USB1_XENLA
ID USB1_XENLA Reviewed; 250 AA.
AC Q7ZYI9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=U6 snRNA phosphodiesterase 1 {ECO:0000250|UniProtKB:Q9BQ65};
DE AltName: Full=3'-5' RNA exonuclease USB1 {ECO:0000250|UniProtKB:Q9BQ65};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:Q9BQ65};
GN Name=usb1 {ECO:0000255|HAMAP-Rule:MF_03040};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' RNA exonuclease that trims the 3' end of oligo(U) and
CC oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule,
CC leading to the formation of a mature U6 snRNA 3' end-terminated with a
CC 2',3'-cyclic phosphate. Participates in the U6 snRNA 3' end processing
CC that prevents U6 snRNA degradation. In addition also removes uridines
CC from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1.
CC {ECO:0000250|UniProtKB:Q9BQ65}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC uridine-RNA + uridine; Xref=Rhea:RHEA:46052, Rhea:RHEA-COMP:17384,
CC Rhea:RHEA-COMP:17385, ChEBI:CHEBI:16704, ChEBI:CHEBI:85643,
CC ChEBI:CHEBI:85644; Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053;
CC Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end uridylyl-adenosine-RNA = a 3'-end 2',3'-cyclophospho-
CC uridine-RNA + adenosine; Xref=Rhea:RHEA:67896, Rhea:RHEA-COMP:17385,
CC Rhea:RHEA-COMP:17386, ChEBI:CHEBI:16335, ChEBI:CHEBI:85644,
CC ChEBI:CHEBI:176518; Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67897;
CC Evidence={ECO:0000250|UniProtKB:Q9BQ65};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03040}.
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DR EMBL; BC043765; AAH43765.1; -; mRNA.
DR RefSeq; NP_001079479.1; NM_001086010.1.
DR AlphaFoldDB; Q7ZYI9; -.
DR SMR; Q7ZYI9; -.
DR DNASU; 379166; -.
DR GeneID; 379166; -.
DR KEGG; xla:379166; -.
DR CTD; 379166; -.
DR Xenbase; XB-GENE-6251623; usb1.L.
DR OrthoDB; 1507496at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 379166; Expressed in testis and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:1990838; F:poly(U)-specific exoribonuclease activity, producing 3' uridine cyclic phosphate ends; ISS:UniProtKB.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03040; USB1; 1.
DR InterPro; IPR027521; Usb1.
DR PANTHER; PTHR13522; PTHR13522; 1.
DR Pfam; PF09749; HVSL; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..250
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000274395"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 105..107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 149
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 187
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 187
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 189..195
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 191..195
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
SQ SEQUENCE 250 AA; 28999 MW; D5BA18A38B98D37F CRC64;
MALVSYSSSE EDEGETSEPP GRRLPPLPPP TTVLRMFQDM EGDEDLDENT KHEGRIRSFK
HERGNWATYV YIPFQPQEEF LDLLDELVSV AAENGVLLTK MSEFHISQSQ TVVLRHHWIN
PFVESLKDKL HCMYRFLCIA ERIKVYTNQE KTRTFLGLEV SVGMEHLLEV VSEVDRSLQE
FNLQTFYQEP SFHVSLAWCV GDKYEKLKGS CLLELQKVID RFEDSDTLTR FNAEEIRCKA
GNKTFCIPLL
