(data stored in SCRATCH zone)

SWISSPROT: A0LFD7_SYNFM

ID   A0LFD7_SYNFM            Unreviewed;       299 AA.
AC   A0LFD7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=rnz {ECO:0000256|HAMAP-Rule:MF_01818};
GN   OrderedLocusNames=Sfum_0439 {ECO:0000313|EMBL:ABK16139.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16139.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16139.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA
CC       maturation, by removing a 3'-trailer from precursor tRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01818}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing extra 3'
CC         nucleotides from tRNA precursor, generating 3' termini of tRNAs.
CC         A 3'-hydroxy group is left at the tRNA terminus and a 5'-
CC         phosphoryl group is left at the trailer molecule.; EC=3.1.26.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01818};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000256|HAMAP-
CC       Rule:MF_01818}.
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DR   EMBL; CP000478; ABK16139.1; -; Genomic_DNA.
DR   RefSeq; WP_011697312.1; NC_008554.1.
DR   STRING; 335543.Sfum_0439; -.
DR   EnsemblBacteria; ABK16139; ABK16139; Sfum_0439.
DR   KEGG; sfu:Sfum_0439; -.
DR   eggNOG; ENOG4105IES; Bacteria.
DR   eggNOG; COG1234; LUCA.
DR   HOGENOM; HOG000272419; -.
DR   KO; K00784; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   BioCyc; SFUM335543:G1G7I-446-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
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; -; 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   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFD7.
DR   SWISS-2DPAGE; A0LFD7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01818,
KW   ECO:0000313|EMBL:ABK16139.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01818}.
FT   DOMAIN       21    261       Lactamase_B. {ECO:0000259|Pfam:PF12706}.
FT   ACT_SITE     54     54       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01818}.
FT   METAL        50     50       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        52     52       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        54     54       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        55     55       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       131    131       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       202    202       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       202    202       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       260    260       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
SQ   SEQUENCE   299 AA;  33549 MW;  3BDB733B7B4FCA04 CRC64;
     MMPMPGRYLA SMAVRLDGRL YLFDAGEGTQ LAWKTCRIGL RGLSVVAVTH LHADHCLGIP
     GLMMLKAQLD DPEPLTVMGP PGIREFILEN HRILDFHLNY PLEFIEWSAD APDWKAYEDE
     LLRIFWEPLE HTRFCLGYRV EELERPGRFH PDAADALDIP EGPLRGRLQR GESVTLPSGT
     VVAAHQVSGP PRRGRHLAYV VDTRPTPAIQ RLCQGADLAF IEGMFLPEHA EQARAKGHLT
     VVEAARAARK AGARRAVLIH ISPRYGEEDL DRLERAAREH FQDAVVGRDL QVYSVPLPD
//

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