ID   C0JJJ6_9VIRU            Unreviewed;       392 AA.
AC   C0JJJ6;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   22-FEB-2023, entry version 33.
DE   SubName: Full=Putative serine protease {ECO:0000313|EMBL:ACN29689.1};
DE   Flags: Fragment;
OS   Astrovirus MLB1.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=568715 {ECO:0000313|EMBL:ACN29689.1};
RN   [1] {ECO:0000313|EMBL:ACN29689.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WD0104 {ECO:0000313|EMBL:ACN29689.1};
RX   PubMed=19239759; DOI=10.3201/eid1503.081213;
RA   Finkbeiner S.R., Le B.M., Holtz L.R., Storch G.A., Wang D.;
RT   "Detection of newly described astrovirus MLB1 in stool samples from
RT   children.";
RL   Emerg. Infect. Dis. 15:441-444(2009).
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FJ227122; ACN29689.1; -; Genomic_RNA.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:ACN29689.1}.
FT   COILED          188..218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACN29689.1"
FT   NON_TER         392
FT                   /evidence="ECO:0000313|EMBL:ACN29689.1"
SQ   SEQUENCE   392 AA;  43918 MW;  F211D177E608F193 CRC64;
     TTLLPNWIGS MYQGARNMLQ KVRTGVATFV RVNPNCLCHV RSEGCSGTGF RLGNDIVTAA
     HVVGNAVQVE VVYNNYVAQA KVRHIPDKDI AYLILPEGLK TMPVLKLAKN PNYEQVTIIA
     LEGNCMLVST TEGVCHGETI SYACATRDGM SGAPVLDVNG NVLGVHQTNT GYTGGATVIR
     ATDAAPYIDE NAALKKEIEE LKKMLREQTM NQRSVQDNEV VGIVRAAVQR EIGILRDELN
     SCYQKKKGKN KKGRGARHRM LRRGQKFLTE EEYQELLDKG LTREQLLDAI EEIVRARIGF
     PDWSDPEYSS EEDDAAVTYW WEQVKESDYK DGVPQFEHIV PKYSPNERVF SEQERKDISE
     ELSALQSIVD GVKKEDWEET KKQTTDALNH AL
//