Q60560 · SMBP2_MESAU
- ProteinDNA-binding protein SMUBP-2
- GeneIGHMBP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids989 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction (By similarity).
Specific to 5'-phosphorylated single-stranded guanine-rich sequences (By similarity).
May play a role in RNA metabolism, ribosome biogenesis or initiation of translation (By similarity).
May play a role in regulation of transcription (By similarity).
Interacts with tRNA-Tyr (By similarity).
Specific to 5'-phosphorylated single-stranded guanine-rich sequences (By similarity).
May play a role in RNA metabolism, ribosome biogenesis or initiation of translation (By similarity).
May play a role in regulation of transcription (By similarity).
Interacts with tRNA-Tyr (By similarity).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + H2O = ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 213-220 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GPPGTGKT | ||||||
Binding site | 402 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 441 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 570 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 891 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 896 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 907 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 910 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 915 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 918 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 924 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 926 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasm | |
Cellular Component | nuclear body | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | 5'-3' DNA helicase activity | |
Molecular Function | 5'-3' RNA helicase activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent activity, acting on DNA | |
Molecular Function | ATP-dependent activity, acting on RNA | |
Molecular Function | double-stranded DNA helicase activity | |
Molecular Function | identical protein binding | |
Molecular Function | ribosome binding | |
Molecular Function | RNA binding | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | single-stranded RNA binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | DNA duplex unwinding | |
Biological Process | RNA secondary structure unwinding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-binding protein SMUBP-2
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Mesocricetus
Accessions
- Primary accessionQ60560
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000080702 | 2-989 | DNA-binding protein SMUBP-2 | |||
Sequence: ALSTVESFVAQQLELLELERDAEVEERRSWQEHSSLKELQSRGVCLLKLQVSSQCTGLYGQRLVTFEPRKLGPVVVLPSNSFTSGDIVGLYDANESSQLATGVLTRITQKSVTVAFDESHDFQLNLDRENTYRLLKLANDVTYKRLKKALMTLKKYHSGPASSLIDVLLGGSSPSPTTEIPPFTFYNTALDPSQKEAVSFALAQKEVAIIHGPPGTGKTTTVVEIILQAVKQGLKILCCAPSNVAVDNLVERLALCKKRILRLGHPARLLESAQQHSLDAVLARSDNAQIVADIRKDIDQVFGKNKKTQDKREKSNFRNEIKLLRKELKEREEAAIVQSLTAADVVLATNTGASSDGPLKLLPENHFDVVVVDECAQALEASCWIPLLKAPKCILAGDHRQLPPTTISHKAALAGLSRSLMERLVEKHGAGAVRMLTVQYRMHQAITRWASEAMYHGQLTAHPSVAGHLLKDLPGVADTEETSVPLLLIDTAGCGLLELDEEDSQSKGNPGEVRLVTLHIQALVDAGVHAGDIAVIAPYNLQVDLLRQSLSNKHPELEIKSVDGFQGREKEAVILTFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKTLVDYFTEHGEVRTAFEYLDDIVPENYTHEGSQGHSHAPKPRGPVTSIRKPTNEQENGQEARAAAGQGRRKPNERPPGSQVHSQPSSGARGCDRTGAIDRTEHFRAMIEGFVASKESQLEFPASLSSHDRLLVHQIAEEHGLRHDSTGEGKARHITVSRKSPAGSGGVAPQLPSPPSPAQAEPEPLSQQPLGQPHCSTQLDLKALHLQRLQRQQGSQAQPAKAQPGVGLHPQKTQQKKKKKETKGPALPCEEDFDALVSAVIKADNTCSFAKCTASTTTLGQFCMHCSRRYCLSHHLPEIHGCGEKARAHARQMISREGVLYAGSGTRDRALDPAKRAQLQRRLDKKLGELSSQRTSKRKEKERGT | ||||||
Modified residue | 797 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 800 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Expression
Tissue specificity
High expression in brain and testis, moderate in heart, spleen, and kidney, and low in other tissues.
Interaction
Subunit
Homooligomer (By similarity).
Interacts with RUVBL1 (By similarity).
Interacts with RUVBL2 (By similarity).
Interacts with GTF3C1 (By similarity).
Interacts with ABT1 (By similarity).
Interacts with ribosomes (By similarity).
Interacts with RUVBL1 (By similarity).
Interacts with RUVBL2 (By similarity).
Interacts with GTF3C1 (By similarity).
Interacts with ABT1 (By similarity).
Interacts with ribosomes (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 637-783 | SS DNA-binding | ||||
Sequence: TAFEYLDDIVPENYTHEGSQGHSHAPKPRGPVTSIRKPTNEQENGQEARAAAGQGRRKPNERPPGSQVHSQPSSGARGCDRTGAIDRTEHFRAMIEGFVASKESQLEFPASLSSHDRLLVHQIAEEHGLRHDSTGEGKARHITVSRK | ||||||
Region | 650-717 | Disordered | ||||
Sequence: YTHEGSQGHSHAPKPRGPVTSIRKPTNEQENGQEARAAAGQGRRKPNERPPGSQVHSQPSSGARGCDR | ||||||
Domain | 721-784 | R3H | ||||
Sequence: IDRTEHFRAMIEGFVASKESQLEFPASLSSHDRLLVHQIAEEHGLRHDSTGEGKARHITVSRKS | ||||||
Compositional bias | 765-779 | Basic and acidic residues | ||||
Sequence: LRHDSTGEGKARHIT | ||||||
Region | 765-818 | Disordered | ||||
Sequence: LRHDSTGEGKARHITVSRKSPAGSGGVAPQLPSPPSPAQAEPEPLSQQPLGQPH | ||||||
Compositional bias | 792-806 | Pro residues | ||||
Sequence: APQLPSPPSPAQAEP | ||||||
Region | 833-869 | Disordered | ||||
Sequence: LQRQQGSQAQPAKAQPGVGLHPQKTQQKKKKKETKGP | ||||||
Motif | 860-864 | Nuclear localization signal | ||||
Sequence: KKKKK | ||||||
Zinc finger | 885-934 | AN1-type | ||||
Sequence: IKADNTCSFAKCTASTTTLGQFCMHCSRRYCLSHHLPEIHGCGEKARAHA | ||||||
Region | 954-989 | Disordered | ||||
Sequence: ALDPAKRAQLQRRLDKKLGELSSQRTSKRKEKERGT |
Domain
The R3H domain recognizes phosphorylated 5'-ends of single-stranded nucleic acids which promotes binding of nucleic acids and stimulates ATPase activity.
Sequence similarities
Belongs to the DNA2/NAM7 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length989
- Mass (Da)108,439
- Last updated1997-11-01 v1
- Checksum9489671E46DAD04E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 765-779 | Basic and acidic residues | ||||
Sequence: LRHDSTGEGKARHIT | ||||||
Compositional bias | 792-806 | Pro residues | ||||
Sequence: APQLPSPPSPAQAEP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L15625 EMBL· GenBank· DDBJ | AAB00104.1 EMBL· GenBank· DDBJ | mRNA |