RRP44_CAEEL
ID RRP44_CAEEL Reviewed; 961 AA.
AC Q17632;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable exosome complex exonuclease RRP44;
DE EC=3.1.13.-;
DE AltName: Full=Protein DIS3 homolog;
DE AltName: Full=Ribosomal RNA-processing protein 44;
GN Name=dis-3; ORFNames=C04G2.6;
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: Putative catalytic component of the RNA exosome complex which
CC has 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. dis-3 has both 3'-5'
CC exonuclease and endonuclease activities (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA exosome complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; Z70718; CAA94677.2; -; Genomic_DNA.
DR PIR; T18925; T18925.
DR RefSeq; NP_501835.2; NM_069434.4.
DR AlphaFoldDB; Q17632; -.
DR SMR; Q17632; -.
DR BioGRID; 42978; 6.
DR STRING; 6239.C04G2.6; -.
DR EPD; Q17632; -.
DR PaxDb; Q17632; -.
DR PeptideAtlas; Q17632; -.
DR PRIDE; Q17632; -.
DR EnsemblMetazoa; C04G2.6.1; C04G2.6.1; WBGene00001001.
DR GeneID; 177875; -.
DR KEGG; cel:CELE_C04G2.6; -.
DR UCSC; C04G2.6; c. elegans.
DR CTD; 177875; -.
DR WormBase; C04G2.6; CE42607; WBGene00001001; dis-3.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; Q17632; -.
DR OMA; VVKRNWR; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q17632; -.
DR Reactome; R-CEL-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q17632; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001001; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR InterPro; IPR033770; RRP44_S1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR Pfam; PF17215; Rrp44_S1; 1.
DR SMART; SM00670; PINc; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Exosome; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..961
FT /note="Probable exosome complex exonuclease RRP44"
FT /id="PRO_0000166420"
FT DOMAIN 73..188
FT /note="PINc"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 108786 MW; D23F2FA6ADFF73A9 CRC64;
MDLNVKQSGI HSVALHTTYF QNRSGKVYKR AEERYLRNDL SCGLAQCGTC KDFGTNPLLK
IENPVRNAKV GRHALIVDST SLIRFYDLFD SSLLRDLIVT QTVWEGVKAK AVPAYKKMNS
LCYEDAKDRF HVFMNEFHCE TFSESSKFED LSRGEELLLS TALYLKTHWQ KHNVAPVVLV
FDEDSKKRME NHYQHVMYLK EYIQNLEDPG KQALLDQMAA YESSGNGNEK QIFDEYLSHD
RIMEGIASGT IKRGNFSVSR ENYREATVII DDQLTSWFIT GNNCNRAVNG DTVAVQLLPE
DQWTAPEKKI RLRDVEEYVK TADDMGNEDE ENDDENDEPK AKKSKKMTVS TAKVVGIIKR
NWREYCGMLL PSTVKGARRH LFCPAERLIP RIRIETEQAE TLSQQRIVVA IDHWPRDSKY
PLGHYVRSIG EMGSRETENE VLLLEHDIPH APFSESVLDC LPREEWEPDL TENRGPLPRV
DLRDLTICSV DPLGCTDIDD ALHCKQIGED LFEVGVHIAD VTHFVRPGTA IDDEAALRGT
TVYLCDRRID MLPCLLSSNL CSLRGEEERY AFSCIWTMTS SADIQSVKYH KSLIKSKAAL
TYEKAQEIID DPKEQNDVAL GLRGLMKLSK VLNARRTGNG ALTLASSEVR FDMDWESRTP
KKVMEKQHLD THSMVEEFML LANISVAEKI LEEYPDCALL RRHPVPLKES YKPLVEAARH
RGFEIIVESG KGLADSLNRC VDKKNPMLNR LLRMLTTRCM TQAVYFSAGT VPVPQYQHFG
LACAIYTHFT SPIRRYADVI VHRLLAAAIG ADDIQSGLLN QARCTKICTN INYRHKQAQY
AGRASVQLNV VRYFKGKVET CEGFVMGVRN NGIQVFVPKY GLESIIVLQT SAASGTTIDV
EEMSVKVNGD VVIKELEPVT VRISVNEKNQ QRPRVELQLI KPAIPGLSVD FDLSSSEGLG
L