USIP1_CAEEL
ID USIP1_CAEEL Reviewed; 662 AA.
AC Q23652;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=U6 snRNA-specific terminal uridylyltransferase {ECO:0000305};
DE Short=TUTase {ECO:0000303|PubMed:25753661};
DE EC=2.7.7.52 {ECO:0000269|PubMed:25753661};
DE AltName: Full=PAP-associated domain-containing protein {ECO:0000305};
DE AltName: Full=U6 snRNA-interacting protein {ECO:0000303|PubMed:25753661};
GN Name=usip-1 {ECO:0000303|PubMed:25753661, ECO:0000312|WormBase:ZK863.4};
GN ORFNames=ZK863.4 {ECO:0000312|EMBL:CAB01456.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN A COMPLEX WITH SART-3 AND
RP U6 SNRNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 183-ASP--ASP-185.
RX PubMed=25753661; DOI=10.1093/nar/gkv196;
RA Rueegger S., Miki T.S., Hess D., Grosshans H.;
RT "The ribonucleotidyl transferase USIP-1 acts with SART3 to promote U6 snRNA
RT recycling.";
RL Nucleic Acids Res. 43:3344-3357(2015).
CC -!- FUNCTION: Acts as a specific terminal uridylyltransferase for U6 snRNA.
CC Responsible for the addition of UTP at the 3' end of U6 snRNA which
CC stabilizes U6 snRNA (PubMed:25753661). Does not have activity towards
CC modified uridine containing 3'-monophosphorylation or 2'-O-methylation
CC (PubMed:25753661). {ECO:0000269|PubMed:25753661}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000269|PubMed:25753661};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC Note=Binds 1 divalent cation per subunit.
CC {ECO:0000250|UniProtKB:Q9H6E5};
CC -!- SUBUNIT: Forms a complex composed of sart-3, terminal
CC uridylyltransferase usip-1 and U6 snRNA; complex formation is mediated
CC by usip-1 and sart-3 binding to U6 snRNA.
CC {ECO:0000269|PubMed:25753661}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000305|PubMed:25753661}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:25753661}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CAB01456.1; -; Genomic_DNA.
DR PIR; T28064; T28064.
DR RefSeq; NP_506056.1; NM_073655.6.
DR AlphaFoldDB; Q23652; -.
DR DIP; DIP-24847N; -.
DR STRING; 6239.ZK863.4.1; -.
DR EPD; Q23652; -.
DR PaxDb; Q23652; -.
DR PeptideAtlas; Q23652; -.
DR EnsemblMetazoa; ZK863.4.1; ZK863.4.1; WBGene00014124.
DR EnsemblMetazoa; ZK863.4.2; ZK863.4.2; WBGene00014124.
DR GeneID; 179670; -.
DR KEGG; cel:CELE_ZK863.4; -.
DR UCSC; ZK863.4.1; c. elegans.
DR CTD; 179670; -.
DR WormBase; ZK863.4; CE23469; WBGene00014124; usip-1.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_414027_0_0_1; -.
DR InParanoid; Q23652; -.
DR OMA; THNISAK; -.
DR OrthoDB; 626698at2759; -.
DR PhylomeDB; Q23652; -.
DR PRO; PR:Q23652; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00014124; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:WormBase.
DR GO; GO:0071076; P:RNA 3' uridylation; IBA:GO_Central.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; IDA:WormBase.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..662
FT /note="U6 snRNA-specific terminal uridylyltransferase"
FT /id="PRO_0000449384"
FT DOMAIN 384..437
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT MUTAGEN 183..185
FT /note="DID->AIA: Loss of terminal uridylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:25753661"
SQ SEQUENCE 662 AA; 75288 MW; 7E2642A83548C29D CRC64;
MSSNLQLVET FDSRQFVVAR WNRNDTTAMV PSAIAVVVFV ESVEYKLGCK EKIGYSPTPE
DQDQFMILQM ESIDEANRIC HDSIAKGFAI NNTKIVFTPL LGLNGFRLQD AIDFMKTSQP
HFNNDELLEV LTMAICQELP ERLKILEDGF SFIEQGVSEL IQNSACEMFG SFASPVRRNG
YSDIDINVES VSAPGQRVST NVRPLNEVVA NPKCLITHPL TKSELETYPQ EEIIKILYRC
FNENSAFKTK FEMRFLPART PIIVFKNIEV EGMNVSYDLS VHNQISVEKA SLLHEFIVKD
KSKGSRMKNA MMFIVHWAKS NKLLSGDYPE EKLEVKTKLN SYIINQLVIH FVQAATNKVH
VNPQAKRDSR VNEYNFDTLF GDYCKFFREL FKYYANFDFT NKAIYGKKAM QKKTLSSAHG
GVEESPLMLM DPMDITHNIS AKVTEDAVKL LNGLIRNALF ILKQNHFHIN YLLETNTMAT
MLMKSREPKI SISTRVTDGA EHQYLSVQLP AVVITSSDLF LLLTRVLRFN VCPNEQGPSV
VDLCTPTGAI FLVTSRAWVG RRNTKRALKN SRHDLTPLQI DVMCSDKYDY EEDIAELRIS
MSTVPGTRIR LACIDIMRGQ VSEVRDAIHF LIDQFINNNY DDLEKNGVQT ISRIPIAAPT
WP
