CID1_SCHPO
ID CID1_SCHPO Reviewed; 405 AA.
AC O13833; O94608;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Terminal uridylyltransferase cid1 {ECO:0000305};
DE Short=TUTase cid1 {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:12218190, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0000269|PubMed:25712096};
DE EC=2.7.7.52 {ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298};
DE AltName: Full=Caffeine-induced death protein 1 {ECO:0000303|PubMed:10757807};
DE AltName: Full=Poly(A) polymerase cid1 {ECO:0000303|PubMed:12218190};
DE Short=PAP {ECO:0000303|PubMed:12218190};
DE AltName: Full=Poly(U) polymerase cid1 {ECO:0000303|PubMed:17449726};
DE Short=PUP {ECO:0000303|PubMed:22608966};
GN Name=cid1 {ECO:0000303|PubMed:10757807}; ORFNames=SPAC19D5.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10757807; DOI=10.1128/mcb.20.9.3234-3244.2000;
RA Wang S.-W., Toda T., MacCallum R., Harris A.L., Norbury C.;
RT "Cid1, a fission yeast protein required for S-M checkpoint control when DNA
RT polymerase delta or epsilon is inactivated.";
RL Mol. Cell. Biol. 20:3234-3244(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-101 AND ASP-103, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12218190; DOI=10.1073/pnas.192467799;
RA Read R.L., Martinho R.G., Wang S.W., Carr A.M., Norbury C.J.;
RT "Cytoplasmic poly(A) polymerases mediate cellular responses to S phase
RT arrest.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12079-12084(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=17353264; DOI=10.1128/mcb.02209-06;
RA Rissland O.S., Mikulasova A., Norbury C.J.;
RT "Efficient RNA polyuridylation by noncanonical poly(A) polymerases.";
RL Mol. Cell. Biol. 27:3612-3624(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17449726; DOI=10.1261/rna.514007;
RA Kwak J.E., Wickens M.;
RT "A family of poly(U) polymerases.";
RL RNA 13:860-867(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19430462; DOI=10.1038/nsmb.1601;
RA Rissland O.S., Norbury C.J.;
RT "Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA
RT turnover.";
RL Nat. Struct. Mol. Biol. 16:616-623(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH UTP, RNA-BINDING,
RP MUTAGENESIS OF ASP-101; ASP-103; LYS-133; ARG-137; ARG-277; LYS-282;
RP LYS-321; ARG-323; ASP-330; GLU-333 AND HIS-336, AND CATALYTIC ACTIVITY.
RX PubMed=22751018; DOI=10.1038/nsmb.2329;
RA Yates L.A., Fleurdepine S., Rissland O.S., De Colibus L., Harlos K.,
RA Norbury C.J., Gilbert R.J.;
RT "Structural basis for the activity of a cytoplasmic RNA terminal uridylyl
RT transferase.";
RL Nat. Struct. Mol. Biol. 19:782-787(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-377 IN COMPLEX WITH ATP; CTP
RP AND UTP, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-160 AND HIS-336,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22885303; DOI=10.1093/nar/gks740;
RA Lunde B.M., Magler I., Meinhart A.;
RT "Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism
RT for UTP selectivity.";
RL Nucleic Acids Res. 40:9815-9824(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 40-377 IN COMPLEX WITH UTP AND
RP MAGNESIUM, AND RNA-BINDING.
RX PubMed=22608966; DOI=10.1016/j.str.2012.04.006;
RA Munoz-Tello P., Gabus C., Thore S.;
RT "Functional implications from the Cid1 poly(U) polymerase crystal
RT structure.";
RL Structure 20:977-986(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 40-377 IN COMPLEX WITH UTP,
RP MUTAGENESIS OF LYS-144; ASP-160; ASN-165 AND PHE-332, AND CATALYTIC
RP ACTIVITY.
RX PubMed=24322298; DOI=10.1093/nar/gkt1278;
RA Munoz-Tello P., Gabus C., Thore S.;
RT "A critical switch in the enzymatic properties of the Cid1 protein
RT deciphered from its product-bound crystal structure.";
RL Nucleic Acids Res. 42:3372-3380(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 40-405, MUTAGENESIS OF PHE-88;
RP ASN-164 AND ASN-165, AND CATALYTIC ACTIVITY.
RX PubMed=25712096; DOI=10.1093/nar/gkv122;
RA Yates L.A., Durrant B.P., Fleurdepine S., Harlos K., Norbury C.J.,
RA Gilbert R.J.;
RT "Structural plasticity of Cid1 provides a basis for its distributive RNA
RT terminal uridylyl transferase activity.";
RL Nucleic Acids Res. 43:2968-2979(2015).
