AATNT_SYNY3
ID AATNT_SYNY3 Reviewed; 942 AA.
AC P74081;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=sll1253 {ECO:0000312|EMBL:BAA18159.1};
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).
RN [3]
RP FUNCTION AS A NUCLEOTIDYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12601000; DOI=10.1074/jbc.m211571200;
RA Rott R., Zipor G., Portnoy V., Liveanu V., Schuster G.;
RT "RNA polyadenylation and degradation in cyanobacteria are similar to the
RT chloroplast but different from Escherichia coli.";
RL J. Biol. Chem. 278:15771-15777(2003).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. Adds the terminal adenosine residue to tRNA
CC (PubMed:12370185). Acts as a nucleotidyltransferase and not a poly(A)
CC polymerase (PubMed:12601000). {ECO:0000269|PubMed:12370185,
CC ECO:0000269|PubMed:12601000}.
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 -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:12601000}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000022; BAA18159.1; -; Genomic_DNA.
DR PIR; S75598; S75598.
DR AlphaFoldDB; P74081; -.
DR SMR; P74081; -.
DR IntAct; P74081; 4.
DR STRING; 1148.1653244; -.
DR PaxDb; P74081; -.
DR EnsemblBacteria; BAA18159; BAA18159; BAA18159.
DR KEGG; syn:sll1253; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR InParanoid; P74081; -.
DR OMA; ILCHTTA; -.
DR PhylomeDB; P74081; -.
DR Proteomes; UP000001425; Chromosome.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01743; PolyA_pol; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW ATP-binding; CBS domain; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Repeat; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..942
FT /note="A-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447567"
FT DOMAIN 335..394
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 398..453
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 452..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517..520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 628..629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 673..682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
SQ SEQUENCE 942 AA; 105906 MW; F4C587D0D34375DB CRC64;
MDLILCHQTA DFDVLGAAVG LAKLHPGSRI VLTGGSHPTV RQFLALHRNE FPLIELRSVN
PDKIRSLYIV DNQQGDRLGK AADWLTLPHL RQVAIYDHHL NSPRDIEADI WELEAVGAST
TLIVEKLQRA DISLSMVEAS VMALGIHVDT GSLTFTQTTV RDVKALAWLM EQGANLRLIA
EYADPGFPPP LQFLFAEAMQ NLHKEMVRGY WLGSVLLTTE NFVPGLSHLT ERLLSLTECD
ALLLGHVYDK GKDKTKNDEQ REKTGVISNQ RFSLIGRTRI PDTDLTQLLE PYGGGGHAQA
AAVNLRDVEP TTVMAEIYQA LQRQIPKPLL ARDFMSSPVR TIRPHTTIEQ AQRVLFRYGH
SGLTVVNQEE KLVGIISRRD LDLALHHGFS HAPVKGYMTR NVKTIAPDTP LPRIEAIMVA
DDVGRLPVMD QEKLVGIVTR TDVLRQLLQD KQEQSGRFGA PRSGSLRDRP TTPNQNFGQG
SLLQLLKTHL PPATWQLLTT AAQQAQTRGW HLYLVGGAVR DLWLRHSQGA EKHQNITFQD
IDLVVDGFHA TADVGAGVEL AQALQGDYPG ARLSVHGEFQ TAALLWHKDP QLDTLWVDIA
TARTEFYPYP AANPEVEASS IRQDLYRRDF TINALSIRLT NPNPGKLLDF FGGMNDLQSQ
QVRVLHANSF IEDPTRIYRA VRFVVRLGFE LEPQTETYIR YAIASGVYER WRLTEHPTPA
LTTRLKAELS IILKAPYWKG ALTLLADLDA LKCLHAELKL TEQLWWQVRY LSRWLRWFDP
ERNLEHWLLR LGILLGALPP QEREKIAAGL QLPKATIDGL TNLETIETAI AKGLNSPASP
KSSPKSSVIY QTLKDYDRFS LFLVAARGNK LLRKQIWFYF SQLCQVSPFL TGHDLKALGY
KPGPQFKQIL TDLLNACLDG ELGDRQQEEA WLRTHYPLPN KV
