ID H6WX89_9VIRU Unreviewed; 852 AA.
AC H6WX89;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE SubName: Full=ORF1a {ECO:0000313|EMBL:AEZ67024.1};
OS Astrovirus wild boar/WBAstV-1/2011/HUN.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=1137931 {ECO:0000313|EMBL:AEZ67024.1, ECO:0000313|Proteomes:UP000168579};
RN [1] {ECO:0000313|EMBL:AEZ67024.1, ECO:0000313|Proteomes:UP000168579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild boar/WBAstV-1/2011/HUN {ECO:0000313|EMBL:AEZ67024.1};
RX PubMed=22398915; DOI=10.1007/s00705-012-1272-4;
RA Reuter G., Nemes C., Boros A., Kapusinszky B., Delwart E., Pankovics P.;
RT "Astrovirus in wild boars (Sus scrofa) in Hungary.";
RL Arch. Virol. 157:1143-1147(2012).
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 -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004301};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
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; JQ340310; AEZ67024.1; -; Genomic_RNA.
DR RefSeq; YP_005271207.1; NC_016896.1.
DR MEROPS; S01.109; -.
DR GeneID; 11763564; -.
DR KEGG; vg:11763564; -.
DR OrthoDB; 507at10239; -.
DR Proteomes; UP000168579; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
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 598..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..674
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 95086 MW; C66444ABD57990C4 CRC64;
MVDQLRCLPG HRPNSPWDIR TLPRHMIYPT LSTDPRDRVI IASSVTTDNE WVTYVLDGDS
WRQTICAPDE QSVILVCALL IDKEEKENEI ATLKMENDRK NQQCAYFSQQ IPPKTTGAKW
SWLSILALLV LIHATFKGAV AWVTQSTSHG VEYDKTIKLN EELDEFITIA LQKNWTRSVT
EGSAGHYVTS GLGWKGKSGE GAIGRYGSRK HRLHADTVYK AIPSSGTEWS RERRGGMCTW
QERCTIAEGN GRKVCGCLNR AAGCVSQLRI SVTVLAPLQT IYTIYLTCGL AVIYHFDPIA
TSLISVVHLV TFSIVGMFLP DVDYIKNLRA VGSVTVIVLA HGFVNFLESP PLCSTAVCFV
WRLVRLLQAM RGQVIEIRDS SGKITQKISS LEGPLFKFFQ GLKAKLKQVR ATSVPLVRIN
PAAVCHISTG DGSKGTGFFC ANYVVTAAHV TGNHKVATIS YQGKNYQSNV KKTSEKDMIF
LEIPPALQGV PRFKLSKKYN CDWVCVLAPS GEGAFVTSVV EGKAHGDTFS YPCPTRDGMS
GAPLLDVDGH VLGIHQTNTG YTGGAVRLEH EDVIDPPKEN TQVAALKKQI EELKMQLAQK
DAAPATPPPK PQRPPRIKDM KQCNMEDSDI VELIRIAMQR EMGILREEIN DSLLQKKKGK
SKHGRGRKHG GGRTRKIGKM FTEEEYQEML DSGLEPEQIR AIAEELYEQQ HDFPEWSDPE
DDDEVNEWWF GGDHSANVND DDNDIPSYYQ KKKKPLSDYL IKEWTKESID EMLTSLSPLE
MKKAQPLLQH LKCEDPLKKT VIVAMLDRVL TSNGLSPVSD GLEYQQRMKP KNGKPGRHDP
QKPTSARGKS QQ
//