CC -!- FUNCTION: Cytoplasmic uridylyltransferase that mediates the terminal
CC uridylation of mRNAs with short poly(A) tails such as such as act1,
CC hcn1 and urg1 mRNAs, hence facilitating global mRNA decay
CC (PubMed:17353264, PubMed:17449726, PubMed:19430462, PubMed:22751018,
CC PubMed:22885303). Uridylates the 3' ends of actin mRNAs upon S-phase
CC arrest (PubMed:17353264). Has also a weak poly(A) polymerase (PAP)
CC activity (PubMed:22751018, PubMed:22885303). Residue His-336 is
CC responsible for the specificity for UTP (PubMed:22751018,
CC PubMed:22885303). Involved in cell cycle arrest where in association
CC with crb2/rhp9 and chk1 it inhibits unscheduled mitosis
CC (PubMed:10757807). {ECO:0000269|PubMed:10757807,
CC ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726,
CC ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303}.
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:17353264, ECO:0000269|PubMed:17449726,
CC ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018,
CC ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298,
CC ECO:0000269|PubMed:25712096};
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:12218190, ECO:0000269|PubMed:22751018,
CC ECO:0000269|PubMed:22885303};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:22885303};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17353264};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for UTP {ECO:0000269|PubMed:22885303};
CC KM=312 uM for ATP {ECO:0000269|PubMed:22885303};
CC Note=Mutation of His-336 to Asn decreases the Km for ATP to 65 uM and
CC increases the Km for UTP to 45 uM. {ECO:0000269|PubMed:22885303};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218190}.
CC -!- DISRUPTION PHENOTYPE: Stabilizes urg1 transcripts (PubMed:19430462).
CC {ECO:0000269|PubMed:19430462}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- CAUTION: Has been first identified as a cytoplasmic poly(A) polymerase
CC (PAP) implicated in cell cycle checkpoint controls (PubMed:12218190).
CC Further studies showed that cid1 had robust poly(U) polymerase activity
CC in vitro and that is was rather an RNA uridylyltransferase
CC (PubMed:17353264, PubMed:17449726). {ECO:0000269|PubMed:17353264,
CC ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:19430462}.
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DR EMBL; CU329670; CAB50789.1; -; Genomic_DNA.
DR EMBL; AF105076; AAD16889.1; -; mRNA.
DR PIR; T37963; T37963.
DR RefSeq; NP_594901.1; NM_001020330.2.
DR PDB; 4E7X; X-ray; 3.20 A; A/B/C/D=1-405.
DR PDB; 4E80; X-ray; 3.02 A; A/B/C/D=1-405.
DR PDB; 4E8F; X-ray; 2.60 A; A/B=1-405.
DR PDB; 4EP7; X-ray; 2.28 A; A/B=40-377.
DR PDB; 4FH3; X-ray; 2.00 A; A=33-377.
DR PDB; 4FH5; X-ray; 2.30 A; A=33-377.
DR PDB; 4FHP; X-ray; 2.50 A; A=33-377.
DR PDB; 4FHV; X-ray; 2.10 A; A=33-377.
DR PDB; 4FHW; X-ray; 2.50 A; A=33-377.
DR PDB; 4FHX; X-ray; 2.70 A; A=33-377.
DR PDB; 4FHY; X-ray; 2.70 A; A=33-377.
DR PDB; 4NKT; X-ray; 1.90 A; A/B=40-377.
DR PDB; 4NKU; X-ray; 1.94 A; A/B=40-377.
DR PDB; 4UD4; X-ray; 1.74 A; A/B=40-405.
DR PDB; 4UD5; X-ray; 2.52 A; A/B=40-405.
DR PDBsum; 4E7X; -.
DR PDBsum; 4E80; -.
DR PDBsum; 4E8F; -.
DR PDBsum; 4EP7; -.
DR PDBsum; 4FH3; -.
DR PDBsum; 4FH5; -.
DR PDBsum; 4FHP; -.
DR PDBsum; 4FHV; -.
DR PDBsum; 4FHW; -.
DR PDBsum; 4FHX; -.
DR PDBsum; 4FHY; -.
DR PDBsum; 4NKT; -.
DR PDBsum; 4NKU; -.
DR PDBsum; 4UD4; -.
DR PDBsum; 4UD5; -.
DR AlphaFoldDB; O13833; -.
DR SMR; O13833; -.
DR BioGRID; 278883; 30.
DR STRING; 4896.SPAC19D5.03.1; -.
DR iPTMnet; O13833; -.
DR MaxQB; O13833; -.
DR PaxDb; O13833; -.
DR PRIDE; O13833; -.
DR EnsemblFungi; SPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03.
DR GeneID; 2542420; -.
DR KEGG; spo:SPAC19D5.03; -.
DR PomBase; SPAC19D5.03; cid1.
DR VEuPathDB; FungiDB:SPAC19D5.03; -.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_033943_0_2_1; -.
DR InParanoid; O13833; -.
DR OMA; LNRKELC; -.
DR PhylomeDB; O13833; -.
