CATNT_GEOSL
ID CATNT_GEOSL Reviewed; 430 AA.
AC Q74B57;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=CC-adding tRNA nucleotidyltransferase {ECO:0000303|PubMed:18952795};
DE Short=C-adding TNT {ECO:0000303|PubMed:18952795};
DE EC=2.7.7.- {ECO:0000269|PubMed:18952795};
DE AltName: Full=CC-adding enzyme {ECO:0000305};
DE AltName: Full=NTSFII {ECO:0000303|PubMed:18952795};
GN OrderedLocusNames=GSU2184 {ECO:0000312|EMBL:AAR35560.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=18952795; DOI=10.1128/jb.01166-08;
RA Bralley P., Cozad M., Jones G.H.;
RT "Geobacter sulfurreducens contains separate C- and A-adding tRNA
RT nucleotidyltransferases and a poly(A) polymerase.";
RL J. Bacteriol. 191:109-114(2009).
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:18952795}.
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:18952795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:18952795};
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; AE017180; AAR35560.1; -; Genomic_DNA.
DR RefSeq; NP_953233.1; NC_002939.5.
DR RefSeq; WP_010942824.1; NC_002939.5.
DR AlphaFoldDB; Q74B57; -.
DR SMR; Q74B57; -.
DR STRING; 243231.GSU2184; -.
DR EnsemblBacteria; AAR35560; AAR35560; GSU2184.
DR KEGG; gsu:GSU2184; -.
DR PATRIC; fig|243231.5.peg.2215; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_0_7; -.
DR InParanoid; Q74B57; -.
DR OMA; YNYELRI; -.
DR Proteomes; UP000000577; 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; 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 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..430
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447570"
FT BINDING 33..36
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 108..109
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 113
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 150..159
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 190
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 430 AA; 45587 MW; 2ADF9C87168ED266 CRC64;
MDHRLLSFIS APLPSLIASL ARHGGFGAWF VGGCVRDALL ARPSNDIDIV VGPGGEDLPR
AVAARIGGSF FPLDEERGHA RVVLKGEGAS CDFAPLQGGT IAADLALRDF TINALAVSCG
SDDLLDPLGG AADLAQRVIR ACSAGAFAAD PLRIVRAYRF AAHLDFEIHA ATLALIPDHA
PLLATVAGER IRDELFRMLD LPHAVPYVLK MSCAGVTGAI FGADDLPADT AAGALDRVES
LCRDLSAFGT EAEPVRARLR QEVQPGITIR ALAKLAAFLN GAGIPAGIAS QRLMLGKAAT
RLLELLCSSA RLTWPAPAAA PDPHALFTLF CHREPAGCEQ LILPLAEGIL PEDRCRHLAA
YLTRQHIPRG GRLLLTGDDI MILLGLPPGR QVGEAIELLR AAQSTGEVRT RAEAQRYLAK
KQLTTPEPLR
