CATNT_AQUAE
ID CATNT_AQUAE Reviewed; 512 AA.
AC O67911;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=CC-adding tRNA nucleotidyltransferase {ECO:0000305};
DE Short=C-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:11701927};
DE AltName: Full=CC-adding enzyme {ECO:0000303|PubMed:11701927};
GN OrderedLocusNames=aq_2158 {ECO:0000312|EMBL:AAC07883.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11701927; DOI=10.1126/science.1063816;
RA Tomita K., Weiner A.M.;
RT "Collaboration between CC- and A-adding enzymes to build and repair the 3'-
RT terminal CCA of tRNA in Aquifex aeolicus.";
RL Science 294:1334-1336(2001).
RN [3] {ECO:0007744|PDB:3WFO, ECO:0007744|PDB:3WFP, ECO:0007744|PDB:3WFQ, ECO:0007744|PDB:3WFR, ECO:0007744|PDB:3WFS}
RP X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) IN COMPLEXES WITH CTP; TRNA AND
RP MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS
RP OF ASP-58; ASP-60; PHE-83; PHE-85; ASP-112; ARG-132; ASP-133; ASP-182;
RP ARG-185; GLU-221; ARG-222; ARG-361; GLY-363 AND HIS-377.
RX PubMed=24389024; DOI=10.1016/j.str.2013.12.002;
RA Yamashita S., Takeshita D., Tomita K.;
RT "Translocation and rotation of tRNA during template-independent RNA
RT polymerization by tRNA nucleotidyltransferase.";
RL Structure 22:315-325(2014).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. Adds the two cytidine residues to tRNA.
CC {ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2
CC diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896,
CC ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:11701927,
CC ECO:0000269|PubMed:24389024};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24389024};
CC -!- DOMAIN: Adopts a seahorse-like shape and consists of four domains:
CC head, neck, body, and tail. {ECO:0000305|PubMed:24389024}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07883.1; -; Genomic_DNA.
DR PIR; C70485; C70485.
DR RefSeq; NP_214480.1; NC_000918.1.
DR RefSeq; WP_010881416.1; NC_000918.1.
DR PDB; 3WFO; X-ray; 3.40 A; A/B/C=1-512.
DR PDB; 3WFP; X-ray; 4.00 A; A/B/C/D/E/F/G/H=17-450.
DR PDB; 3WFQ; X-ray; 3.62 A; E/F/G/H=16-448.
DR PDB; 3WFR; X-ray; 3.50 A; E/F/G/H=16-453.
DR PDB; 3WFS; X-ray; 3.31 A; C/D=16-448.
DR PDBsum; 3WFO; -.
DR PDBsum; 3WFP; -.
DR PDBsum; 3WFQ; -.
DR PDBsum; 3WFR; -.
DR PDBsum; 3WFS; -.
DR AlphaFoldDB; O67911; -.
DR SMR; O67911; -.
DR STRING; 224324.aq_2158; -.
DR EnsemblBacteria; AAC07883; AAC07883; aq_2158.
DR KEGG; aae:aq_2158; -.
DR PATRIC; fig|224324.8.peg.1668; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_2_0; -.
DR InParanoid; O67911; -.
DR OMA; GWTFHGH; -.
DR OrthoDB; 2018439at2; -.
DR BRENDA; 2.7.7.19; 396.
DR BRENDA; 2.7.7.72; 396.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..512
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447568"
FT BINDING 42..45
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 132..133
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 137
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 182..191
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:24389024"
FT BINDING 222
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 58
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 60
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 83
FT /note="F->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 85
FT /note="F->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 112
FT /note="D->A: Reduces CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 132
FT /note="R->A: Strong decrease in CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 133
FT /note="D->A: Strong decrease in CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 182
FT /note="D->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 185
FT /note="R->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 221
FT /note="E->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 222
FT /note="R->A: Reduces CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 361
FT /note="R->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 363
FT /note="G->Y: Reduces the CMP incorporation at position 74
FT of the tRNA, but does not affect the CMP incorporation at
FT position 75."
FT /evidence="ECO:0000269|PubMed:24389024"
FT MUTAGEN 377
FT /note="H->A: Does not affect CMP incorporation."
FT /evidence="ECO:0000269|PubMed:24389024"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3WFO"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3WFO"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:3WFO"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3WFS"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3WFO"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:3WFS"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:3WFS"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:3WFS"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:3WFS"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 408..421
FT /evidence="ECO:0007829|PDB:3WFS"
FT HELIX 426..444
FT /evidence="ECO:0007829|PDB:3WFS"
SQ SEQUENCE 512 AA; 58913 MW; 58CDB8FD1A1B6F0F CRC64;
MENIEIVSSG KHTLHGLNFY LSYFDDVAKV LPREHYCFIV GGWVRDRILG EPVGYNIDVD
FLTTADPVEL AKNFAKRIGG HFFVFEKRGF LIKRPTIASV VLHLPPYRYR FDFSPLKGKD
LEKALIEDLK ERDFTANAIA VNLDDVLSIG AKQTIVYDPT GGIKDLEQGL LRPVSIENLK
RDPVRVLRGF RIAIEKNLQL TEDFYEFVKE DPRIVLKSAV ERITHELFKI MKEKTAHKVI
RELYEYGVLE AIIPEIGRLR EVKDQGEHHI YPLDEHTLKT LEYLEQVIED RAKYLSAELL
ENFGKKRVLG EFTDVELLKW GALFHDIGKP QTFAVREGKV TFYEHDKVGA QIVREIGERL
RWGDEATEFV AKLVRHHLRP FFLREAFKKG ELKRRGMANF WRECGDIAPH LFLLSIADAM
ASGDEEEDIK ALMETIAELE SFNRNEMKEE IQKPLLNGDE IMEILGIKPG KIVGILKKAL
LEAQIDGKVE TKEEAIEFIK RSTKNLKPLD EG
