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Database: UniProt
Entry: D9MNM1_9VIRU
LinkDB: D9MNM1_9VIRU
Original site: D9MNM1_9VIRU 
ID   D9MNM1_9VIRU            Unreviewed;       312 AA.
AC   D9MNM1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=ORF1a {ECO:0000313|EMBL:ADJ38389.1};
DE   Flags: Fragment;
GN   Name=ORF1a {ECO:0000313|EMBL:ADJ38389.1};
OS   Astrovirus rat/RS118/HKG/2007.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae.
OX   NCBI_TaxID=858506 {ECO:0000313|EMBL:ADJ38389.1};
RN   [1] {ECO:0000313|EMBL:ADJ38389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RS118 {ECO:0000313|EMBL:ADJ38389.1};
RX   PubMed=20554799; DOI=10.1099/vir.0.022764-0;
RA   Chu D.K., Chin A.W., Smith G.J., Chan K.H., Guan Y., Peiris J.S.,
RA   Poon L.L.;
RT   "Detection of novel astroviruses in urban brown rats and previously known
RT   astroviruses in humans.";
RL   J. Gen. Virol. 91:2457-2462(2010).
RN   [2] {ECO:0000313|EMBL:ADJ38389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RS118 {ECO:0000313|EMBL:ADJ38389.1};
RA   Chu D.K.W., Chin A.W.H., Smith G.J., Chan K.H., Guan Y., Peiris J.S.,
RA   Poon L.L.M.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein covalently attached to the 5' extremity of the
CC       genomic and subgenomic RNAs. {ECO:0000256|ARBA:ARBA00029406}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         Evidence={ECO:0000256|ARBA:ARBA00024586};
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DR   EMBL; HM450381; ADJ38389.1; -; Genomic_RNA.
DR   MEROPS; S01.109; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR045836; Astro_VPg.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   Pfam; PF19416; Astro_VPg; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   REGION          185..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ38389.1"
SQ   SEQUENCE   312 AA;  35182 MW;  FF1C096DF537790F CRC64;
     HTYQTEVVRH VTGKDIVLLK IPPQCVAVPR YKVAKEPCYD WVCVLAPDGN GAYITSVTNG
     FGHGDTISYA TPTRDGMSGA PVVDQNGHVV GVHQTNTGFT GGAQVLVLTD IEMPSKQQIE
     VNELKAEIER LKAMLPPEKE KEEIVESSAL DQCMNDVDIV HLVRAAVGRE VAVLREELAF
     EQAKGKTKHG RGFRHNPRTF NRPVPVKGGK RKRKVFTEQE YKELLEAGLD ADKIRELVDE
     ILTREAEEVG YPEWSDPDED QDEELEDEWF GRYNENEKEQ VPENTDAEQP QQQQQSKNER
     RGRRRGPKNG TN
//
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