CATNT_SYNY3
ID CATNT_SYNY3 Reviewed; 416 AA.
AC Q55428;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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:12370185};
DE AltName: Full=CC-adding enzyme {ECO:0000303|PubMed:12370185};
GN OrderedLocusNames=sll0825 {ECO:0000312|EMBL:BAA10528.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12370185; DOI=10.1074/jbc.m207527200;
RA Tomita K., Weiner A.M.;
RT "Closely related CC- and A-adding enzymes collaborate to construct and
RT repair the 3'-terminal CCA of tRNA in Synechocystis sp. and Deinococcus
RT radiodurans.";
RL J. Biol. Chem. 277:48192-48198(2002).
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:12370185}.
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:12370185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:12370185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O67911};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10528.1; -; Genomic_DNA.
DR PIR; S75793; S75793.
DR AlphaFoldDB; Q55428; -.
DR SMR; Q55428; -.
DR STRING; 1148.1001282; -.
DR PaxDb; Q55428; -.
DR EnsemblBacteria; BAA10528; BAA10528; BAA10528.
DR KEGG; syn:sll0825; -.
DR eggNOG; COG0617; Bacteria.
DR OMA; FDEAIYK; -.
DR PhylomeDB; Q55428; -.
DR Proteomes; UP000001425; 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; IPR032810; CCA-adding_enz_C.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR Pfam; PF13735; tRNA_NucTran2_2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..416
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447571"
FT BINDING 31..34
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 106..107
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 111
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 148..157
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 188
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 416 AA; 46388 MW; A846C6CFBB9FD312 CRC64;
MLCPVSHLAD LRQQVPFDLA LLPPQACLVG GAVRDALLGR RREYLDWDFV VPSGAIETAS
AIASRYRAGF VVLDKARHIA RVVFAHGTVD FAQQEGMSLE QDLARRDFTV NAIAYNFQQN
KLIDPMAGVG DLQRGQLKMV AAVNLADDPL RLLRAYRQAA QLQFTLDPDT RTVLRELAPR
IKTVAAERVQ AEFNYLLGSP RGSQWLLAAW QDGILAHWFS HANLSSLNAI GCIDLAIAAI
KNQLTLVERQ QFFQALGKKG IAIAKLASLV CADVKIAEGE LQRLKYSRHE LRSVQAILQG
YPQLSCLENS PTVRQLYFFF VELGKYLPHF VLYALAHCPH NYHSFIFELL THYLNSGDRL
AHPQPLITGK DLIDKLHIKP SPLIGQLLTE INIAHIEGKI SNEQEALAYA QELGKS
