Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.13.2 - exoribonuclease H

for references in articles please use BRENDA:EC3.1.13.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.2 exoribonuclease H
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: P33334 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Synonyms
rnase h, rnase h1, rnase hi, rnaseh, rt rnase h, hiv rnase h, t4 rnase h, rt/rnase h, lc11-rnase h1, retroviral rnase h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RNase H
domain of pre-mRNA-splicing factor 8, scPrp8
retroviral reverse transcriptase RNaseH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9050-76-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRP8_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2413
0
279504
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1853A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
D1853N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
E1960K
mutant of prp8-101
K1864E
prp8-D143, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D
prp8-151, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D/S1970R
prp8-152, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
R1937A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
R1937K
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1855A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1936A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1982A
prp8-153, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A, SA1966/7AG
prp8-154, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A,V1987A
prp8-155, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
V1870N
prp8-162, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pena, V.; Rozov, A.; Fabrizio, P.; Luehrmann, R.; Wahl, M.C.
Structure and function of an RNase H domain at the heart of the spliceosome
EMBO J.
27
2929-2940
2008
Saccharomyces cerevisiae (P33334), Saccharomyces cerevisiae
Manually annotated by BRENDA team