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SYNY3:PNP
Contents
Species (Taxon ID) | Synechocystis sp. (strain PCC 6803 / Kazusa). (1111708) | |
Gene Name(s) | pnp (ECO:0000255 with HAMAP-Rule:MF_01595) | |
Protein Name(s) | Polyribonucleotide nucleotidyltransferase (ECO:0000255 with HAMAP-Rule:MF_01595)
Polynucleotide phosphorylase (ECO:0000255 with HAMAP-Rule:MF_01595) PNPase (ECO:0000255 with HAMAP-Rule:MF_01595) | |
External Links | ||
UniProt | P72659 | |
EMBL | BA000022 | |
PIR | S74509 | |
RefSeq | NP_439981.1 YP_005650036.1 YP_007449864.1 | |
ProteinModelPortal | P72659 | |
IntAct | P72659 | |
STRING | 1148.sll1043 | |
PaxDb | P72659 | |
EnsemblBacteria | BAA16661 | |
GeneID | 953146 | |
KEGG | syn:sll1043 | |
PATRIC | 23837032 | |
eggNOG | COG1185 | |
HOGENOM | HOG000218326 | |
InParanoid | P72659 | |
KO | K00962 | |
OMA | RFMFHYN | |
OrthoDB | EOG6WT8CC | |
PhylomeDB | P72659 | |
Proteomes | UP000001425 | |
GO | GO:0005737 GO:0000175 GO:0000287 GO:0004654 GO:0003723 GO:0006402 GO:0006396 | |
Gene3D | 1.10.10.400 2.40.50.140 3.30.1370.10 3.30.230.70 | |
HAMAP | MF_01595 | |
InterPro | IPR001247 IPR015847 IPR004087 IPR004088 IPR012340 IPR012162 IPR027408 IPR015848 IPR003029 IPR020568 IPR022967 | |
PANTHER | PTHR11252 | |
Pfam | PF00013 PF03726 PF01138 PF03725 PF00575 | |
PIRSF | PIRSF005499 | |
SMART | SM00322 SM00316 | |
SUPFAM | SSF50249 SSF54211 SSF54791 SSF55666 | |
TIGRFAMs | TIGR03591 | |
PROSITE | PS50084 PS50126 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0000175 |
3'-5'-exoribonuclease activity |
ECO:0000314 |
F |
Figure 5: Using exoribonucleolytic activity assays, compares SynRNB of Synechocystis to RNase II and RNase R of E. coli. The ability of these proteins to degrade three synthetic substrates, a poly(A) oligomer of 30nts, a 16-mer oligoribonucleotide, and a 30-mer oligoribonucleotide, were analyzed and compared according to time. |
complete | |||||
involved_in |
GO:0006401 |
RNA catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000134193 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10743 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10743 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0000175 |
3'-5'-exoribonuclease activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10743 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090503 |
RNA phosphodiester bond hydrolysis, exonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0000175 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0003676 |
nucleic acid binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003723 |
RNA binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR004088 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006396 |
RNA processing |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006402 |
mRNA catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001279 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003723 |
RNA binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001279 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001279 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006402 |
mRNA catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001279 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001279 |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016779 |
nucleotidyltransferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003723 |
RNA binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Matos, RG et al. (2012) The rnb gene of Synechocystis PCC6803 encodes a RNA hydrolase displaying RNase II and not RNase R enzymatic properties. PLoS ONE 7 e32690 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page