P23540 · RNMC1_MOMCH
- ProteinRibonuclease MC
- GeneMC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids191 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ribonuclease cleaving preferentially the 5'-side of uridine.
Miscellaneous
Has a remarkably high specificity toward CpU, ApU, and UpU.
Catalytic activity
- a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.38 mM | CpU |
kcat is 745 min-1 with CpU as substrate.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 34 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 34 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 72-73 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: NV | ||||||
Binding site | 75 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 81 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 84-85 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: HE | ||||||
Active site | 85 | |||||
Sequence: E | ||||||
Binding site | 88-89 | UMP residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI) | ||||
Sequence: KH | ||||||
Active site | 89 | Proton acceptor | ||||
Sequence: H | ||||||
Site | 102 | Involved in thermostability | ||||
Sequence: Y | ||||||
Site | 103 | Involved in thermostability | ||||
Sequence: F | ||||||
Site | 106 | Involved in thermostability | ||||
Sequence: A | ||||||
Site | 126 | Involved in thermostability | ||||
Sequence: P | ||||||
Site | 128 | Involved in thermostability | ||||
Sequence: G | ||||||
Site | 145 | Involved in thermostability | ||||
Sequence: G | ||||||
Site | 163 | Involved in thermostability | ||||
Sequence: L | ||||||
Site | 166 | Involved in thermostability | ||||
Sequence: V | ||||||
Site | 191 | Involved in thermostability | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ribonuclease T2 activity | |
Molecular Function | RNA binding |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease MC
- EC number
- Short namesRNase MC ; RNase MC1
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Cucurbitales > Cucurbitaceae > Momordiceae > Momordica
Accessions
- Primary accessionP23540
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 72 | Altered substrate specificity from uridine specific to guanosine specific. | ||||
Sequence: N → S | ||||||
Mutagenesis | 72 | Decreased catalytic efficiency and affinity for uridine (CpU substrate). Altered substrate specificity from uridine specific to guanosine specific. | ||||
Sequence: N → T | ||||||
Mutagenesis | 73 | Normal catalytic efficiency and affinity for uridine (CpU substrate). | ||||
Sequence: V → L | ||||||
Mutagenesis | 74 | Decreased affinity for uridine (CpU substrate). | ||||
Sequence: L → A | ||||||
Mutagenesis | 75 | Slightly decreased catalytic efficiency for uridine (CpU substrate). | ||||
Sequence: R → S | ||||||
Mutagenesis | 102 | Decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: Y → A | ||||||
Mutagenesis | 103 | Decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: F → A | ||||||
Mutagenesis | 106 | Decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: A → L | ||||||
Mutagenesis | 126 | Slightly decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: P → A | ||||||
Mutagenesis | 128 | Slightly decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: G → A | ||||||
Mutagenesis | 145 | Slightly decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: G → A | ||||||
Mutagenesis | 166 | Slightly decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: V → A | ||||||
Mutagenesis | 191 | Decreased thermostability (at 47-58 degrees Celsius). | ||||
Sequence: F → A |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-? | |||||
Chain | PRO_0000206508 | 2-191 | Ribonuclease MC | |||
Sequence: DSFWFVQQWPPAVCSFQKSGSCPGSGLRTFTIHGLWPQGSGTSLTNCPQGSPFDITKISHLQSQLNTLWPNVLRANNQQFWSHEWTKHGTCSESTFNQAAYFKLAVDMRNNYDIIGALRPHAAGPNGRTKSRQAIKGFLKAKFGKFPGLRCRTDPQTKVSYLVQVVACFAQDGSTLIDCTRDTCGANFIF | ||||||
Disulfide bond | 15↔23 | |||||
Sequence: CSFQKSGSC | ||||||
Disulfide bond | 48↔92 | |||||
Sequence: CPQGSPFDITKISHLQSQLNTLWPNVLRANNQQFWSHEWTKHGTC | ||||||
Disulfide bond | 152↔185 | |||||
Sequence: CRTDPQTKVSYLVQVVACFAQDGSTLIDCTRDTC | ||||||
Disulfide bond | 169↔180 | |||||
Sequence: CFAQDGSTLIDC |
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length191
- Mass (Da)21,260
- Last updated1991-11-01 v1
- ChecksumA67958CB471DC7D2
Keywords
- Technical term