2A9MR07;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ATPase ASNA1 homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenical pump-driving ATPase homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenite-stimulated ATPase {ECO:0000256|HAMAP-Rule:MF_03112};
GN ORFNames=BESB_010040 {ECO:0000313|EMBL:PFH38662.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH38662.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH38662.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH38662.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFH38662.1}.
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DR EMBL; NWUJ01000001; PFH38662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9MR07; -.
DR STRING; 94643.A0A2A9MR07; -.
DR VEuPathDB; ToxoDB:BESB_010040; -.
DR OrthoDB; 3135429at2759; -.
DR Proteomes; UP000224006; Chromosome i.
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: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; 2.
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 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:UP000224006};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112}.
FT DOMAIN 21..265
FT /note="Anion-transporting ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF02374"
FT DOMAIN 340..386
FT /note="Anion-transporting ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF02374"
FT ACT_SITE 57
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ SEQUENCE 400 AA; 44215 MW; EA1C646ED37B0121 CRC64;
MEDDLELEGS LKELLETPSL RWIFVGGKGG VGKTTTSCAV AAQLAKRRES VLIISTDPAH
NISDAFTQKF SNTPSLVNGF ENLYAMEIDS SYQETLDFQL GSLPGEGNAA FNLTSLLPEM
LQAVPGIDEA LSFAELMQSV QSMKYSVIVF DTAPTGHTLR LLAFPDLLER GLKKLSTFKD
KIQSAIQMLN AVSGKQIQEQ DFAAKIENLK AVTTSVREAF QDPAHTTFVC VCIPEFLSVY
ETERLVQELA KQRIDCSNIV VNQVLFPVGG VEDEDARAPP ASLSYSATEV PGSLVPLEQL
LAPPAPRPAS EGPEEEATRL RRLVHRLQIR LLALEKSHYS RRAMQSRYLQ QIQDLYSFDF
HVVPIPQQPE EVRGIERLLR FGELLTTARP LPLLPVSSSS
//
