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Database: UniProt
Entry: A0A1W1VTD3_DESTI
LinkDB: A0A1W1VTD3_DESTI
Original site: A0A1W1VTD3_DESTI 
ID   A0A1W1VTD3_DESTI        Unreviewed;       449 AA.
AC   A0A1W1VTD3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=tRNA nucleotidyltransferase (CCA-adding enzyme) {ECO:0000313|EMBL:SMB96586.1};
GN   ORFNames=SAMN00017405_2329 {ECO:0000313|EMBL:SMB96586.1};
OS   Desulfonispora thiosulfatigenes DSM 11270.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfonispora.
OX   NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB96586.1, ECO:0000313|Proteomes:UP000192731};
RN   [1] {ECO:0000313|EMBL:SMB96586.1, ECO:0000313|Proteomes:UP000192731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB96586.1,
RC   ECO:0000313|Proteomes:UP000192731};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FWWT01000024; SMB96586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1VTD3; -.
DR   STRING; 656914.SAMN00017405_2329; -.
DR   Proteomes; UP000192731; Unassembled WGS sequence.
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: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; IPR032810; CCA-adding_enz_C.
DR   InterPro; IPR003607; HD/PDEase_dom.
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; 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   Pfam; PF13735; tRNA_NucTran2_2; 1.
DR   SMART; SM00471; HDc; 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   Reference proteome {ECO:0000313|Proteomes:UP000192731};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          247..376
FT                   /note="HD/PDEase"
FT                   /evidence="ECO:0000259|SMART:SM00471"
SQ   SEQUENCE   449 AA;  51590 MW;  13CFC0AF5CA63114 CRC64;
     MGDVMIEIDN SANLILNKLQ SNGYEAYVVG GCVRDSLLKK IPMDWDMCTN ADPLEVIELF
     NEYKVIPTGL KHGTVSIIID SKSYEVTTYR IDGDYLNNRK PDQVFFTNSL REDLSRRDFT
     INSLAYNSHE GLIDFFNGYK DLSEKVIKAV GDADRRYQED ALRMLRAIRF ACQLNFSIED
     LTLKAIKKNA NLLNNISQER IRDEFCKILI SDYPSKGLKL LADSKLLEFI APELIPSLDF
     MQHNPHHDKD VFNHTLAVLE NTPNKLVIRL AALLHDIGKP HTFSLDKNKI GHFYGHQHES
     EKLAKNFLNR LKFDNKTINT VSILVKEHMS WFDKISDKGI KRLITRVGVD NINDLFTLQI
     ADVKGTKPPY DFSKILQVKE RVHKILTKKE PLTIKDLNIT GNDLKQIGIK PSKEMGQIIE
     NLFQRVLEEP KLNYKDKLLE LANNMNKTN
//
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