STPAP_XENTR
ID STPAP_XENTR Reviewed; 843 AA.
AC A9JTS5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
DE Short=Star-PAP;
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q9H6E5};
DE AltName: Full=RNA-binding motif protein 21;
DE Short=RNA-binding protein 21;
DE AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1;
DE Short=U6-TUTase;
DE EC=2.7.7.52 {ECO:0000250|UniProtKB:Q9H6E5};
GN Name=tut1; Synonyms=rbm21;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=TGA IC; TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC specific pre-mRNAs. In addition to polyadenylation, it is also required
CC for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted
CC pre-mRNAs and promotes the recruitment and assembly of the CPSF complex
CC on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity,
CC also has uridylyltransferase activity. However, the ATP ratio is higher
CC than UTP in cells, suggesting that it functions primarily as a poly(A)
CC polymerase. {ECO:0000250|UniProtKB:Q9H6E5}.
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:0000250|UniProtKB:Q9H6E5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000250|UniProtKB:Q9H6E5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H6E5};
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: Associates with the cleavage and polyadenylation specificity
CC factor (CPSF) complex. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- DOMAIN: The zinc-finger domain is required for terminal
CC uridylyltransferase activity. Together with the RRM domain, binds the
CC 5'-area of U6 snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- DOMAIN: The RRM domain is required for terminal uridylyltransferase
CC activity. Together with the zinc-finger domain, binds the 5'-area of U6
CC snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; BC155457; AAI55458.1; -; mRNA.
DR RefSeq; XP_002941502.2; XM_002941456.4.
DR AlphaFoldDB; A9JTS5; -.
DR SMR; A9JTS5; -.
DR STRING; 8364.ENSXETP00000061858; -.
DR PaxDb; A9JTS5; -.
DR GeneID; 100127188; -.
DR KEGG; xtr:100127188; -.
DR CTD; 64852; -.
DR Xenbase; XB-GENE-491663; tut1.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; A9JTS5; -.
DR OrthoDB; 1188122at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; ISS:UniProtKB.
DR CDD; cd12279; RRM_TUT1; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034388; Star-PAP_RRM.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF19088; TUTase; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW RNA-binding; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..843
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000404591"
FT DOMAIN 54..126
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 456..516
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT ZN_FING 25..55
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 134..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..837
FT /note="KA1; binds the bulging loops of U6 snRNA but is
FT dispensable for terminal uridylyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT REGION 653..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 226
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 228
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 354
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 376
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 398
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 516
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
SQ SEQUENCE 843 AA; 94496 MW; B36785E0C7A5A4CC CRC64;
MEAEESSSSV VPLPQDVQSV VRGGFRCLLC GVNIPNRPSL TDHLSGRRHV RLHEERDKRN
QQQERSVYVS NFPRETSEEQ LRDVFQKISP VRNIVMDKDR GLYAIVEFES KDGMCAALEE
PQIKLSGKRL RVKPREKKEF QRKKGGSPRT LQPPDPEALS KELLNCADVE QQIKKLVSLC
SPSHHESHLR ELLLSLLQET FTEFFPGCQL LPFGSSVNGF EISGCDLDLY LDLGDDEAEN
VEGKAEKEIQ NREESSTDME VSMEDPETER KEEEMEIGNS KNDEDEDVTP GLSLKGLSSE
EILEVVGKVL RHCVPGVHGV QSVPTARRPV IHFQHKTSGL RGDVTLNNRL ALRNSSFLRL
CSDLDARVPQ LVYTVRYWAR VNQLAGNPFG GGPLLNNYAL TLLVFFFLQT RNPPVLPTLV
HLREETANEV PQVIDGWDCS FPSDPAQVKE SGNQQSLSSL LSEFFSFYAS LDLHLLILCP
CNGLTIPLPF SSPPPAWSEG FRLGPLNIQD PFELSHNVCG NVSSRAARRF ISHCAAAARI
CRTPNYNLHS TSHPWGITPI LLPPPTEREC VGRGGTEISI PLGGVSPEKT YAAVSKVFVD
VLLCTLEEGR EDSCQEGKAL ELSTKHAKAQ CKVEKNEVGG ELGEQEVPCK AEQNNTKEAS
KQKSIFKTEE GMTESARRKR EMTEPCMSDM TNGKKRRLEF TRGIWDHHLA TSAMEEEMCG
EAHKDSKTKI DYSNNGTAQW ELLVWHRVWE GRRKERRRKQ KGEADGVELE IAVSQALALE
KEDKCDGPLM KLILTAQLTV KESLQLYLTP KFDPQGLSST FFHFLESYLP RMVAQIQGCG
DPV
