USB1_DANRE
ID USB1_DANRE Reviewed; 276 AA.
AC Q6DEF6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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}; ORFNames=zgc:91896;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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; BC077163; AAH77163.1; -; mRNA.
DR RefSeq; NP_001003460.1; NM_001003460.1.
DR AlphaFoldDB; Q6DEF6; -.
DR SMR; Q6DEF6; -.
DR STRING; 7955.ENSDARP00000002264; -.
DR PaxDb; Q6DEF6; -.
DR Ensembl; ENSDART00000007029; ENSDARP00000002264; ENSDARG00000003841.
DR GeneID; 445066; -.
DR KEGG; dre:445066; -.
DR CTD; 79650; -.
DR ZFIN; ZDB-GENE-040801-197; usb1.
DR eggNOG; KOG3102; Eukaryota.
DR GeneTree; ENSGT00390000004596; -.
DR HOGENOM; CLU_057212_2_0_1; -.
DR InParanoid; Q6DEF6; -.
DR OMA; KTVVLQY; -.
DR OrthoDB; 1507496at2759; -.
DR PhylomeDB; Q6DEF6; -.
DR TreeFam; TF324364; -.
DR PRO; PR:Q6DEF6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000003841; Expressed in camera-type eye and 25 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:ZFIN.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:ZFIN.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; ISS:UniProtKB.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..276
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000274394"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 131..133
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 213
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 213
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 215..221
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 217..221
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
SQ SEQUENCE 276 AA; 31570 MW; C3F1FA60EBC207CA CRC64;
MIVNYSSSSS EEESGSSSSP SGKRQKLDTE TSEALDHGSA QRKVCKSSHL TPRLPLPESV
KEMFRDSEEL WTDKSEEHGG RLRSFQHERG NWATYVFFPY DPEEAFLEVL NKMMAAAEAH
DIPLTVSEEF HLSLSKTVVL RHHWIQPFVQ SIRTSLTHFQ KFYCVAYKLK VYSNAEKTRT
FLGMEVSTGT PHLLELSKIV DETMKEFNLS TFYEDPSFHI SLAWCVGDQT ERLKKACLLE
LQGLIDAHED GPFHARLNCN ELRCKTGNKV FVFPLQ