DR PRO; PR:O13833; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:PomBase.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:PomBase.
DR GO; GO:0002134; F:UTP binding; IDA:PomBase.
DR GO; GO:0036450; P:polyuridylation-dependent decapping of nuclear-transcribed mRNA; IMP:PomBase.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:PomBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..405
FT /note="Terminal uridylyltransferase cid1"
FT /id="PRO_0000120312"
FT DOMAIN 267..336
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT REGION 377..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22885303"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22885303"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22885303"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22885303"
FT BINDING 168..172
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 211..212
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22885303"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22608966,
FT ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22885303"
FT MUTAGEN 88
FT /note="F->D: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:25712096"
FT MUTAGEN 101
FT /note="D->A: Abolishes catalytic activity but does not
FT affect RNA binding; when associated with A-103."
FT /evidence="ECO:0000269|PubMed:12218190,
FT ECO:0000269|PubMed:22751018"
FT MUTAGEN 103
FT /note="D->A: Abolishes catalytic activity but does not
FT affect RNA binding; when associated with A-101."
FT /evidence="ECO:0000269|PubMed:12218190,
FT ECO:0000269|PubMed:22751018"
FT MUTAGEN 133
FT /note="K->A: Impairs binding to RNA; when associated with
FT A-137; A-321 and A-323. Impairs also binding to RNA; when
FT associated with A-137; A-277 and A-282."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 137
FT /note="R->A: Impairs binding to RNA; when associated with
FT A-133; A-321 and A-323. Impairs also binding to RNA; when
FT associated with A-133; A-277 and A-282."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 144
FT /note="K->A: Reduces association with a 15-mer A stretch
FT but does not affect association with a 15-mer U stretch."
FT /evidence="ECO:0000269|PubMed:24322298"
FT MUTAGEN 160
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22885303,
FT ECO:0000269|PubMed:24322298"
FT MUTAGEN 164
FT /note="N->P: Predominantly performs monouridylation."
FT /evidence="ECO:0000269|PubMed:25712096"
FT MUTAGEN 165
FT /note="N->A,P: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:24322298,
FT ECO:0000269|PubMed:25712096"
FT MUTAGEN 277
FT /note="R->A: Impairs binding to RNA; when associated with
FT A-282; A-133 and A-137. Impairs also binding to RNA; when
FT associated with A-282; A-321 and A-323."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 282
FT /note="K->A: Impairs binding to RNA; when associated with
FT A-277; A-133 and A-137. Impairs also binding to RNA; when
FT associated with A-277; A-321 and A-323."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 321
FT /note="K->A: Impairs binding to RNA; when associated with
FT A-323; A-277 and A-282. Impairs also binding to RNA; when
FT associated with A-323; A-133 and A-137."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 323
FT /note="R->A: Impairs binding to RNA; when associated with
FT A-321; A-277 and A-282. Impairs also binding to RNA; when
FT associated with A-321; A-133 and A-137."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 330
FT /note="D->A: Leads to diminished TUTase activity."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 332
FT /note="F->A: Reduces capacity for binding RNAs."
FT /evidence="ECO:0000269|PubMed:24322298"
FT MUTAGEN 333
FT /note="E->A: Leads to diminished TUTase activity."
FT /evidence="ECO:0000269|PubMed:22751018"
FT MUTAGEN 336
FT /note="H->A,N: Abolishes the UTP specificity and converts
FT Cid1 from a TUTase into a poly(A) polymerase (PAP)."
FT /evidence="ECO:0000269|PubMed:22751018,
FT ECO:0000269|PubMed:22885303"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 59..79
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4FH3"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4UD4"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:4UD4"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4EP7"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:4UD5"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4UD5"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4EP7"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:4UD4"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:4UD4"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:4UD4"
SQ SEQUENCE 405 AA; 46257 MW; 0AA24B4411B61027 CRC64;
MNISSAQFIP GVHTVEEIEA EIHKNLHISK SCSYQKVPNS HKEFTKFCYE VYNEIKISDK
EFKEKRAALD TLRLCLKRIS PDAELVAFGS LESGLALKNS DMDLCVLMDS RVQSDTIALQ
FYEELIAEGF EGKFLQRARI PIIKLTSDTK NGFGASFQCD IGFNNRLAIH NTLLLSSYTK
LDARLKPMVL LVKHWAKRKQ INSPYFGTLS SYGYVLMVLY YLIHVIKPPV FPNLLLSPLK
QEKIVDGFDV GFDDKLEDIP PSQNYSSLGS LLHGFFRFYA YKFEPREKVV TFRRPDGYLT
KQEKGWTSAT EHTGSADQII KDRYILAIED PFEISHNVGR TVSSSGLYRI RGEFMAASRL
LNSRSYPIPY DSLFEEAPIP PRRQKKTDEQ SNKKLLNETD GDNSE
