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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
 
 
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