ID   TSR1_CAEEL              Reviewed;         785 AA.
AC   Q19329;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Pre-rRNA-processing protein TSR1 homolog;
GN   Name=tag-151; ORFNames=F10G7.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Required during maturation of the 40S ribosomal subunit in
CC       the nucleolus. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Bms1-like GTPase family. TSR1 subfamily. {ECO:0000305}.
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DR   EMBL; FO081114; CCD69203.1; -; Genomic_DNA.
DR   PIR; C88131; C88131.
DR   RefSeq; NP_494840.1; NM_062439.6.
DR   AlphaFoldDB; Q19329; -.
DR   SMR; Q19329; -.
DR   BioGRID; 39166; 4.
DR   STRING; 6239.F10G7.1.2; -.
DR   EPD; Q19329; -.
DR   PaxDb; Q19329; -.
DR   PeptideAtlas; Q19329; -.
DR   EnsemblMetazoa; F10G7.1.1; F10G7.1.1; WBGene00006497.
DR   EnsemblMetazoa; F10G7.1.2; F10G7.1.2; WBGene00006497.
DR   GeneID; 173812; -.
DR   KEGG; cel:CELE_F10G7.1; -.
DR   UCSC; F10G7.1.2; c. elegans.
DR   CTD; 173812; -.
DR   WormBase; F10G7.1; CE02624; WBGene00006497; tag-151.
DR   eggNOG; KOG1980; Eukaryota.
DR   GeneTree; ENSGT00940000153195; -.
DR   HOGENOM; CLU_009858_1_0_1; -.
DR   InParanoid; Q19329; -.
DR   OMA; KTPHQQV; -.
DR   OrthoDB; 186926at2759; -.
DR   PhylomeDB; Q19329; -.
DR   PRO; PR:Q19329; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006497; Expressed in larva and 4 other tissues.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR   GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   InterPro; IPR012948; AARP2CN.
DR   InterPro; IPR039761; Bms1/Tsr1.
DR   InterPro; IPR007034; BMS1_TSR1_C.
DR   InterPro; IPR030387; G_Bms1/Tsr1_dom.
DR   PANTHER; PTHR12858; PTHR12858; 1.
DR   Pfam; PF08142; AARP2CN; 1.
DR   Pfam; PF04950; RIBIOP_C; 1.
DR   SMART; SM00785; AARP2CN; 1.
DR   SMART; SM01362; DUF663; 1.
DR   PROSITE; PS51714; G_BMS1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..785
FT                   /note="Pre-rRNA-processing protein TSR1 homolog"
FT                   /id="PRO_0000311279"
FT   DOMAIN          83..243
FT                   /note="Bms1-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..412
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  89221 MW;  1D40D32ED1263A45 CRC64;
     MSTTGHRAGV FKKPSKPHKS WKGKRTKGEI TSENRGREGV KQLTRSAHST HRTISKDARR
     NQLKMARDQK MADAMERRRT SNAPCLVTVV SLGVGARPTE FIKKLATCDE TIIQTTSPST
     IDFAIPRFKS RVSFLTPDKD NVDGVLDAIR ASDVLCFLWP MSAELSEWDE QLLTIIKANG
     LPTIVSVVPG LGSIANHKKK EDVRKGIEFI ISKWSMSNAG VMPADSVTDN LQLLRILNET
     KKKPLTLQAR HSYMLVENLE CSDKTGETCT LVAQGYLRGP EWNANNLVHL PGFGDFQISK
     IESTVDPHPL KAHNKTPEAQ IIAKSDDKRQ NTETEITPDS MDGEQTWPTR EELEEADKEL
     RRVPKGTSSY QAAWILDDED DEDEEDSDED MDDSDNEEVE DDSEEEEPMD DLKSEAGETT
     ASEMMFDDGI DEDINMAEVE KYRKERENAQ WPDEVDTPMD MPARIAFQKY RGLKSFRTST
     WDPKENLPLD YARIFQFANY RNTKKNVMSK IGGNDVDADS VADKKFNGAF ASVFIENVPV
     AVLEAYKDAK NLVLFQLLPH EHKMSVLNMV LKKHPSCTIP ITSDQNQKFI FYVGFRQFEA
     NAVFSSNTPG DKFKLERFMP TEKTFVATVY APITFNPATV LCFRQDDKGR QELVATGSIL
     DSNPDRIVLK RTVLAGHPYK INRRAVVVRY MFFNREDIEW FKPVELYTPS GRRGHIKEAV
     GTHGNMKCRF DQQLNAQDSV MLNLYKRVFP VWNYSIFNRS LNPSRFVERS RVESISLVNE
     DAMEE