USB1_BOVIN
ID USB1_BOVIN Reviewed; 265 AA.
AC Q0II50;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 -!- SUBUNIT: Interacts with PLRG1, CDC5L AND PRPF19.
CC {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; BC122807; AAI22808.1; -; mRNA.
DR RefSeq; NP_001068945.1; NM_001075477.2.
DR AlphaFoldDB; Q0II50; -.
DR SMR; Q0II50; -.
DR STRING; 9913.ENSBTAP00000020923; -.
DR PaxDb; Q0II50; -.
DR Ensembl; ENSBTAT00000020923; ENSBTAP00000020923; ENSBTAG00000015758.
DR GeneID; 510934; -.
DR KEGG; bta:510934; -.
DR CTD; 79650; -.
DR VEuPathDB; HostDB:ENSBTAG00000015758; -.
DR VGNC; VGNC:36703; USB1.
DR eggNOG; KOG3102; Eukaryota.
DR GeneTree; ENSGT00390000004596; -.
DR HOGENOM; CLU_057212_2_0_1; -.
DR InParanoid; Q0II50; -.
DR OMA; KTVVLQY; -.
DR OrthoDB; 1507496at2759; -.
DR TreeFam; TF324364; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015758; Expressed in neutrophil and 104 other tissues.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0034472; P:snRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; ISS:UniProtKB.
DR HAMAP; MF_03040; USB1; 1.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027521; Usb1.
DR PANTHER; PTHR13522; PTHR13522; 1.
DR Pfam; PF09749; HVSL; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..265
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000274390"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 120..122
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 164
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 202
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 202
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 204..210
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 206..210
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
SQ SEQUENCE 265 AA; 29957 MW; B7B2579F0F46CACB CRC64;
MSAAPLVGYS SSGSEDEAEA GARVRPGAEG RSRGQSPLPG QRLPVPDSVL HMFPSTEEGP
VDDSAKHGGR VRTFPHERGN WATHVYIPYE AREEFLDLLD ALLCHAQTYV PRLVRMEAFH
LSLSQSVVLR HHWILPFVQA LKDRVASFHR FCFTTDQVKI YTNQEKTRTF VGLEVTSGHA
HFLDLVAEVD RVMEEFDLST FYQDPSFHIS LAWCVGDARL QMEGPCLQEL QGIVDEFEDS
EMLLRAYAEQ IRCKSGNKFF SMPLK
