UniProtKB - P77766 (RNAAM_ECOLI)
Protein
5'-3' exoribonuclease
Gene
yciV
Organism
Escherichia coli (strain K12)
Status
Functioni
Efficiently catalyzes the hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and DNA, with no specificity toward the identity of the nucleotide base. Is more efficient at hydrolyzing RNA oligonucleotides than DNA oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency approximately 10-fold lower than that of the corresponding single-stranded oligonucleotides.1 Publication
Miscellaneous
Since E.coli possesses another enzyme, CysQ, which has been demonstrated to catalyze the hydrolysis of 3',5'-pAp to 5'-AMP and phosphate during sulfur assimilation, it seems therefore unlikely that the hydrolysis of 3',5'-bis-phosphonucleotides will be the primary physiological function of YciV.1 Publication
Catalytic activityi
- EC:3.1.3.971 Publication
Cofactori
Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit (PubMed:25871919). However, the sequence similarity to CV_1693 from C.violaceum tends to indicate a trinuclear metal center.Curated1 Publication
Kineticsi
kcat is 9.9 sec(-1) with pAp as substrate. kcat is 5.6 sec(-1) with 2'-deoxy-pAp as substrate. kcat is 6.0 sec(-1) with pCp (2'5'/3'5' mixture) as substrate. kcat is 1.9 sec(-1) with 2'-deoxy-pCp as substrate. kcat is 5.5 sec(-1) with pGp (2'5'/3'5' mixture) as substrate. kcat is 1.7 sec(-1) with 2'-deoxy-pGp as substrate. kcat is 4.7 sec(-1) with pUp as substrate. kcat is 2.1 sec(-1) with 2'-deoxy-pUp as substrate. kcat is 1.6 sec(-1) with 2'-deoxy-pTp as substrate. kcat is 3.3 sec(-1) with 2'-deoxy-pIp as substrate. kcat is 0.22 sec(-1) with 3'-AMP as substrate. kcat is 0.60 sec(-1) with p(Gp)G as substrate. kcat is 14 sec(-1) with p(Ap)A as substrate. kcat is 3.8 sec(-1) with p(Ap)2A as substrate. kcat is 3.6 sec(-1) with p(Ap)3A as substrate. kcat is 2.7 sec(-1) with p(Ap)4A as substrate. kcat is 2.5 sec(-1) with p(dAp)dA as substrate. kcat is 0.72 sec(-1) with p(dAp)2dA as substrate. kcat is 1.20 sec(-1) with p(dAp)3dA as substrate. kcat is 0.79 sec(-1) with p(dAp)4dA as substrate.1 Publication
- KM=56 µM for pAp1 Publication
- KM=53 µM for 2'-deoxy-pAp1 Publication
- KM=86 µM for pCp (2'5'/3'5' mixture)1 Publication
- KM=114 µM for 2'-deoxy-pCp1 Publication
- KM=45 µM for pGp (2'5'/3'5' mixture)1 Publication
- KM=30 µM for 2'-deoxy-pGp1 Publication
- KM=59 µM for pUp (2'5'/3'5' mixture)1 Publication
- KM=110 µM for 2'-deoxy-pUp1 Publication
- KM=32 µM for 2'-deoxy-pTp1 Publication
- KM=48 µM for 2'-deoxy-pIp1 Publication
- KM=420 µM for 3'-AMP1 Publication
- KM=14.0 µM for p(Gp)G1 Publication
- KM=160 µM for p(Ap)A1 Publication
- KM=55 µM for p(Ap)2A1 Publication
- KM=45 µM for p(Ap)3A1 Publication
- KM=59 µM for p(Ap)4A1 Publication
- KM=149 µM for p(dAp)dA1 Publication
- KM=67 µM for p(dAp)2dA1 Publication
- KM=180 µM for p(dAp)3dA1 Publication
- KM=280 µM for p(dAp)4dA1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 13 | Manganese 1; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 15 | Manganese 1; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 20 | Manganese 2By similarity | 1 | |
Metal bindingi | 45 | Manganese 2; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 72 | Manganese 1By similarity | 1 | |
Metal bindingi | 72 | Manganese 3By similarity | 1 | |
Metal bindingi | 83 | Manganese 3; via pros nitrogenBy similarity | 1 | |
Metal bindingi | 198 | Manganese 3; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 255 | Manganese 1By similarity | 1 | |
Metal bindingi | 257 | Manganese 2; via tele nitrogenBy similarity | 1 |
GO - Molecular functioni
- 3',5'-nucleotide bisphosphate phosphatase activity Source: RHEA
