ENDUD_XENLA
ID ENDUD_XENLA Reviewed; 305 AA.
AC A8E627;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Uridylate-specific endoribonuclease D;
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Protein endoU-D;
DE AltName: Full=XendoU-D;
DE Flags: Precursor;
GN Name=endou-d;
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=Intestine;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at 5' of
CC uridylates and releases a product with a 2',3'-cyclic phosphate at the
CC 3'-end. {ECO:0000250|UniProtKB:P21128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ribonucleotidyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC ribonucleotide-RNA + a 5'-end dephospho-uridine-RNA;
CC Xref=Rhea:RHEA:67792, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17354,
CC Rhea:RHEA-COMP:17356, ChEBI:CHEBI:83064, ChEBI:CHEBI:173117,
CC ChEBI:CHEBI:173224; Evidence={ECO:0000250|UniProtKB:P21128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67793;
CC Evidence={ECO:0000250|UniProtKB:P21128};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR EMBL; BC153814; AAI53815.1; -; mRNA.
DR RefSeq; NP_001104223.1; NM_001110753.1.
DR AlphaFoldDB; A8E627; -.
DR SMR; A8E627; -.
DR GeneID; 100126655; -.
DR KEGG; xla:100126655; -.
DR CTD; 100126655; -.
DR Xenbase; XB-GENE-5929438; endoul2.S.
DR OrthoDB; 823332at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 100126655; Expressed in pancreas and 14 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR CDD; cd21159; XendoU; 1.
DR InterPro; IPR039787; ENDOU.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR018998; EndoU_C.
DR PANTHER; PTHR12439; PTHR12439; 1.
DR Pfam; PF09412; XendoU; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR PROSITE; PS51959; ENDOU; 1.
PE 2: Evidence at transcript level;
KW Endonuclease; Glycoprotein; Hydrolase; Lyase; Manganese; Metal-binding;
KW Nuclease; Reference proteome; RNA-binding; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..305
FT /note="Uridylate-specific endoribonuclease D"
FT /id="PRO_0000394228"
FT DOMAIN 33..305
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 305 AA; 34060 MW; 90013FB66A4AA80A CRC64;
MKVYFVFLCL LPSLISGASI LPEPRKDVRA SASNAEIQSL AEQFYAADTN KAASGDITLN
LQYKASSTQT SSGTDFASQK LFNYVNEAKL FARPTFARLV DLLDNYVHTT GTAESVPTAE
VNEQNAFIDE IFKTSIITKL SDFFISKGYY SSAASFKTDL KEMWFGLYTR TSGPLDSSGF
EHVFHGEIHK GKISGLHNWV RLYLLEKSGQ VNYLSYSSDG VWNGYPDIYA FQLKWSTYLK
TLGSFFIGSS PEFDIAMYTL CYVTRPDSLC SVKMGGSIFQ IQTYTWANST YGNGKRYVAS
SYPNI