AATNT_DEIRA
ID AATNT_DEIRA Reviewed; 434 AA.
AC Q9RV39;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=A-adding tRNA nucleotidyltransferase {ECO:0000305};
DE Short=A-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:12370185};
DE AltName: Full=A-adding enzyme {ECO:0000303|PubMed:12370185};
GN OrderedLocusNames=DR_1191 {ECO:0000312|EMBL:AAF10763.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 terminal adenosine residue to tRNA.
CC {ECO:0000269|PubMed:12370185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end +
CC diphosphate; Xref=Rhea:RHEA:60012, Rhea:RHEA-COMP:10468, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83069,
CC ChEBI:CHEBI:83071; Evidence={ECO:0000269|PubMed:12370185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60013;
CC Evidence={ECO:0000269|PubMed:12370185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O66728};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; AE000513; AAF10763.1; -; Genomic_DNA.
DR PIR; F75425; F75425.
DR RefSeq; NP_294915.1; NC_001263.1.
DR RefSeq; WP_010887834.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RV39; -.
DR SMR; Q9RV39; -.
DR STRING; 243230.DR_1191; -.
DR EnsemblBacteria; AAF10763; AAF10763; DR_1191.
DR KEGG; dra:DR_1191; -.
DR PATRIC; fig|243230.17.peg.1391; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_2_0; -.
DR InParanoid; Q9RV39; -.
DR OMA; GWTFHGH; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; 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; cd00077; HDc; 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.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..434
FT /note="A-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447565"
FT DOMAIN 227..339
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 20..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 91..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 132..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
SQ SEQUENCE 434 AA; 47988 MW; A792A1A6BDD6A0D2 CRC64;
MFRRRPPLPP FPPGAALVGG AVRDWLRGVR SADYDWAHPD PAAGARALAA LVGGAAFPLD
EERGYWRVTA GEVQHDFVPL PPNLEDDLRR RDFTVNAIAL REGRRLVDPL GGQQDLKRRV
LRMVSEDNLR ADPLRAWRAA RFVTTLSFTL EPQTEQAVRQ VAADLKAGRL PFPAWERVRD
ELHALLRSPD AARGILTLEA LGLLDLTLPE LREGQGLTQG GFHHLDVFEH GVEALHQLLT
RRPDADLLLR WATLLHDVGK PRTFARDPDT GRRSFHGHDR VGAELTTQIL TRLKLPGADV
KRAAALVKAH MVQLPADDAQ ARRFVHRRRE LLPDLLSLML ADREAARGPS SSELGRFAYM
LAMERVLAAL EEQPAAPPPL LSGKEVMALL GLTPGPRVGE VLRALAEARA LGEVGTPQEA
RAFVQRWAEE TPGS
