ID A0A0A7KBC6_9FLAO Unreviewed; 473 AA.
AC A0A0A7KBC6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=tRNA nucleotidyltransferase {ECO:0000313|EMBL:AIZ43441.1};
GN ORFNames=M666_18930 {ECO:0000313|EMBL:AIZ43441.1};
OS Cellulophaga baltica 18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=1348584 {ECO:0000313|EMBL:AIZ43441.1, ECO:0000313|Proteomes:UP000030786};
RN [1] {ECO:0000313|EMBL:AIZ43441.1, ECO:0000313|Proteomes:UP000030786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18 {ECO:0000313|EMBL:AIZ43441.1,
RC ECO:0000313|Proteomes:UP000030786};
RX PubMed=24428166; DOI=10.1111/1462-2920.12391;
RA Holmfeldt K., Howard-Varona C., Solonenko N., Sullivan M.B.;
RT "Contrasting genomic patterns and infection strategies of two co-existing
RT Bacteroidetes podovirus genera.";
RL Environ. Microbiol. 16:2501-2513(2014).
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}.
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DR EMBL; CP009976; AIZ43441.1; -; Genomic_DNA.
DR RefSeq; WP_029445600.1; NZ_CP009976.1.
DR AlphaFoldDB; A0A0A7KBC6; -.
DR STRING; 1348584.M666_18930; -.
DR GeneID; 78062781; -.
DR KEGG; cbat:M666_18930; -.
DR HOGENOM; CLU_015961_6_1_10; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000030786; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 1.10.246.80; -; 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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR NCBIfam; TIGR00277; HDIG; 1.
DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR Pfam; PF01966; HD; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 29..158
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 185..245
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 264..348
FT /note="HD"
FT /evidence="ECO:0000259|Pfam:PF01966"
SQ SEQUENCE 473 AA; 53973 MW; DEBFED2B420306BC CRC64;
MTQTNHEQAL TNPVFKVISN AAKELNLDCY VIGGFVRDYL LERGTAKDID IVAIGSGIAL
AKKVASKLKG KPEVSVFKNF GTAMIKHGDL ELEFVGARKE SYHEDSRKPV VEDGTLEDDQ
KRRDFTINAL AISLNEENYA TLLDPFKGIQ DLSDKIIRTP LAPGITYSDD PLRMMRSIRF
ATQLDFKIEE ASLNAITEHK DRIKIISKER IVDELHKILA SKTPSLGFSL LHKTELLGYI
LPELTALQGI EEIEGQRHKD NFWHTLEVVD NIAKNTDNVW LRWAALLHDI GKAPTKRFDK
KIGWTFHSHE FIGSKMVYKL FKRLRMPLND KMKFVQKMVL LSSRPIILSE DFATDSAVRR
LIFDAGENIE DLMTLCEADI TTKNPKKQKR YQNNFKLVRQ KIVEVEERDH VRNFQPPISG
EEIMETFNLK PSKEIGIIKE AIKEAILEGE IPNEYDAAYQ FMLQKGSEIG LES
//
