FIGL1_ARATH
ID FIGL1_ARATH Reviewed; 680 AA.
AC F4JEX5; Q5BPQ2; Q9LSC3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATPase family AAA domain-containing protein FIGL1 {ECO:0000305};
DE AltName: Full=AAA-ATPase FIDGETIN-LIKE 1 {ECO:0000303|PubMed:26161528};
DE EC=3.6.4.- {ECO:0000305};
GN Name=FIGL1 {ECO:0000303|PubMed:26161528};
GN OrderedLocusNames=At3g27120 {ECO:0000312|Araport:AT3G27120};
GN ORFNames=MOJ10.20 {ECO:0000312|EMBL:BAB01094.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-680.
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26161528; DOI=10.1371/journal.pgen.1005369;
RA Girard C., Chelysheva L., Choinard S., Froger N., Macaisne N., Lemhemdi A.,
RA Lehmemdi A., Mazel J., Crismani W., Mercier R.;
RT "AAA-ATPase FIDGETIN-LIKE 1 and helicase FANCM antagonize meiotic
RT crossovers by distinct mechanisms.";
RL PLoS Genet. 11:E1005369-E1005369(2015).
CC -!- FUNCTION: Involved in DNA double-strand break (DBS) repair via
CC homologous recombination (HR). Limits class II meiotic crossover (CO)
CC formation by regulating the invasion step of meiotic HR. May counteract
CC DMC1 and RAD51-mediated inter-homolog strand invasion to limit CO
CC formation. Functions independently of FANCM.
CC {ECO:0000269|PubMed:26161528}.
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; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26161528}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026649; BAB01094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77270.2; -; Genomic_DNA.
DR EMBL; AY924776; AAX23851.1; -; mRNA.
DR RefSeq; NP_001319654.1; NM_001338858.1.
DR AlphaFoldDB; F4JEX5; -.
DR SMR; F4JEX5; -.
DR STRING; 3702.AT3G27120.1; -.
DR PaxDb; F4JEX5; -.
DR PRIDE; F4JEX5; -.
DR ProteomicsDB; 228905; -.
DR EnsemblPlants; AT3G27120.1; AT3G27120.1; AT3G27120.
DR GeneID; 822331; -.
DR Gramene; AT3G27120.1; AT3G27120.1; AT3G27120.
DR KEGG; ath:AT3G27120; -.
DR Araport; AT3G27120; -.
DR TAIR; locus:2092025; AT3G27120.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_10_1; -.
DR InParanoid; F4JEX5; -.
DR OMA; AKLEMDT; -.
DR OrthoDB; 1176820at2759; -.
DR PRO; PR:F4JEX5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JEX5; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..680
FT /note="ATPase family AAA domain-containing protein FIGL1"
FT /id="PRO_0000440041"
FT REGION 214..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 446..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
SQ SEQUENCE 680 AA; 75348 MW; 16A0A5290DD17F42 CRC64;
MCGSVVSDSE REFEFHFWGF GHLGKEEERI MAGKRSSPFS SPLLRPPPEF LNVKEEGETE
TPCWRKEVDE NLKRLQSLLF GADKFLEKSD FSSAQILGLR LLGFLDSRSV TDADRDFIGP
IRREVASKID LALEGLVSDS DRKAFELANT APGAIFGSKG GFDVEKIKQS KYFGFHVSQS
NGKGVKEMEE RHDTDKLIPK APKSMMQAKL TSLYGNSIGK PDNQRKTSVN NQDRASDECV
IVERSHGFGF GTKRPHAETS SLANDGEVKE DGAPNGFVSA KIKLEMDVRQ KRGSTESPSS
CLSPQSDKNA LGRGYGSRSG GLRRGYRSNF VPPVKTNGNN VGNLTSRIGG KTDDALDDST
RTCLEMLCGP DGELPEKLRN LEPRLIEHVS NEIMDRDPNV RWDDIAGLEH AKKCVTEMVI
WPLLRPDIFK GCRSPGKGLL LFGPPGTGKT MIGKAIAGEA KATFFYISAS SLTSKWIGEG
EKLVRALFGV ASCRQPAVIF VDEIDSLLSQ RKSDGEHESS RRLKTQFLIE MEGFDSGSEQ
ILLIGATNRP QELDEAARRR LTKRLYIPLP SSEARAWIIQ NLLKKDGLFT LSDDDMNIIC
NLTEGYSGSD MKNLVKDATM GPLREALKRG IDITNLTKDD MRLVTLQDFK DALQEVRPSV
SQNELGIYEN WNNQFGSLSL
