ID S9QXX5_9RHOB Unreviewed; 294 AA.
AC S9QXX5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=tRNA nucleotidyltransferase/poly(A) polymerase {ECO:0000313|EMBL:EPX84462.1};
DE EC=2.7.7.72 {ECO:0000313|EMBL:EPX84462.1};
DE EC=3.1.3.- {ECO:0000313|EMBL:EPX84462.1};
DE EC=3.1.4.- {ECO:0000313|EMBL:EPX84462.1};
GN ORFNames=ruthe_02266 {ECO:0000313|EMBL:EPX84462.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX84462.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX84462.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX84462.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|RuleBase:RU003953}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPX84462.1}.
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DR EMBL; AOLV01000025; EPX84462.1; -; Genomic_DNA.
DR AlphaFoldDB; S9QXX5; -.
DR STRING; 1123069.ruthe_02266; -.
DR PATRIC; fig|1123069.3.peg.2241; -.
DR HOGENOM; CLU_946233_0_0_5; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EPX84462.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EPX84462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 33..155
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 188..243
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 294 AA; 30763 MW; 6720545B03D1E5B7 CRC64;
MTDPRHAPLL APLLADPAAR AVLDLLAGAG HRAWIVGGAV RDALMGRPTG DLDIATDAAP
ETVLTLAGGA GIGAVPTGLA HGTVTLLPQG RPVEVTTLRR DVETFGRHAR VAFGASPEED
ARRRDFTLNA LYLAPDGTLL DPVGGLPDLA ARRIRFVGDP ATRIREDHLR TLRYFRFHAT
HGDPAEGLDP DALDAVARHL EGLESLSRER VGAEMRKLLA APDPAPAVAA MRATGVLQRV
LPGAGDGLLA PLVHVEGEAG LPPDPLRRLA ALGGRMQPRG CACRGPRQDG SGAI
//