ID   ENDUB_DANRE             Reviewed;         282 AA.
AC   Q503V9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Uridylate-specific endoribonuclease B {ECO:0000305};
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE   AltName: Full=Protein endoU-B;
GN   Name=endoub; ORFNames=zgc:110053;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) 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. The UU and GU sites are more efficiently cleaved than CU and AU
CC       sites. {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   -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR   EMBL; BC095160; AAH95160.1; -; mRNA.
DR   RefSeq; NP_001018398.1; NM_001020562.1.
DR   AlphaFoldDB; Q503V9; -.
DR   SMR; Q503V9; -.
DR   PaxDb; Q503V9; -.
DR   GeneID; 553584; -.
DR   KEGG; dre:553584; -.
DR   CTD; 553584; -.
DR   ZFIN; ZDB-GENE-050522-373; endou2.
DR   eggNOG; KOG2849; Eukaryota.
DR   InParanoid; Q503V9; -.
DR   OrthoDB; 823332at2759; -.
DR   PhylomeDB; Q503V9; -.
DR   PRO; PR:Q503V9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; Hydrolase; Lyase; Manganese; Metal-binding; Nuclease;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..282
FT                   /note="Uridylate-specific endoribonuclease B"
FT                   /id="PRO_0000394224"
FT   DOMAIN          4..278
FT                   /note="EndoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
SQ   SEQUENCE   282 AA;  32286 MW;  18B84BB6195C7757 CRC64;
     MTEGDRELSA LIQELWDNDT NRLRPGIDYR ISLQGKAGDL AGVPDDSDGA GMPLFSFVDE
     NIFKKETFLA FISLLDNYES DTGEPEIVTP EEEMENHRFL DSVIKTPTMK IAHKYLVEKR
     LSPEDTTGFK QQLYKIWFEL YARKGSSKPD SSGFEHVFVG ETRGGHTVIG FHNWIQLYLQ
     EKLGHIDYKG YSVNANSPQP DENKHMLALQ FSWKNGIKPK GSIFIGVSPE FEFSLYTLCF
     LMSPNERVKV SFNLYDVEIV CHHYNQKHIG TTYPVPVKYL NV