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Database: UniProt
Entry: A0A0N1C198_9SPHN
LinkDB: A0A0N1C198_9SPHN
Original site: A0A0N1C198_9SPHN 
ID   A0A0N1C198_9SPHN        Unreviewed;       397 AA.
AC   A0A0N1C198;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Polynucleotide adenylyltransferase {ECO:0000313|EMBL:KPF89223.1};
GN   ORFNames=IP83_02845 {ECO:0000313|EMBL:KPF89223.1};
OS   Novosphingobium sp. AAP93.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF89223.1, ECO:0000313|Proteomes:UP000037906};
RN   [1] {ECO:0000313|EMBL:KPF89223.1, ECO:0000313|Proteomes:UP000037906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP93 {ECO:0000313|EMBL:KPF89223.1,
RC   ECO:0000313|Proteomes:UP000037906};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPF89223.1}.
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DR   EMBL; LJHZ01000016; KPF89223.1; -; Genomic_DNA.
DR   RefSeq; WP_054120698.1; NZ_LJHZ01000016.1.
DR   AlphaFoldDB; A0A0N1C198; -.
DR   STRING; 1523427.IP83_02845; -.
DR   PATRIC; fig|1523427.4.peg.1163; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000037906; 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:KPF89223.1}; 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          190..244
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   397 AA;  42594 MW;  1392A8A0140DC96F CRC64;
     MADARLPAAD WTQREDLASL VAALDPHGKG LVRYVGGAVR DTLLGIAVKD IDMATPLEPP
     AVIEHLAAAG IRSVPTGLAH GTVTAVLEGG PVEITTLRRD VATDGRHATV AFSQCWQEDA
     ARRDFTINAL YADPRDLTVH DYFGGLDDLD ARRLRFIGDA EQRIREDYLR ILRYFRFQAR
     FGSLPADATA EAACSALAPG LKGLSRERIA SELLLLLALP NPAPTVSRMA ELGVLAVILP
     EADPAALPPL VTAEQAQAIV PEPLRRLAAL LPAEPALAEQ VGARLRLSIA QRKHLATVAA
     RTVPEEAARP LAYRVGREAA RDRLLITGGD ITPLAGWDIP QFPLKGGMIV ARGITAGPEV
     ARILRTVEAQ WVEEKFPDEA RVMALLDAEI AGRSGPV
//
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