- 5'-3' exodeoxyribonuclease activity Source: EcoCyc
- 5'-3' exoribonuclease activity Source: UniProtKB
- manganese ion binding Source: UniProtKB
- nucleotidase activity Source: UniProtKB
- nucleotide binding Source: UniProtKB-KW
Keywordsi
Molecular function | Exonuclease, Hydrolase, Nuclease |
Ligand | Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:G6634-MONOMER MetaCyc:G6634-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:yciV Synonyms:trpHBy similarity Ordered Locus Names:b1266Imported, JW1258Imported |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000065638 | 1 – 293 | 5'-3' exoribonucleaseAdd BLAST | 293 |
Proteomic databases
PaxDbi | P77766 |
PRIDEi | P77766 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 4260125, 43 interactors 850224, 1 interactor |
IntActi | P77766, 9 interactors |
STRINGi | 511145.b1266 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0613, Bacteria |
HOGENOMi | CLU_067347_0_0_6 |
InParanoidi | P77766 |
PhylomeDBi | P77766 |
Family and domain databases
InterProi | View protein in InterPro IPR004013, PHP_dom IPR003141, Pol/His_phosphatase_N IPR016195, Pol/histidinol_Pase-like |
Pfami | View protein in Pfam PF02811, PHP, 1 hit |
SMARTi | View protein in SMART SM00481, POLIIIAc, 1 hit |
SUPFAMi | SSF89550, SSF89550, 1 hit |
i Sequence
Sequence statusi: Complete.
P77766-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSDTNYAVIY DLHSHTTASD GCLTPEALVH RAVEMRVGTL AITDHDTTAA
60 70 80 90 100
IAPAREEISR SGLALNLIPG VEISTVWENH EIHIVGLNID ITHPLMCEFL
110 120 130 140 150
AQQTERRNQR AQLIAERLEK AQIPGALEGA QRLAQGGAVT RGHFARFLVE
160 170 180 190 200
CGKASSMADV FKKYLARGKT GYVPPQWCTI EQAIDVIHHS GGKAVLAHPG
210 220 230 240 250
RYNLSAKWLK RLVAHFAEHH GDAMEVAQCQ QSPNERTQLA ALARQHHLWA
260 270 280 290
SQGSDFHQPC PWIELGRKLW LPAGVEGVWQ LWEQPQNTTE REL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74348.1 AP009048 Genomic DNA Translation: BAA14800.1 |
PIRi | E64874 |
RefSeqi | NP_415782.1, NC_000913.3 WP_001285661.1, NZ_STEB01000005.1 |
Genome annotation databases
EnsemblBacteriai | AAC74348; AAC74348; b1266 BAA14800; BAA14800; BAA14800 |
GeneIDi | 57732032 945857 |
KEGGi | ecj:JW1258 eco:b1266 |
PATRICi | fig|511145.12.peg.1315 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74348.1 AP009048 Genomic DNA Translation: BAA14800.1 |
PIRi | E64874 |
RefSeqi | NP_415782.1, NC_000913.3 WP_001285661.1, NZ_STEB01000005.1 |
3D structure databases
SMRi | P77766 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4260125, 43 interactors 850224, 1 interactor |
IntActi | P77766, 9 interactors |
STRINGi | 511145.b1266 |
Proteomic databases
PaxDbi | P77766 |
PRIDEi | P77766 |
Genome annotation databases
EnsemblBacteriai | AAC74348; AAC74348; b1266 BAA14800; BAA14800; BAA14800 |
GeneIDi | 57732032 945857 |
KEGGi | ecj:JW1258 eco:b1266 |
PATRICi | fig|511145.12.peg.1315 |
Organism-specific databases
EchoBASEi | EB4005 |
Phylogenomic databases
eggNOGi | COG0613, Bacteria |
HOGENOMi | CLU_067347_0_0_6 |
InParanoidi | P77766 |
PhylomeDBi | P77766 |
Enzyme and pathway databases
BioCyci | EcoCyc:G6634-MONOMER MetaCyc:G6634-MONOMER |
Miscellaneous databases
PROi | PR:P77766 |
Family and domain databases
InterProi | View protein in InterPro IPR004013, PHP_dom IPR003141, Pol/His_phosphatase_N IPR016195, Pol/histidinol_Pase-like |
Pfami | View protein in Pfam PF02811, PHP, 1 hit |
SMARTi | View protein in SMART SM00481, POLIIIAc, 1 hit |
SUPFAMi | SSF89550, SSF89550, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RNAAM_ECOLI | |
Accessioni | P77766Primary (citable) accession number: P77766 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | February 1, 1997 | |
Last modified: | April 7, 2021 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families