ID A0A2T6AUV7_9RHOB Unreviewed; 380 AA.
AC A0A2T6AUV7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Poly(A) polymerase {ECO:0000313|EMBL:PTX47594.1};
GN ORFNames=C8N34_11283 {ECO:0000313|EMBL:PTX47594.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX47594.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX47594.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX47594.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX47594.1}.
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DR EMBL; QBKP01000012; PTX47594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6AUV7; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000244224; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 29..149
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 182..239
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 380 AA; 40409 MW; 1BCAA5A76BCDFE7E CRC64;
MRITGPWIDA PETQGVCAAL TGAGAQALFV GGCVRNALLG AAVNDIDIAT DAQPETVVRL
CEAAGFRVVP TGIDHGTVTV VAKGVPHEVT TFRRDVETDG RRATVAFSSD VAEDAARRDF
TMNALYAAPD GQVIDPLGGL PDLLARRLRF VGEPEQRIRE DYLRILRFFR FHAWYGDPAQ
GIDADGLAAC AVLAEGLETL SAERVGAEMR KLLAAPDPAP SVAAMAQAGI LQRVLPGADP
TALAPLVHLE AGIPPRWMRR LAVLGGEAVD DRWRLSRAES RDLALLLPAV REGGSAAVLG
YRLKALAADA ILARAAMLGH PPGRGWQAEV ARGAAAVMPV RPADLMPQYQ GAELGARLKA
IEARWLQSDL RLDRTALLSP
//
