STPAP_HUMAN
ID STPAP_HUMAN Reviewed; 874 AA.
AC Q9H6E5; A1A527; A8K995; Q2NL65; Q7L583; Q9H6H7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
DE Short=Star-PAP;
DE EC=2.7.7.19 {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955};
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:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:28589955};
GN Name=TUT1; Synonyms=RBM21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC
RP ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16790842; DOI=10.1261/rna.87706;
RA Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R.,
RA Benecke B.-J.;
RT "Identification, cloning, and functional analysis of the human U6 snRNA-
RT specific terminal uridylyl transferase.";
RL RNA 12:1494-1504(2006).
RN [6]
RP LACK OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [7]
RP FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ASP-216 AND ASP-218.
RX PubMed=18288197; DOI=10.1038/nature06666;
RA Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C.,
RA Anderson R.A.;
RT "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of
RT select mRNAs.";
RL Nature 451:1013-1017(2008).
RN [8]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CK1.
RX PubMed=18305108; DOI=10.1074/jbc.m800656200;
RA Gonzales M.L., Mellman D.L., Anderson R.A.;
RT "CKIalpha is associated with and phosphorylates star-PAP and is also
RT required for expression of select star-PAP target messenger RNAs.";
RL J. Biol. Chem. 283:12665-12673(2008).
RN [9]
RP FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, AND
RP INTERACTION WITH CPSF1 AND CPSF3.
RX PubMed=21102410; DOI=10.1038/emboj.2010.287;
RA Laishram R.S., Anderson R.A.;
RT "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF
RT interaction and specificity toward the pre-mRNA.";
RL EMBO J. 29:4132-4145(2010).
RN [10]
RP STRUCTURE BY NMR OF 54-141.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in RNA binding motif protein
RT 21.";
RL Submitted (JUN-2007) to the PDB data bank.
RN [11] {ECO:0007744|PDB:5WU1, ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3, ECO:0007744|PDB:5WU4, ECO:0007744|PDB:5WU5, ECO:0007744|PDB:5WU6}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH
RP MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DOMAIN, AND MUTAGENESIS OF ARG-779 AND ARG-783.
RX PubMed=28589955; DOI=10.1038/ncomms15788;
RA Yamashita S., Takagi Y., Nagaike T., Tomita K.;
RT "Crystal structures of U6 snRNA-specific terminal uridylyltransferase.";
RL Nat. Commun. 8:15788-15788(2017).
CC -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC specific pre-mRNAs (PubMed:18288197, PubMed:21102410). Localizes to
CC nuclear speckles together with PIP5K1A and mediates polyadenylation of
CC a select set of mRNAs, such as HMOX1 (PubMed:18288197). In addition to
CC polyadenylation, it is also required for the 3'-end cleavage of pre-
CC mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the
CC recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs
CC (PubMed:21102410). In addition to adenylyltransferase activity, also
CC has uridylyltransferase activity (PubMed:16790842, PubMed:18288197,
CC PubMed:28589955). However, the ATP ratio is higher than UTP in cells,
CC suggesting that it functions primarily as a poly(A) polymerase
CC (PubMed:18288197). Acts as a specific terminal uridylyltransferase for
CC U6 snRNA in vitro: responsible for a controlled elongation reaction
CC that results in the restoration of the four 3'-terminal UMP-residues
CC found in newly transcribed U6 snRNA (PubMed:16790842, PubMed:18288197,
CC PubMed:28589955). Not involved in replication-dependent histone mRNA
CC degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197,
CC ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955}.
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:16790842, ECO:0000269|PubMed:18288197,
CC ECO:0000269|PubMed:28589955};
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:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410,
CC ECO:0000269|PubMed:28589955};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:28589955};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC Note=Binds 1 divalent cation per subunit.
CC {ECO:0000269|PubMed:28589955};
CC -!- ACTIVITY REGULATION: Adenylyltransferase activity is specifically
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
CC {ECO:0000269|PubMed:18288197}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59 uM for UTP {ECO:0000269|PubMed:28589955};
CC KM=1380 uM for ATP {ECO:0000269|PubMed:28589955};
CC KM=55 uM for U6 snRNA-u4 {ECO:0000269|PubMed:28589955};
CC Note=kcat is 0.059 sec(-1) with UTP as substrate. kcat is 0.002 sec(-
CC 1) with ATP as substrate. kcat is 0.061 sec(-1) with U6 snRNA-u4 as
CC substrate. {ECO:0000269|PubMed:28589955};
CC -!- SUBUNIT: Associates with the cleavage and polyadenylation specificity
CC factor (CPSF) complex (PubMed:21102410). Interacts with CPSF1 and
CC CPSF3; the interaction is direct (PubMed:21102410). Interacts with
CC PIP5K1A (PubMed:18288197). {ECO:0000269|PubMed:18288197,
CC ECO:0000269|PubMed:21102410}.
