ID   SPA5L_BOVIN             Reviewed;         767 AA.
AC   A7YSY2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-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. Acts together with SPATA5, C1orf109 ortholog and
CC       CINP. {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   -!- SUBUNIT: Associates with pre-60S ribosomal particles. Interacts with
CC       C1orf109 ortholog. {ECO:0000250|UniProtKB:Q9BVQ7}.
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; BC114696; AAI14697.1; -; mRNA.
DR   RefSeq; NP_001099095.1; NM_001105625.1.
DR   AlphaFoldDB; A7YSY2; -.
DR   SMR; A7YSY2; -.
DR   STRING; 9913.ENSBTAP00000024327; -.
DR   PaxDb; A7YSY2; -.
DR   PRIDE; A7YSY2; -.
DR   Ensembl; ENSBTAT00000024327; ENSBTAP00000024327; ENSBTAG00000018279.
DR   GeneID; 533070; -.
DR   KEGG; bta:533070; -.
DR   CTD; 79029; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018279; -.
DR   VGNC; VGNC:35188; SPATA5L1.
DR   eggNOG; KOG0730; Eukaryota.
DR   GeneTree; ENSGT00940000160700; -.
DR   HOGENOM; CLU_000688_12_2_1; -.
DR   InParanoid; A7YSY2; -.
DR   OMA; RAPDLCD; -.
DR   OrthoDB; 194195at2759; -.
DR   TreeFam; TF325792; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000018279; Expressed in tongue muscle and 106 other tissues.
DR   ExpressionAtlas; A7YSY2; baseline and differential.
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; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW   Ribosome biogenesis.
FT   CHAIN           1..767
FT                   /note="Ribosome biogenesis protein SPATA5L1"
FT                   /id="PRO_0000330585"
FT   BINDING         241..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         507..514
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVQ7"
SQ   SEQUENCE   767 AA;  82554 MW;  ECABA36492439D67 CRC64;
     MAPDSGSFPE GPPLKLLPVD TRDRGTQRCR LGPTALRALG AHLGSAVKIS LPDGGSCLCT
     AWPRRDGADG FVQLDPQCTS PGSAVGAPGS GGIINLNRLR LVPCPPLRSL AVWPELREQA
     GASGAPSPAA VLEAVQELLR NRPVSQGYVV AAPPGAPGPV AALHIVSGAP SPNPAGLVTP
     RTHISLSEVP PSEEEPQPEV PLGGLSEAAD SLRELLRLPL RYPRALASLG LEVPRGVLLA
     GPPGVGKTQL VRAVARETGA ELLAVSAPAL QGARPGETEE NVRRIFKRAR ELASRRPTLL
     FLDEVDALCP RRGGPHQAPE SRVVAQVLTL LDGIGEDREV VVVGSTNRPD ALDPALRRPG
     RFDREVVIGT PTLRQRKAIL QVITSKMPIS GQVDLNLLAE MTVGYVGADL TALCREAAMQ
     ALLHSEKNQD NPTIDETDFL EAFKKIQPSS FRSVIGVTDI KPVGWEQIGG LEDVKLKLKQ
     SIEWPLKFPR EFVRMGLTQP KGVLLYGPPG CAKTTLVRAL ATSCRCSFVS VSGADLFSPF
     VGDSEKILSQ VFRQARANTP AIVFLDEIDS ILGSRSISRT ECNVQDRVLS VLLNELDGVG
     LKTIERRGSK SDQHGKCKQL EKNEELEFQE IFNSNVIVVA ATNRPDVLDD ALLRPGRLDK
     IIYIPPPDEK GRLSILKVCT KNTPMGPDVS LEKVAAETCF FSGADLGNLC KEAALLALQE
     NGLEVTTVKQ EHFLESLKTV KPSLSHKDLT LYKNLFQKKE FSILEDI