FIGL1_XENLA
ID FIGL1_XENLA Reviewed; 655 AA.
AC Q6DDU8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Fidgetin-like protein 1;
DE EC=3.6.4.-;
GN Name=fignl1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in DNA double-strand break (DBS) repair via
CC homologous recombination (HR). May regulate osteoblast proliferation
CC and differentiation (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Hexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8BPY9}.
CC -!- DOMAIN: The N-terminus is necessary for its recruitment to DNA damage
CC sites. {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC077410; AAH77410.1; -; mRNA.
DR RefSeq; NP_001086763.1; NM_001093294.1.
DR AlphaFoldDB; Q6DDU8; -.
DR SMR; Q6DDU8; -.
DR GeneID; 446598; -.
DR KEGG; xla:446598; -.
DR CTD; 446598; -.
DR Xenbase; XB-GENE-1000363; fignl1.L.
DR OrthoDB; 1176820at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 446598; Expressed in oocyte and 19 other tissues.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; 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; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..655
FT /note="Fidgetin-like protein 1"
FT /id="PRO_0000302726"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 425..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
SQ SEQUENCE 655 AA; 72152 MW; 93C4912332FB24B8 CRC64;
MQIPETSSVH QNEWQRDVFV LSSGTCLPQQ KAEVYRAHLA QIQYAWANSE ISEASAVHLF
KKYAEKYSAI LDSDKLEIGL NNYADSILTM AKCQRNESDK WQSSLTTNNV LKLKSVQEMA
EAGRRAQLSL LNSTDASVRV GNEIGTSGYS TVLAHNVLRN PSHAVPHAAS SDCQIPEGSS
NFLQNSKVSA FTKANTSSNT LINNSIPINT SLMQRNEVKA PTTFSTQSGP NVFSSTTSVY
SGKRKACYAL GDESTDIQPK PLVQRQLASK EATGDSDFKT AKEQLWVDQQ KKHSNQPQRN
PGPLYGGGKK SLGAARSRGL HGKFIPPLPR QEDVEDSNRK VYGQGNSEMN STSDEHLKNI
EPKMIELIMS EIMDHGPPLN WDDIAGLEFA KTTIKEIVVW PMLRPDIFTG LRGPPKGILL
FGPPGTGKTL IGKCIACQSG ATFFSISASS LTSKWVGEGE KMVRALFTVA RCHQPAVIFI
DEIDSLLSQR GEGEHESSRR IKTEFLVQLD GATTSSEDRI LVVGATNRPQ EIDEAARRRL
VKRLYIPLPE ASARKQIVVS LMSKEHCSLT EQEVEAIVLQ ADGFSGADMT QLCREAALGP
IRSIQLMDIS TITAEQVRPI AYIDFQSAFL VVRPSVSQKD LELYENWNKT FGCGR