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Database: UniProt
Entry: Q1J0Y1_DEIGD
LinkDB: Q1J0Y1_DEIGD
Original site: Q1J0Y1_DEIGD 
ID   Q1J0Y1_DEIGD            Unreviewed;       377 AA.
AC   Q1J0Y1;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=tRNA nucleotidyltransferase, Cca {ECO:0000313|EMBL:ABF44853.1};
GN   OrderedLocusNames=Dgeo_0551 {ECO:0000313|EMBL:ABF44853.1};
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF44853.1, ECO:0000313|Proteomes:UP000002431};
RN   [1] {ECO:0000313|Proteomes:UP000002431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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|ARBA:ARBA00007265,
CC       ECO:0000256|RuleBase:RU003953}.
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DR   EMBL; CP000359; ABF44853.1; -; Genomic_DNA.
DR   RefSeq; WP_011529695.1; NC_008025.1.
DR   AlphaFoldDB; Q1J0Y1; -.
DR   STRING; 319795.Dgeo_0551; -.
DR   KEGG; dge:Dgeo_0551; -.
DR   eggNOG; COG0617; Bacteria.
DR   HOGENOM; CLU_015961_5_1_0; -.
DR   Proteomes; UP000002431; 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:0000049; F:tRNA 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   PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR   Pfam; PF01743; PolyA_pol; 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   Reference proteome {ECO:0000313|Proteomes:UP000002431};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          39..161
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
SQ   SEQUENCE   377 AA;  39598 MW;  BB2B2A72EF851767 CRC64;
     MDSTAQDPTG QAWQRLLVAD RRWLTDLAQR AGPGTRLALV GGAVRDALLG KTPLDLDVVV
     EGTDAGKLAA ATGLPFLVHP AFGNATVTLP DGRHVDLVRA RRETYPVPGG NPVPAPGTLA
     DDLQRRDFGL NALALPIGPD GPGPLLDEVN GLDDLRKRAL RPLHPRSLYE DASRLVRGAR
     LAGRLDLSAH PELLRQVPDA LEQADTTPRL RAELRLLLHE PRPGRAARML EAWGAASLLP
     PGTATRLEAL DAQQDAGQPV PAQAYAAALL SAAPDPTALA ARLGLGEKPG GLLARALSDT
     PTSPGSAEAV LRSLLRPDAY PPLSGRDVLA LGVPPGPAVG QALAHLATLR RAGQVHSPEE
     ERAALRAYLQ DAATAQR
//
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