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Database: UniProt
Entry: F6B536_DESCC
LinkDB: F6B536_DESCC
Original site: F6B536_DESCC 
ID   F6B536_DESCC            Unreviewed;       472 AA.
AC   F6B536;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Polynucleotide adenylyltransferase/metal dependent phosphohydrolase {ECO:0000313|EMBL:AEF93055.1};
GN   OrderedLocusNames=Desca_0151 {ECO:0000313|EMBL:AEF93055.1};
OS   Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS   (Desulfotomaculum carboxydivorans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF93055.1, ECO:0000313|Proteomes:UP000009226};
RN   [1] {ECO:0000313|Proteomes:UP000009226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC   {ECO:0000313|Proteomes:UP000009226};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA   Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT   "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL   Submitted (MAY-2011) 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; CP002736; AEF93055.1; -; Genomic_DNA.
DR   RefSeq; WP_013809454.1; NC_015565.1.
DR   AlphaFoldDB; F6B536; -.
DR   STRING; 868595.Desca_0151; -.
DR   KEGG; dca:Desca_0151; -.
DR   eggNOG; COG0617; Bacteria.
DR   HOGENOM; CLU_015961_6_2_9; -.
DR   Proteomes; UP000009226; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
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; 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:SF2; CC-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 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   Hydrolase {ECO:0000313|EMBL:AEF93055.1};
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   ECO:0000313|EMBL:AEF93055.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009226};
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};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          243..393
FT                   /note="HD/PDEase"
FT                   /evidence="ECO:0000259|SMART:SM00471"
SQ   SEQUENCE   472 AA;  53456 MW;  44011F92B33DFC7A CRC64;
     MWNLLKMVAQ QAADLGTDVY LVGGAVRDLL WGLRPRDLDL AVANGALDLA RRMADRHRGT
     LVVLDGQRQM ARVVFKQDYQ LDFSPFKGAH IEGDLRARDF TINAMALHLN SLCSSKNCTS
     PADQGWRSFL VDPTGGKRDL QLGLLQATGN EALLDDPLRV IRGVRLAAQF NLSITPETVV
     LMRQGARRIE QVAGERIWQE LGQALTLPHV HHWVEFMDRE LNLWQYLLPG RLRMEATEQN
     YYHVENVWRH CLRTFGCLEI VLKKYQFYHH LAGGATGPAV FKLAALLHDV GKPDTAKIRP
     DGRISFYGHA QAGVPYAEAL ADRLRLSGME RQYLVTLIRH HMQPLHYFLN KGYSDLKVFR
     LFRLLEGSFL DILILSLADV TATYTASERL SELTAYREYI LKLIHRYEHE PEFFHPAKLL
     SGKDLIALGV PEGPLVGKFL ARLAEMQITG AVTDLHSAKQ WVIAELKNIT PQ
//
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