CC -!- INTERACTION:
CC Q9H6E5; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-2511680, EBI-715394;
CC Q9H6E5; Q99755: PIP5K1A; NbExp=3; IntAct=EBI-2511680, EBI-726414;
CC Q9H6E5; Q99755-1: PIP5K1A; NbExp=2; IntAct=EBI-2511680, EBI-15687389;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16790842}.
CC Nucleus speckle {ECO:0000269|PubMed:18288197,
CC ECO:0000269|PubMed:18305108}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18288197}.
CC -!- DOMAIN: The zinc-finger domain is required for terminal
CC uridylyltransferase activity (PubMed:28589955). Together with the RRM
CC domain, binds the 5'-area of U6 snRNA (PubMed:28589955).
CC {ECO:0000269|PubMed:28589955}.
CC -!- DOMAIN: The RRM domain is required for terminal uridylyltransferase
CC activity (PubMed:28589955). Together with the zinc-finger domain, binds
CC the 5'-area of U6 snRNA (PubMed:28589955).
CC {ECO:0000269|PubMed:28589955}.
CC -!- DOMAIN: The proline-rich region is dispensable for terminal
CC uridylyltransferase activity. {ECO:0000269|PubMed:28589955}.
CC -!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
CC {ECO:0000269|PubMed:18305108}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK025920; BAB15282.1; ALT_INIT; mRNA.
DR EMBL; AK026000; BAB15314.1; -; mRNA.
DR EMBL; AK292610; BAF85299.1; -; mRNA.
DR EMBL; AP002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74029.1; -; Genomic_DNA.
DR EMBL; BC005013; AAH05013.2; -; mRNA.
DR EMBL; BC110910; AAI10911.1; -; mRNA.
DR EMBL; BC128263; AAI28264.1; -; mRNA.
DR CCDS; CCDS8021.2; -.
DR RefSeq; NP_073741.2; NM_022830.2.
DR PDB; 2E5G; NMR; -; A=55-141.
DR PDB; 5WU1; X-ray; 2.80 A; A/B=141-874.
DR PDB; 5WU2; X-ray; 2.95 A; A/B=141-874.
DR PDB; 5WU3; X-ray; 2.70 A; A/B=141-874.
DR PDB; 5WU4; X-ray; 2.80 A; A/B=141-874.
DR PDB; 5WU5; X-ray; 3.40 A; A/B/C/D=141-874.
DR PDB; 5WU6; X-ray; 3.21 A; A/B/C/D=53-599.
DR PDBsum; 2E5G; -.
DR PDBsum; 5WU1; -.
DR PDBsum; 5WU2; -.
DR PDBsum; 5WU3; -.
DR PDBsum; 5WU4; -.
DR PDBsum; 5WU5; -.
DR PDBsum; 5WU6; -.
DR AlphaFoldDB; Q9H6E5; -.
DR SMR; Q9H6E5; -.
DR BioGRID; 122325; 61.
DR DIP; DIP-53651N; -.
DR IntAct; Q9H6E5; 32.
DR MINT; Q9H6E5; -.
DR STRING; 9606.ENSP00000308000; -.
DR iPTMnet; Q9H6E5; -.
DR MetOSite; Q9H6E5; -.
DR PhosphoSitePlus; Q9H6E5; -.
DR BioMuta; TUT1; -.
DR DMDM; 126302611; -.
DR EPD; Q9H6E5; -.
DR jPOST; Q9H6E5; -.
DR MassIVE; Q9H6E5; -.
DR MaxQB; Q9H6E5; -.
DR PaxDb; Q9H6E5; -.
DR PeptideAtlas; Q9H6E5; -.
DR PRIDE; Q9H6E5; -.
DR ProteomicsDB; 80983; -.
DR Antibodypedia; 28452; 89 antibodies from 17 providers.
DR DNASU; 64852; -.
DR Ensembl; ENST00000476907.6; ENSP00000419607.1; ENSG00000149016.16.
DR GeneID; 64852; -.
DR KEGG; hsa:64852; -.
DR MANE-Select; ENST00000476907.6; ENSP00000419607.1; NM_022830.3; NP_073741.3.
DR UCSC; uc058cig.1; human.
DR CTD; 64852; -.
DR DisGeNET; 64852; -.
