ID A0A432Z8I0_9GAMM Unreviewed; 210 AA.
AC A0A432Z8I0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Ribonuclease T {ECO:0000256|HAMAP-Rule:MF_00157};
DE EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_00157};
DE AltName: Full=Exoribonuclease T {ECO:0000256|HAMAP-Rule:MF_00157};
DE Short=RNase T {ECO:0000256|HAMAP-Rule:MF_00157};
GN Name=rnt {ECO:0000256|HAMAP-Rule:MF_00157};
GN ORFNames=CWI80_01995 {ECO:0000313|EMBL:RUO74150.1};
OS Pseudidiomarina sediminum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=431675 {ECO:0000313|EMBL:RUO74150.1, ECO:0000313|Proteomes:UP000287022};
RN [1] {ECO:0000313|EMBL:RUO74150.1, ECO:0000313|Proteomes:UP000287022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c121 {ECO:0000313|Proteomes:UP000287022};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:0000256|HAMAP-Rule:MF_00157}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00157};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00157}.
CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000256|HAMAP-
CC Rule:MF_00157}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUO74150.1}.
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DR EMBL; PIQE01000001; RUO74150.1; -; Genomic_DNA.
DR RefSeq; WP_026861987.1; NZ_PIQE01000001.1.
DR AlphaFoldDB; A0A432Z8I0; -.
DR STRING; 1122124.GCA_000423165_00999; -.
DR Proteomes; UP000287022; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016896; F:RNA exonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
DR GO; GO:0006259; P:DNA metabolic process; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd06134; RNaseT; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 NCBIfam; TIGR01298; RNaseT; 1.
DR PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR PANTHER; PTHR30231:SF2; RIBONUCLEASE T; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00157}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00157};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00157};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00157};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00157};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00157}.
FT DOMAIN 17..202
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 180
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 28
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 76
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 123
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 145
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
SQ SEQUENCE 210 AA; 23245 MW; 1CC87521571726D9 CRC64;
MSEQDVSLMK QRFRGYLPVV IDVETAGFNA KTDALLEVAA VTLAFDEQGW LHPDQTFHYH
VEPFEGANLE PAALEFNGID PNSPLRGAVP EGEALKEIFK PIRKAQKDAG CQRSILVGHN
ATFDHGFVMA AAERANLKRN PFHPFVTFDT AALAALTLGQ TVLIKACQEA GIAFDSRQAH
SALYDTERTA ELFCWMVNRY KNLGGWPLVK
//
