ID   STPAP_DANRE             Reviewed;         797 AA.
AC   Q4KMD7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
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; ORFNames=zgc:112254;
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].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2005) 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; BC098614; AAH98614.1; -; mRNA.
DR   RefSeq; NP_001025359.1; NM_001030188.1.
DR   AlphaFoldDB; Q4KMD7; -.
DR   SMR; Q4KMD7; -.
DR   STRING; 7955.ENSDARP00000074395; -.
DR   PaxDb; 7955-ENSDARP00000074395; -.
DR   GeneID; 564388; -.
DR   KEGG; dre:564388; -.
DR   AGR; ZFIN:ZDB-GENE-050706-68; -.
DR   CTD; 64852; -.
DR   ZFIN; ZDB-GENE-050706-68; tut1.
DR   eggNOG; KOG2277; Eukaryota.
DR   InParanoid; Q4KMD7; -.
DR   OrthoDB; 170176at2759; -.
DR   PhylomeDB; Q4KMD7; -.
DR   PRO; PR:Q4KMD7; -.
DR   Proteomes; UP000000437; Chromosome 12.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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: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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; ISS:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
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   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00451; ZnF_U1; 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..797
FT                   /note="Speckle targeted PIP5K1A-regulated poly(A)
FT                   polymerase"
FT                   /id="PRO_0000404590"
FT   DOMAIN          54..126
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          421..495
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         14..44
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT   REGION          544..787
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          611..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         216
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         218
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         319
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         341
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         363
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         495
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
SQ   SEQUENCE   797 AA;  89937 MW;  C11F915CC7CCA221 CRC64;
     MELDKDIQTT QKGFHCNLCH VNIPNRPSLE DHVKGKKHLH LLRLRAQRKT QEENSVFVSG
     FKADTSQTEL KEYFQQFGLV TDVIMDKQKG VYAIVEFSES QDVQTTLAQP QHQLNGLKLR
     VKPREKKEFK LASRGKQDCK NTLISLDKLN FELCKAMSVN EQIQKVVESL ELKDNEKKVR
     DLLVQLLQEV FTEFFPDCQI VPFGSSVNTF GLHSCDLDLF LDLENTKVFQ ARAKSSEQTG
     ENQSEDCRSE DSILSDIDLS TASPAEILEL VAVILRKCVP GVHKVQALST ARLPVVKFSH
     KELNLQGDIT INNRLAVRNT KFLQLCSGID SRLRPLVYTI RLWAKQKQLA GNLSGPGPLL
     NNYALTLLVI FFLQNRDPPV LPSVNQLKNM ACEEEECAIE EWDCTFPSQP FSVPPSKNTE
     DLCTLLFGFF TFYSKFDFPA SVVSLRDGHV LPITDFLKSD MEALKTADAS SPKPKRSSAP
     RLGPMNVLDP FELNHNVAGN LNERTQKNFK RECCEAEKYC RSLQYQRKSA KGKSWGLVRL
     FAPQSEAAAS SQPRAEKVLE VSVPFKPASL PESLRAQLAS AGKDFRGLWF AEVCSAVQKV
     FNEILQCSPT EETQSLDKTD KSGSEMEVNN NRSLEDTNIQ VKGEAGKKRP LSVEEGPSTF
     TITQAKRQRL DVDLEHPEPL HWTWTQRSRV WAGRRKVRRD LLKTSDEASK PEGGCVDMES
     RVTQSIVEKE EKLHDALEFK VDAEVVGGNE STKVVLRFHP SIDTAGVFQD FFHFLESFLP
     KMAETIMGRA EDITDMS
//