ID A0A0P6WX08_9SPHN Unreviewed; 396 AA.
AC A0A0P6WX08;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polynucleotide adenylyltransferase {ECO:0000313|EMBL:KPL67069.1};
GN ORFNames=SZ64_02535 {ECO:0000313|EMBL:KPL67069.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL67069.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL67069.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL67069.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL67069.1}.
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DR EMBL; JXQC01000003; KPL67069.1; -; Genomic_DNA.
DR RefSeq; WP_054529390.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6WX08; -.
DR STRING; 1603897.SZ64_02535; -.
DR PATRIC; fig|1603897.4.peg.395; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000049978; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KPL67069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 34..156
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 186..243
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 396 AA; 43463 MW; EC4B8AE1D253C12A CRC64;
MAEVLPAAHW TQREDLARLI DALGNGPDGA AQARWVGGAV RDSLLGVEPY DIDAATPLKP
RDVMARLERA GIRTIPTGID HGTVTALLPD GKVELTTLRR DVSTDGRRAT VEYASEWRDD
AARRDFTINA LYVDPRTLEI FDYFGGLDDL AARRVRFIGD ARQRIREDHL RILRYYRFQA
RFGSGLDPEA EEACAELAAT LKGLSRERVA MELLNLLGLP DPTDTLLRMY QREVLGVVLP
EVTQQAIENL PGLIAAEKAA GIAPLAIRRM EALLPPLPTV AEGVAARLRL SRAQRERLSC
VAARQCDDGA DPHALAYRCG LDCAVDRLLL SGSDPAPIMG WAIPELPLKG GEIVRRGVKA
GPDVARILRT VEARWIAEGF PGRERVLDLL ESELPA
//
