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Database: UniProt
Entry: A0A1A7KKP6_9FLAO
LinkDB: A0A1A7KKP6_9FLAO
Original site: A0A1A7KKP6_9FLAO 
ID   A0A1A7KKP6_9FLAO        Unreviewed;       304 AA.
AC   A0A1A7KKP6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Ribonuclease Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE            Short=RNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE            EC=3.1.26.11 {ECO:0000256|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNA 3 endonuclease {ECO:0000256|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
GN   Name=rbn {ECO:0000313|EMBL:OBW42712.1};
GN   Synonyms=rnz {ECO:0000256|HAMAP-Rule:MF_01818};
GN   ORFNames=AB670_00925 {ECO:0000313|EMBL:OBW42712.1};
OS   Chryseobacterium sp. MOF25P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1664318 {ECO:0000313|EMBL:OBW42712.1, ECO:0000313|Proteomes:UP000092708};
RN   [1] {ECO:0000313|EMBL:OBW42712.1, ECO:0000313|Proteomes:UP000092708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOF25P {ECO:0000313|EMBL:OBW42712.1,
RC   ECO:0000313|Proteomes:UP000092708};
RA   David V.-J., Thomas B., Ramon P.Y., Thao N., David R., Richard E.,
RA   Roderick C., Nikki M., Timothy W.J., Alexander A.E., Kimberley T.;
RT   "A floR containing integrative conjugative element found in multidrug
RT   resistant Chryseobacterium spp. isolates: exception to the general rule?";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA maturation,
CC       by removing a 3'-trailer from precursor tRNA. {ECO:0000256|HAMAP-
CC       Rule:MF_01818}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC         from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC         group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC         at the trailer molecule.; EC=3.1.26.11; Evidence={ECO:0000256|HAMAP-
CC         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. {ECO:0000256|HAMAP-
CC       Rule:MF_01818}.
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:OBW42712.1}.
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DR   EMBL; LFEG01000030; OBW42712.1; -; Genomic_DNA.
DR   RefSeq; WP_066676286.1; NZ_LFEG01000030.1.
DR   AlphaFoldDB; A0A1A7KKP6; -.
DR   PATRIC; fig|1664318.4.peg.948; -.
DR   OrthoDB; 9800940at2; -.
DR   Proteomes; UP000092708; Unassembled WGS sequence.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; 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; PF12706; Lactamase_B_2; 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   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:UP000092708};
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          33..152
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
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         142
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         213
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         213
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         271
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   304 AA;  34560 MW;  F7415FDFA2122F00 CRC64;
     MSTYLTILGF NSAIPTINTS PTAQLLEMEE RCFLIDCGEG TQVQLRKAKA RFSKINHIFI
     SHLHGDHCFG LPGLIASFRL LGRETPLHVY GPKGIKKMLE TIFSITETHR GFELVYHELG
     KDYSEKIYED NRVEVFTIPL DHRIYCNGYL FKEKPKERHI NMEEVSKYSE IETCDYHNLK
     AGKDFVLSDG YVLKNEILTT TPAPSVSYAF CSDTRYLESV IPIIKNVTVL YHESTFLHDL
     KEMADYTGHA TALEAATIAK KAEVGKLILG HFSNRYGDLT VFTDEARTVF PNSYLPKALE
     CVKI
//
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