ID U3TZ06_9ENTR Unreviewed; 303 AA.
AC U3TZ06;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Ribonuclease BN {ECO:0000256|HAMAP-Rule:MF_01818};
DE Short=RNase BN {ECO:0000256|HAMAP-Rule:MF_01818};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01818};
DE AltName: Full=Ribonuclease Z homolog {ECO:0000256|HAMAP-Rule:MF_01818};
DE Short=RNase Z homolog {ECO:0000256|HAMAP-Rule:MF_01818};
GN Name=rbn {ECO:0000256|HAMAP-Rule:MF_01818};
GN ORFNames=E05_43440 {ECO:0000313|EMBL:BAN99110.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN99110.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN99110.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
CC -!- FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and
CC endoribonuclease activities. {ECO:0000256|HAMAP-Rule:MF_01818}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01818};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_01818};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01818}.
CC -!- SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01818}.
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DR EMBL; AP012551; BAN99110.1; -; Genomic_DNA.
DR AlphaFoldDB; U3TZ06; -.
DR KEGG; psts:E05_43440; -.
DR eggNOG; COG1234; Bacteria.
DR HOGENOM; CLU_031317_2_0_6; -.
DR Proteomes; UP000016901; Chromosome.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016891; F:RNA endonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01818; RNase_Z_BN; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR013471; RNase_Z/BN.
DR NCBIfam; TIGR02651; RNase_Z; 1.
DR PANTHER; PTHR46018; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR PANTHER; PTHR46018:SF2; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01818};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01818};
KW Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01818}.
FT DOMAIN 18..194
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
SQ SEQUENCE 303 AA; 32961 MW; F088C07C02FDCB29 CRC64;
MHLTFLGTGA GAPSLQRNVT AIALTLSKRG ETWLFDCGEA TQHQFMRSAL KPGKLEKIFI
THLHGDHIFG LPGLLTSRSI AGLTEPVTLY GPKGLRQFVD TALSLSGSYT GYPLEIVEIE
AGPVLDNGEF RVIAYALNHV VECYGYRIEQ HDKPGFLDAP RLKAEGVPRG PWYQDLKQGK
RITLEDGREI NGADYLGPAT KGKVLAIFGD TGPTEVALQL AANADVMVHE TTLEAAMVEK
ANGRGHSTTV QAASVAQRAG AKRMIATHFS SRYLSQDRER LLAECQSVFP ATELAHDFAI
FEV
//
