RNT_HAEIE
ID RNT_HAEIE Reviewed; 229 AA.
AC A5UAG1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00157};
DE AltName: Full=Exoribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157};
DE Short=RNase T {ECO:0000255|HAMAP-Rule:MF_00157};
GN Name=rnt {ECO:0000255|HAMAP-Rule:MF_00157};
GN OrderedLocusNames=CGSHiEE_01410;
OS Haemophilus influenzae (strain PittEE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374930;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittEE;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- FUNCTION: Trims short 3' overhangs of a variety of RNA species, leaving
CC a one or two nucleotide 3' overhang. Responsible for the end-turnover
CC of tRNA: specifically removes the terminal AMP residue from uncharged
CC tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00157}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00157};
CC Note=Binds two Mg(2+) per subunit. The active form of the enzyme binds
CC two Mg(2+) ions in its active site. The first Mg(2+) forms only one
CC salt bridge with the protein. {ECO:0000255|HAMAP-Rule:MF_00157};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00157}.
CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000255|HAMAP-
CC Rule:MF_00157}.
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DR EMBL; CP000671; ABQ97762.1; -; Genomic_DNA.
DR RefSeq; WP_005686760.1; NC_009566.1.
DR AlphaFoldDB; A5UAG1; -.
DR SMR; A5UAG1; -.
DR KEGG; hip:CGSHiEE_01410; -.
DR HOGENOM; CLU_082724_0_0_6; -.
DR OMA; CYMVNHL; -.
DR GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd06134; RNaseT; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00157; RNase_T; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR005987; RNase_T.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR30231:SF2; PTHR30231:SF2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR01298; RNaseT; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW tRNA processing.
FT CHAIN 1..229
FT /note="Ribonuclease T"
FT /id="PRO_1000011396"
FT DOMAIN 23..197
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 32
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 80
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 127
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 149
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
SQ SEQUENCE 229 AA; 25502 MW; D712291E3281D584 CRC64;
MSDSQEIPYH NQLKNRFRGY FPVIIDVETA GFDAKKDALL ELAAITLKMD ENGYLHPDQK
CHFHIEPFEG ANINPESLKF NGIDIHNPLR GAVSELDAIT GLFQMIRRGQ KDADCQRSII
VAHNAAFDQS FVMAAAERTG VKRNPFHPFG MFDTASLAGL MFGQTVLVKA CLAAKIPFDG
KQAHSALYDT ERTAELFCYM VNHLKDLGGF PHISQIDETE NTAENQTAL
