Aiemman SARS Koronaviruksen nsp3, domeeni, ADPriboosi binding moduli PubMed struktuuri

NSp3 otan tämän uudestaan esiin kokonaan:

 https://www.sciencedirect.com/science/article/pii/S0166354214003660?via%3Dihub#f0015

https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=289172

https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=289172

 
 Protein         <1 ..="">1922
                     /product="orf1a polyprotein"
     mat_peptide     1..1922
                     /product="nsp3"
     Region          103..171
                     /region_name="DUF3655"
                     /note="Protein of unknown function (DUF3655); pfam12379"
                     /db_xref="CDD:289172"

Protein of unknown function (DUF3655)


Accession:
cl13772

PSSM Id:
301111

Name:
DUF3655

Created:
20-Jan-2010

Updated:
8-Jan-2020


This
 domain family is found in viruses, and is approximately 70 amino acids 
in length. The family is found in association with pfam08716, pfam01661,
 pfam05409, pfam06471, pfam08717, pfam06478, pfam09401, pfam06460, 
pfam08715, pfam08710.

 
     Site            order(204,222,229,231..232,310,312..314)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:239150"

 Macro domain, a high-affinity ADP-ribose binding module found in a
 variety of proteins as a stand-alone domain or in combination with 
other domains like in histone macroH2A and some PARPs (poly ADP-ribose 
polymerases). Some macro domains recognize poly ADP-ribose as a ligand. 
Previously identified as displaying an Appr-1"-p 
(ADP-ribose-1"-monophosphate) processing activity, the macro domain may 
play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation
 of proteins, an important post-translational modification which occurs 
in DNA repair, transcription, chromatin biology, and long-term memory 
formation, among other processes.

 
     Region          218..325
                     /region_name="Macro"
                     /note="Macro domain; pfam01661"
                     /db_xref="CDD:279930"

      Region          509..651
                     /region_name="SUD-M"
                     /note="Single-stranded poly(A) binding domain; pfam11633"
                     /db_xref="CDD:152069"

Single-stranded poly(A) binding domain
This
 family of proteins represents Nsp3c, the product of ORF1a in group 2 
coronavirus. The domain exhibits a macrodomain fold containing the nsp3 
residues 528 to 648, with a flexibly extended N-terminal tail from 
residues 513 to 527 and a C-terminal flexible tail of residues 649 to 
651. SUD-M(527-651) binds single-stranded poly(A); the contact area with
 this RNA on the protein surface, and the electrophoretic mobility shift
 assays confirm that SUD-M has higher affinity for purine bases than for
 pyrimidine bases.

 
     Region          655..720
                     /region_name="Nsp3_PL2pro"
                     /note="Coronavirus polyprotein cleavage domain; pfam12124"
                     /db_xref="CDD:288939"

Coronavirus polyprotein cleavage domain
This
 domain is found in SARS coronaviruses, and is about 70 amino acids in 
length. It is found associated with various other coronavirus proteins 
due to the polyprotein nature of most viral translation. PL2pro is a 
domain of the non-structural protein nsp3. The domain performs three of 
the cleavages required to separate the translated polyprotein into its 
distinct proteins.

 
     Region          723..1040
                     /region_name="Viral_protease"
                     /note="Papain like viral protease; pfam08715"
                     /db_xref="CDD:285877"

Papain like viral protease
This family 
of viral proteases are similar to the papain protease and are required 
for proteolytic processing of the replicase polyprotein. The structure 
of this protein has shown it adopts a fold similar that of 
de-ubiquitinating enzymes.

      Region          1066..1178
                     /region_name="NAR"
                     /note="Nucleic acid-binding domain (NAR); pfam16251"
                     /db_xref="CDD:292868"

Nucleic acid-binding domain (NAR)

This domain, approximately 100 residues in length, is mainly found in Orf1a polyproteins in severe acute respiratory syndrome coronavirus. The global domain of the NAR represents a new fold, with a parallel four-strand beta-sheet holding two alpha-helices of three and four turns that are oriented antiparallel to the beta-strands and a group of residues form a positively charged patch on the protein surface as the binding site responsible for binding affinity for nucleic acids.

     CDS             1..4382
                     /coded_by="FJ882960.1:225..13373"