ID A0A022RQZ4_ERYGU Unreviewed; 528 AA.
AC A0A022RQZ4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=MIMGU_mgv1a004413mg {ECO:0000313|EMBL:EYU42411.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU42411.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU42411.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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|ARBA:ARBA00001836};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007448}.
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DR EMBL; KI630292; EYU42411.1; -; Genomic_DNA.
DR RefSeq; XP_012831291.1; XM_012975837.1.
DR RefSeq; XP_012831292.1; XM_012975838.1.
DR AlphaFoldDB; A0A022RQZ4; -.
DR STRING; 4155.A0A022RQZ4; -.
DR GeneID; 105952302; -.
DR KEGG; egt:105952302; -.
DR eggNOG; KOG0743; Eukaryota.
DR OMA; QDFANGQ; -.
DR OrthoDB; 819832at2759; -.
DR PhylomeDB; A0A022RQZ4; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF110; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..528
FT /note="AAA+ ATPase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001508284"
FT DOMAIN 236..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 528 AA; 59106 MW; 153D6177EA701342 CRC64;
MKEIWTTMAS MMGVWAFCQS LLHTVFPPEL RFAFLKFFHR FFSYFSTYCY YDITEIDGVN
TNELYNAVQL YLSSSASISG SRLSLTRGLN SSSITYGLSN NDRLIDSYRG ASVEWEHIVT
QRQSQTFSWR PLPEEKRGFT LRVRKKNKQL VLSSYLDYVM EKANELRRKN QDRLLYTNSR
GGSLDSRGHP WESVPFKHPS TFDTLAMDPS KKAEIMADLL DFANGESFYQ KTGRAWKRGY
LLYGPPGTGK SSMIAAMANY LGYDIYDLEL TEVNTNSELR KLLMKTSSKS IIVIEDIDCS
INLTNRNKSG GGGGGAAARK NSYDIGSPPG GGGAAGGGEE GGNTITLSGL LNFTDGLWSC
CGSERIFVFT TNHIEKLDPA LLRSGRMDMH INMSYCSFQS LKILLKNYLG FEESGLREGV
LAELEAVVAA AEMTPADISE VLIKNRRDKN KAVEELVEAL KIRAEKNRLK KTNVVVVIGN
DVVVEDEEQE KRALEYPKEN GSHLNCGKCG VKEEENHIEE GEEGKMKE
//
