AATNT_GEOSL
ID AATNT_GEOSL Reviewed; 880 AA.
AC Q74CU0;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=A-adding tRNA nucleotidyltransferase {ECO:0000303|PubMed:18952795};
DE Short=A-adding TNT {ECO:0000303|PubMed:18952795};
DE EC=2.7.7.- {ECO:0000269|PubMed:18952795};
DE AltName: Full=A-adding enzyme {ECO:0000305};
DE AltName: Full=NTSFIII {ECO:0000303|PubMed:18952795};
GN OrderedLocusNames=GSU1581 {ECO:0000312|EMBL:AAR34955.1};
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 terminal adenosine residue to tRNA.
CC {ECO:0000269|PubMed:18952795}.
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:18952795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60013;
CC Evidence={ECO:0000269|PubMed:18952795};
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; AE017180; AAR34955.1; -; Genomic_DNA.
DR RefSeq; NP_952632.1; NC_002939.5.
DR RefSeq; WP_010942226.1; NC_002939.5.
DR AlphaFoldDB; Q74CU0; -.
DR SMR; Q74CU0; -.
DR STRING; 243231.GSU1581; -.
DR EnsemblBacteria; AAR34955; AAR34955; GSU1581.
DR KEGG; gsu:GSU1581; -.
DR PATRIC; fig|243231.5.peg.1622; -.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR eggNOG; COG3620; Bacteria.
DR HOGENOM; CLU_015961_5_0_7; -.
DR InParanoid; Q74CU0; -.
DR OMA; ILCHTTA; -.
DR Proteomes; UP000000577; 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: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; 3.10.580.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 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..880
FT /note="A-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447566"
FT DOMAIN 315..373
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 377..435
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 487..490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 574..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 619..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
SQ SEQUENCE 880 AA; 98394 MW; A12E9EE5DF87750F CRC64;
MDVITTHVNA DFDCLGAMVA ASKLYPDALM VFSGSQEKSM RDLFLKTTGY ALPFTRLRDV
DFSDITRLVL VDCQHTSRIG RFAEVARRPG VEVHIYDHHP GSSGDIRPSG GEIRDCGSST
TILTRKLMEQ GIEVTAVEAT LMMLGIYEDT GNLTFPSTTP EDYAAASWLL ERGANLNIVS
DFVSQELTAE QVALLNDLLK SLRSTPVNGV DIAVAHATLD HYVGDIAVLA HMMRDMQNLD
AIFLVVGMGE RVYLVARSRI AEVDAGAVMR VFGGGGHATA AAATVRDQTV IQVLGRLNRL
LPELVNPVRT AADLMSSPVI TLPLATTITE AREILTRYNV NAMPVMDGER MAGIISRRIV
EKALYHGLGN LPVDEYMHTE FLRAAPDTPI NAIQDYIVGQ HRRLVPVFSG ERLVGVITRT
DLLRYMYTGT QRNAEPVYDL GSENLPVRRR EVVHLMNRHL PRPTVAMLRD LGKVGDELEL
PVYAVGGFVR DLLLGAENDD IDVSVEGDGI LFAETVANRV GCRVKSHAKF GTAVIVFPDG
LKVDVASTRL EYYETPGALP TVERSSLKMD LYRRDFTINT LAVKLNAEGF GTLIDYFGAY
RDLQEKTIRV LHNLSFVEDP TRVFRAIRFE QRLGFPISRH TENLIKNAVK MGFLDKLGGR
RLLNELVLIL REREPVKAIL RMSGLGLLRF IHPDLVLAPN TLQVLDEVKK VITWFDLLYL
GEKVETWVVY FLALTSSLPD EGFWGTCTRL SVSEHYREKL IDMRVHGEQV LEVMTRKAAR
REDVRRSDIY FWLRGLSPEV LLYIMAKTRS DEVRRYVSLY VTQLRGIVTH ITGDDLKTLG
IPSGPRYREI LDRVLTARLN GEAATRDDEM RIAVRLADSA