DR GeneCards; TUT1; -.
DR HGNC; HGNC:26184; TUT1.
DR HPA; ENSG00000149016; Low tissue specificity.
DR MIM; 610641; gene.
DR neXtProt; NX_Q9H6E5; -.
DR OpenTargets; ENSG00000149016; -.
DR PharmGKB; PA162407405; -.
DR VEuPathDB; HostDB:ENSG00000149016; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000159914; -.
DR HOGENOM; CLU_018757_1_0_1; -.
DR InParanoid; Q9H6E5; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q9H6E5; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q9H6E5; -.
DR SignaLink; Q9H6E5; -.
DR BioGRID-ORCS; 64852; 780 hits in 1062 CRISPR screens.
DR ChiTaRS; TUT1; human.
DR EvolutionaryTrace; Q9H6E5; -.
DR GenomeRNAi; 64852; -.
DR Pharos; Q9H6E5; Tbio.
DR PRO; PR:Q9H6E5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H6E5; protein.
DR Bgee; ENSG00000149016; Expressed in cerebellar vermis and 177 other tissues.
DR ExpressionAtlas; Q9H6E5; baseline and differential.
DR Genevisible; Q9H6E5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; IMP:UniProtKB.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; IDA:UniProtKB.
DR CDD; cd12279; RRM_TUT1; 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; IPR036236; Znf_C2H2_sf.
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; SSF57667; SSF57667; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..874
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000254186"
FT DOMAIN 56..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 491..549
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT ZN_FING 16..46
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..874
FT /note="KA1; binds the bulging loops of U6 snRNA but is
FT dispensable for terminal uridylyltransferase activity"
FT /evidence="ECO:0000269|PubMed:28589955"
FT REGION 638..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU4"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:28589955"
FT BINDING 216
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:28589955"
FT BINDING 218
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU4"
FT BINDING 392
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT BINDING 414
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT BINDING 432
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT BINDING 549
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:28589955,
FT ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MHT4"
FT VARIANT 442
FT /note="L -> F (in dbSNP:rs3197865)"
FT /id="VAR_028833"
FT MUTAGEN 216
FT /note="D->A: Abolishes adenylyltransferase activity; when
FT associated with A-218."
FT /evidence="ECO:0000269|PubMed:18288197"
FT MUTAGEN 218
FT /note="D->A: Abolishes adenylyltransferase activity; when
FT associated with A-216."
FT /evidence="ECO:0000269|PubMed:18288197"
FT MUTAGEN 779
FT /note="R->A: Reduced terminal uridylyltransferase activity;
FT when associated with A-783."
FT /evidence="ECO:0000269|PubMed:28589955"
FT MUTAGEN 783
FT /note="R->A: Reduced terminal uridylyltransferase activity;
FT when associated with A-779."
FT /evidence="ECO:0000269|PubMed:28589955"
FT CONFLICT 66
FT /note="D -> G (in Ref. 1; BAB15314)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="Q -> R (in Ref. 1; BAF85299)"
FT /evidence="ECO:0000305"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5WU6"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:5WU6"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5WU6"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5WU6"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5WU6"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:5WU6"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:5WU6"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5WU6"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5WU3"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 388..402
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 406..419
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:5WU3"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:5WU3"
FT TURN 551..554
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 557..574
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 616..628
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 764..770
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 778..791
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 805..812
FT /evidence="ECO:0007829|PDB:5WU3"
FT TURN 816..819
FT /evidence="ECO:0007829|PDB:5WU5"
FT STRAND 829..836
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 842..849
FT /evidence="ECO:0007829|PDB:5WU3"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:5WU3"
FT HELIX 855..874
FT /evidence="ECO:0007829|PDB:5WU3"
SQ SEQUENCE 874 AA; 93847 MW; 85A4117A040FC90D CRC64;
MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV
SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG DVGAREAVLS QSQHSLGGHR
LRVRPREQKE FQSPASKSPK GAAPDSHQLA KALAEAADVG AQMIKLVGLR ELSEAERQLR
SLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS
LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA
SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG CVPGVYRVQT
VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR
GLSGSGPLLS NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS
RLEPSINVEP LSSLLAQFFS CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN
LQDPFDLSHN VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP
SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG ESSQGGTSKR
LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV QDWAMQSPGQ PGDLPLTTGK
HGAPGEEGQP SHAALAERGP KGHEAAQEWS QGEAGKGASL PSSASWRCAL WHRVWQGRRR
ARRRLQQQTK EGAGGGAGTR AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD
RMLTVTPLQD PQGLFPDLHH FLQVFLPQAI RHLK
