ID K9ZWG9_DEIPD Unreviewed; 364 AA.
AC K9ZWG9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=tRNA nucleotidyltransferase/poly(A) polymerase {ECO:0000313|EMBL:AFZ65931.1};
GN OrderedLocusNames=Deipe_0330 {ECO:0000313|EMBL:AFZ65931.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ65931.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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; CP003382; AFZ65931.1; -; Genomic_DNA.
DR RefSeq; WP_015234242.1; NC_019793.1.
DR AlphaFoldDB; K9ZWG9; -.
DR STRING; 937777.Deipe_0330; -.
DR KEGG; dpd:Deipe_0330; -.
DR PATRIC; fig|937777.3.peg.340; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_5_1_0; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000010467; 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:UP000010467};
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 31..150
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
SQ SEQUENCE 364 AA; 39724 MW; 6622BC50799592C7 CRC64;
MNAERAWSAL EQDRQLLSEL AQQAFPARLA VVGGALRDAL LGRPARELDI VLEGASVAEF
ARQSQLPFTY HPRYDNATLR LPDGRFIDLI RTRGERYPSP GAAPEVFPAD LHTDLARRDF
SVNAMALDLR GGELIDPLGG QRDLTHSALR PLHDRSFRDD PSRLARGARL AARLEFDLEA
SGRAQVPDAL RYAPQTRRLC GELALCFQEP FPGKVFERLQ TWGAEHLFGA NATSSLLLLD
ERRASGNAVP ASIYGAVWLA LQPDPAEASR RYGLGEKALR LLARARSEGR FALHTPEDEV
RRALQLPVPL PGLAGADLVA LGVAPGPAVG QALRFLQGLR EAGEVSSAED ERAALKAYLE
SARP
//
