ID B8E134_DICTD Unreviewed; 845 AA.
AC B8E134;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=CBS domain containing protein {ECO:0000313|EMBL:ACK42771.1};
GN OrderedLocusNames=Dtur_1497 {ECO:0000313|EMBL:ACK42771.1};
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42771.1, ECO:0000313|Proteomes:UP000007719};
RN [1] {ECO:0000313|Proteomes:UP000007719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42771.1; -; Genomic_DNA.
DR RefSeq; WP_012583849.1; NC_011661.1.
DR RefSeq; YP_002353385.1; NC_011661.1.
DR AlphaFoldDB; B8E134; -.
DR STRING; 515635.Dtur_1497; -.
DR EnsemblBacteria; ACK42771; ACK42771; Dtur_1497.
DR KEGG; dtu:Dtur_1497; -.
DR PATRIC; fig|515635.4.peg.1546; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_0; -.
DR InParanoid; B8E134; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000007719; 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; cd04595; CBS_pair_DHH_polyA_Pol_assoc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
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:UP000007719};
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 317..373
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 379..436
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 845 AA; 98133 MW; 31576A38624E9600 CRC64;
MEKVPIILTH TYLDFDALSS LYAAKKLYPK AIAYTSKSME RKVYEFYLLY KDILRFVENP
EINVEIEKII LVDNHWLNRI EKKFHDFIKE KKVPIEIYDH HETGDIKGDI EFIEKTGSTT
TILVEKLIEK RIPIDPIEAT IFLLGIYQDT GNFVFLNTTP KDLRIASYLL ERGADLNIIN
RYIYEKLTDE QKELLNDLLQ ISKEISISGY KIVIAKIERE KYVEGLSIIA HRVLDEKEAD
ILFIILQVKD KIFVMGRSKT QNIDLREVLK DFNPGGHKTA TTIVLNSQET DPNSAENLII
ERLKKHLPRD FLAKDIMSYP VVTISPDISV KEAFKIMMKH GYGGLCVEEN GKLVGIISRR
DIEKAINLKL TKKKVKSFMS KPVITVTPET PIWEIEKILV EKNIGRVPVV DRDKIVGIIT
RQDILRFRFL RSTIYSPLGS IFQISEEKIK SSPWKEILEE LKNLTSQYNI SIYAIGGFVR
DLLLGQSNYD LDIVVEGDIQ LVISKIIDKW QSKVITHPQF GTSEILLNDR KRIDIATARI
EYYEEPGSLP KVERSSLWLD LKRRDFTINA LAMSLNEENF GEIIDLYGGL EDLTRKELRV
LHNLSFIEDP TRILRGVRLE VRLGFNFEEK TFKLLKEAIE NGFLNKIAKE RLKDEIFLIL
QEPQPEKVLK RLEELNALSY ILPVKRLPKN FEKKNQILRR EFPEKLELHI LNIISEADTE
EGKKWLQDLK FPKKVLYQFI LLKKYENTNT LSEKDIKSLL DLPNDLLLLL SLTAKKIGKN
ILRIKLLKEK GVPYLKGEDL INMGFKGKII GDLLKKLFLK HYYGEVKSKE DEEKIIKEFI
NSTQL
//
