ID   FIGL1_CAEBR             Reviewed;         591 AA.
AC   Q60QD1; A8Y106;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Fidgetin-like protein 1;
DE            EC=3.6.4.-;
GN   Name=figl-1; ORFNames=CBG21866;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Has a role in spindle assembly which acts in the progression
CC       through mitosis during embryogenesis. Required for fertility (By
CC       similarity). {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; HE601531; CAP38575.1; -; Genomic_DNA.
DR   RefSeq; XP_002635669.1; XM_002635623.1.
DR   AlphaFoldDB; Q60QD1; -.
DR   SMR; Q60QD1; -.
DR   STRING; 6238.CBG21866; -.
DR   EnsemblMetazoa; CBG21866a.1; CBG21866a.1; WBGene00040545.
DR   GeneID; 8577664; -.
DR   KEGG; cbr:CBG_21866; -.
DR   CTD; 8577664; -.
DR   WormBase; CBG21866a; CBP20245; WBGene00040545; Cbr-figl-1.
DR   eggNOG; KOG0740; Eukaryota.
DR   HOGENOM; CLU_032424_0_0_1; -.
DR   InParanoid; Q60QD1; -.
DR   OMA; AYAAWDK; -.
DR   OrthoDB; 1176820at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblMetazoa.
DR   GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR   GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:EnsemblMetazoa.
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   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Hydrolase; Magnesium;
KW   Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..591
FT                   /note="Fidgetin-like protein 1"
FT                   /id="PRO_0000302728"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT   BINDING         359..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PIW4"
SQ   SEQUENCE   591 AA;  65913 MW;  3096DEA5D298E7FB CRC64;
     MYSPKRVKLN LTNGMRKRPE TEENRGELYP PTAMARNGIS PYFIGKPRRK IVGDHKASEA
     GPPPPFPLKP KRKEPDDDPE SIVIDEDDEE DEPAPQVEKR EPKKTHNRPF FGEKSSLTAT
     ELETAKKEEV VKKKDPFTMR GFDFGSDEKV VKIRDKICDI VDPTGARRSD PAFIQQMHSN
     TLKGIEVATN PKFKQKRTAN NKNRAAIGST LGTIYPNFLT ASGQEPQKSK FQIPLDRQSS
     SQSNHSQPIR KTLPEIPRRC SNSLVKKAMG MDTDGGGKDE RMDGLRSEPT LKHFDENIIS
     LIESEIMSVN NQIGWADVAG LEGAKKALKE IVVLPFQRPD IFTGLRAPPK GVLLFGPPGT
     GKTMIGRCVA SQAQATFFNI SASSLTSKWV GEGEKLVRAL FSVARLKLPS VIFIDEIDSL
     LSARSESEHE SSRRIKTEFL VQLDGVNTAP DERLLVLGAT NRPQELDEAA RRRFQKRLYI
     ALPEPDSRTQ IVENLLRGTR HEITDHNLEK IRRLTDGYSG ADMRQLCTEA AMGPIREIGD
     QIATINKDDI RAVTVADFTE AARVVRPTVD DSQLDAYAAW DKKFGCLPPP L