SPA5L_XENTR
ID SPA5L_XENTR Reviewed; 593 AA.
AC Q0VA52;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Ribosome biogenesis protein SPATA5L1 {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P32794};
DE AltName: Full=Spermatogenesis-associated protein 5-like protein 1;
GN Name=spata5l1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent chaperone, which plays an essential role in the
CC cytoplasmic maturation steps of pre-60S ribosomal particles by
CC promoting the release of shuttling protein RSL24D1/RLP24 from the pre-
CC ribosomal particles. {ECO:0000250|UniProtKB:Q9BVQ7}.
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; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P32794};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVQ7}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BVQ7}.
CC Nucleus {ECO:0000250|UniProtKB:D4A2B7}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC121246; AAI21247.1; -; mRNA.
DR RefSeq; NP_001072787.1; NM_001079319.1.
DR AlphaFoldDB; Q0VA52; -.
DR SMR; Q0VA52; -.
DR STRING; 8364.ENSXETP00000054098; -.
DR DNASU; 780248; -.
DR GeneID; 780248; -.
DR KEGG; xtr:780248; -.
DR CTD; 79029; -.
DR Xenbase; XB-GENE-967079; spata5l1.
DR InParanoid; Q0VA52; -.
DR OrthoDB; 194195at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
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; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis.
FT CHAIN 1..593
FT /note="Ribosome biogenesis protein SPATA5L1"
FT /id="PRO_0000330588"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 593 AA; 64731 MW; F4115201F34AD2A4 CRC64;
MDTVLKCLPS NPDDHCSQRC RLGPKAMALI GAKVGFPVLV SLQSGSCLCT AWPRRDLCDG
FVQADYMCST SHKPMAVFKD TGICLNQIKS MASTKLRKVS VKVVVRSLDV KRATSEAALL
ETVRDLLRNV FVLNDYVLSV NADSPVVHIE ILDTDPATSN AGLITGKTSI VIKEVITLEW
YKHKLQEAPQ LKVAAMDDTC ASLKEIIHMP LHYPETMHKL GLPCPKGVLL IGPPGVGKTL
LVKAVAREVG AYVIGLSGPA IHGSRPGESE ENLRKIFEKA REAACSGPAL LFIDEVDALC
PKRGHSNSAP ENRVVAQLLT LMDGIDSDNK MVTVAATSRP DAIDPALRRP GRFDREVIIG
TPTHKQRQAI LEMMISNMPT DRDVDAAALA DVTVGYVGAD LTALCRDAAM QAVLQASLDS
LCNLVSRAHF YEAFKRIRPS SARSSIGRVE FKPVHWEHIG GLEDIKHKLR QSIEWPMKYP
EAFSRMGLTP PKGVLLYGPP GCAKTTLVKA VATSCHCSFF SISAADLFSP YVGDSEKTLA
QVSNRCSDKR GLALQPLFSL MKLMPWWGPD QKVEQDLGSR KGSFLFSLMS WMA