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   27-MAR-2024, entry version 75.
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.ENSXETP00000027805; -.
DR   PaxDb; 8364-ENSXETP00000061858; -.
DR   GeneID; 100127188; -.
DR   KEGG; xtr:100127188; -.
DR   AGR; Xenbase:XB-GENE-491663; -.
DR   CTD; 64852; -.
DR   eggNOG; KOG2277; Eukaryota.
DR   InParanoid; A9JTS5; -.
DR   OrthoDB; 170176at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
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:0140767; F:enzyme-substrate adaptor activity; ISS:UniProtKB.
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:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; ISS:UniProtKB.
DR   GO; GO:0016180; P:snRNA processing; ISS:UniProtKB.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   CDD; cd12279; RRM_TUT1; 1.
DR   Gene3D; 1.10.1410.10; -; 2.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 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; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF127; SPECKLE TARGETED PIP5K1A-REGULATED POLY(A) POLYMERASE; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 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
//