RNSE_THET8
ID RNSE_THET8 Reviewed; 431 AA.
AC Q5SLP1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ribonuclease TTHA0252;
DE EC=3.1.-.-;
GN OrderedLocusNames=TTHA0252;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, COFACTOR, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=16945939; DOI=10.1093/jb/mvj183;
RA Ishikawa H., Nakagawa N., Kuramitsu S., Masui R.;
RT "Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA
RT degradation protein of the metallo-beta-lactamase superfamily.";
RL J. Biochem. 140:535-542(2006).
CC -!- FUNCTION: Has endoribonuclease activity towards 23S and 16S rRNA (in
CC vitro). {ECO:0000269|PubMed:16945939}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16945939};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:16945939};
CC -!- ACTIVITY REGULATION: Inhibited by cadmium, cobalt, manganese,
CC magnesium, calcium and nickel ions. {ECO:0000269|PubMed:16945939}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16945939}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. {ECO:0000305}.
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DR EMBL; AP008226; BAD70075.1; -; Genomic_DNA.
DR RefSeq; WP_011227806.1; NC_006461.1.
DR RefSeq; YP_143518.1; NC_006461.1.
DR PDB; 2DKF; X-ray; 2.80 A; A/B/C/D=1-431.
DR PDB; 3A4Y; X-ray; 2.50 A; A/B/C/D=1-431.
DR PDB; 3IDZ; X-ray; 2.50 A; A/B/C/D=1-431.
DR PDB; 3IE0; X-ray; 2.73 A; A/B/C/D=1-431.
DR PDB; 3IE1; X-ray; 2.85 A; A/B/C/D=1-431.
DR PDB; 3IE2; X-ray; 2.80 A; A/B/C/D=1-431.
DR PDB; 3IEK; X-ray; 2.05 A; A/B/C/D=1-431.
DR PDB; 3IEL; X-ray; 2.35 A; A/B/C/D=1-431.
DR PDB; 3IEM; X-ray; 2.50 A; A/B/C/D=1-431.
DR PDBsum; 2DKF; -.
DR PDBsum; 3A4Y; -.
DR PDBsum; 3IDZ; -.
DR PDBsum; 3IE0; -.
DR PDBsum; 3IE1; -.
DR PDBsum; 3IE2; -.
DR PDBsum; 3IEK; -.
DR PDBsum; 3IEL; -.
DR PDBsum; 3IEM; -.
DR AlphaFoldDB; Q5SLP1; -.
DR SMR; Q5SLP1; -.
DR STRING; 300852.55771634; -.
DR EnsemblBacteria; BAD70075; BAD70075; BAD70075.
DR GeneID; 3170139; -.
DR KEGG; ttj:TTHA0252; -.
DR PATRIC; fig|300852.9.peg.252; -.
DR eggNOG; COG1236; Bacteria.
DR HOGENOM; CLU_009673_5_0_0; -.
DR OMA; YLDGMIW; -.
DR PhylomeDB; Q5SLP1; -.
DR EvolutionaryTrace; Q5SLP1; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..431
FT /note="Ribonuclease TTHA0252"
FT /id="PRO_0000319322"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:3IEK"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:3IEK"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:3IEK"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:3IEK"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:3IEK"
SQ SEQUENCE 431 AA; 47055 MW; 89BB88D1F61D4BFC CRC64;
MRIVPFGAAR EVTGSAHLLL AGGRRVLLDC GMFQGKEEAR NHAPFGFDPK EVDAVLLTHA
HLDHVGRLPK LFREGYRGPV YATRATVLLM EIVLEDALKV MDEPFFGPED VEEALGHLRP
LEYGEWLRLG ALSLAFGQAG HLPGSAFVVA QGEGRTLVYS GDLGNREKDV LPDPSLPPLA
DLVLAEGTYG DRPHRPYRET VREFLEILEK TLSQGGKVLI PTFAVERAQE ILYVLYTHGH
RLPRAPIYLD SPMAGRVLSL YPRLVRYFSE EVQAHFLQGK NPFRPAGLEV VEHTEASKAL
NRAPGPMVVL AGSGMLAGGR ILHHLKHGLS DPRNALVFVG YQPQGGLGAE IIARPPAVRI
LGEEVPLRAS VHTLGGFSGH AGQDELLDWL QGEPRVVLVH GEEEKLLALG KLLALRGQEV
SLARFGEGVP V
