O71188 · R1A_GLRV3

Function

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit.

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site311For leader protease activity
Active site357For leader protease activity
Site393-394Cleavage; by the leader protease
Binding site1619Fe cation (UniProtKB | ChEBI)
Binding site1621Fe cation (UniProtKB | ChEBI)
Binding site1676Fe cation (UniProtKB | ChEBI)
Binding site16852-oxoglutarate (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functioncysteine-type peptidase activity
Molecular Functiondioxygenase activity
Molecular Functionmetal ion binding
Molecular FunctionmRNA methyltransferase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Biological Processmethylation
Biological ProcessmRNA modification
Biological Processproteolysis
Biological ProcessRNA processing
Biological Processviral translational frameshifting

Keywords

Names & Taxonomy

Protein names

Gene names

    • ORF names
      1a

Organism names

Accessions

  • Primary accession
    O71188

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004025321-393Leader protease
ChainPRO_00004025311-2233Replicase protein 1a
ChainPRO_0000402533394-2233Methyltransferase/helicase

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region143-163Disordered
Compositional bias146-161Basic and acidic residues
Domain478-669Alphavirus-like MT
Region1277-1301Disordered
Region1400-1442Disordered
Compositional bias1412-1442Polar residues
Domain1601-1694Fe2OG dioxygenase
Region1708-1746Disordered
Compositional bias1714-1737Polar residues
Domain1902-2066+RNA virus helicase ATP-binding
Domain2067-2230+RNA virus helicase C-terminal

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Ribosomal frameshifting. The replicase 1a is produced from conventional translation of the 1a ORF. The replicase 1ab is generated probably by a +1 ribosomal frameshifting mechanism occurring at the 1a-1b genes boundary.

O71188-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Replicase 1a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    2,233
  • Mass (Da)
    244,804
  • Last updated
    2003-06-01 v2
  • Checksum
    CDDC18B6133FB08C
MDYIRPLRVFSFPHVNNTLEYVRYNKANGDVGAFLTTMKFIGNVKLSDFTPRCAAMIYIGKLTKGVKRTFVPPPVKGFARQYAVVSGSVSALRGDGKKVLMEARTSTSATSDVSDFDVVFEAVSNALLVVHYHRVVPYAPVKREQPKPAVKQDEQKPKRQASHWAVKPTAVGVHVPLPKKQEALEPAQSVPQQSLEEKAALTFGLFFSKGGGDESDAVILRKGKLFNRALNVPIDVKNTFVWAKIWDEASRRRGYFYVKDRAVKFFPIVRGRATIEDFIVNTAPGCDVALPRIELWSMRERAFVCTTKGWCWFNNERLRGEIYRRRCFSSSFSIGFLMHLGFRSLKVIRFAGTNILHMPSLNEERTFGWKGGDVYLPNVPKTAIVAGDRTRLGGEILASVANALNQEEVYSSVVSSITNRLVLRDQSALLSHLDTKLCDMFSQRDAMIREKPSHRCDVFLKPREREKLRELFPELSIQFSDSVRSSHPFANAMRSCFNGIFSRRCGNVCFFDIGGSFTYHVKAGHVNCHVCNPVLDVKDVKRRINEILFLSTAGGDSYVSSDLLTEAASKSVSYCSRESQNCDSRADAGFMVDVYDISPQQVAEAMDKKGALVFDIALMFPVELLYGNGEVYLEELDTLVKREGDYLAYNVGQCGEMYEHSFSNVSGFFTFSYVRTSSGNVFKLEYEGYRCGYHHLTMCRAQKSPGTEVTYRSLVPSFVGKSLVFIPVVAGSSVSFKTIVLDSDFVDRIYSYALNTIGTFENRTFEYAVGAVRSQKTHVITGSRVVHSKVDISPDDMWGLVVAVMAQAIKDRAKSIRSYNFIKASEGSLAGVFKLFFQTVGDCFSNAVSVYAKAMVHDNFNVLETLMSMPRAFIRKVPGSVVVTICTSGASDRLELRGAFDISKETFGRKLKNSRLRVFSRAIVEDSIKVMKAMKTEDGKPLPITEDSVYAFIMGNVSNVHCTRAGLLGGSKATVVSSVSKGLVARGAATKAFSGITSFFSTGSLFYDRGLTEDERLDALVRTENAINSPVGILETSRVAVSKVVAGTKEFWSEVSLNDFTTFVLRNKVLIGIFVASLGAAPIAWKYRRGIAANARRYAGSSYETLSSLSSQAAGGLRGLTSSTVSGGSLVVRRGFSSAVTVTRATVAKRQVPLALLSFSTSYAISGCSMLGIWAHALPRHLMFFFGLGTLLGARASANTWKFGGFSNNWCAVPEVVWRGKSVSSLLLPITLGVSLIIRGLLNDTIPQLAYVPPVEGRNVYDETLRYYRDFDYDEGAGPSGTQHEAVPGDDNDGSTSSVSSYDVVTNVRDVGISTNGEVTGEEETHSPRSVQYTYVEEEVAPSAAVAERQGDPSGSGTADAMAFVESVKKGVDDVFHQQSSGETAREVEVDGKGLLPESVVGEAPTQERGRAADGNTAQTAVNEGDREPVQSSLVSSPQADIPKVTQSEVHAQKEVKQEVPLATVSGATPIVDEKPAPSVTTRGVKIIDKGKAVAHVAEKKQVQVEQPKQRSLTINEGKAGKQLCMFRTCSCGVQLDVYNEATIATRFSNAFTFVDNLKGRSAVFFSKLGEGYTYNGGSHVSSGWPRALEDILTAIKYPSVFDHCLVQKYKMGGGVPFHADDEECYPSDNPILTVNLVGKANFSTKCRKGGKVMVINVASGDYFLMPCGFQRTHLHSVNSIDEGRISLTFRATRRVFGVGRMLQLAGGVSDEKSPGVPNQQPQSQGATRTITPKSGGKALSEGSGREVKGRSTYSIWCEQDYVRKCEWLRADNPVMALEPDYTPMTFEVVKTGTSEDAVVEYLKYLAIGIERTYRALLMARNIAVTTAEGVLKVPNQVYESLPGFHVYKSGTDLIFHSTQDGLRVRDLPYVLIAEKGIFTKGKDVDAVVALGDNLFVCDDILVFHDAINLIGALKVARCGMVGESFKSFEYKCYNAPPGGGKTTTLVDEFVKSPNSTATITANVGSSEDINMAVKKRDPNLEGLNSATTVNSRVVNFIVRGMYKRVLVDEVHMMHQGLLQLGVFATGASEGLFFGDINQIPFINREKVFRMDCAVFVPKKESVVYTSKSYRCPLDVCYLLSSMTVRGTEKCYPEKVVSGKDKPVVRSLSKRPIGTTDDVAEINADVYLCMTQLEKSDMKRSLKGKGKETPVMTVHEAQGKTFSDVVLFRTKKADDSLFTKQPHILVGLSRHTRSLVYAALSSKLDDKVGTYISDASPQSVSDALLHTFAPAGC

O71189-1

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    Replicase 1ab
  • See also
    sequence in UniParc or sequence clusters in UniRef

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias146-161Basic and acidic residues
Compositional bias1412-1442Polar residues
Compositional bias1714-1737Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF037268
EMBL· GenBank· DDBJ
AAC40717.3
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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