NS1AB_OASV1
ID NS1AB_OASV1 Reviewed; 1351 AA.
AC Q9JH66;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Non-structural polyprotein 1AB;
DE Contains:
DE RecName: Full=VPg;
DE Contains:
DE RecName: Full=Protein p19;
DE Contains:
DE RecName: Full=Transmembrane protein 1A;
DE Contains:
DE RecName: Full=Serine protease p27;
DE Short=p27;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Protein p20;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase p57;
DE Short=p57;
DE EC=2.7.7.48;
GN Name=ORF1;
OS Ovine astrovirus 1 (OAstV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=1239577;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12573498; DOI=10.1016/s0168-1702(02)00269-1;
RA Jonassen C.M., Jonassen T.O., Sveen T.M., Grinde B.;
RT "Complete genomic sequences of astroviruses from sheep and turkey:
RT comparison with related viruses.";
RL Virus Res. 91:195-201(2003).
CC -!- FUNCTION: [Non-structural polyprotein 1AB]: Contains the viral protease
CC participating in the cleavage of the polyprotein into functional
CC products. It contains also the activities necessary for replication of
CC genomic RNA, as well as transcription of subgenomic mRNA.
CC -!- FUNCTION: [VPg]: Protein covalently attached to the 5' extremity of the
CC genomic and subgenomic RNAs. {ECO:0000250}.
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 EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=nsp1ab;
CC IsoId=Q9JH66-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q9JH67-1; Sequence=External;
CC -!- PTM: Cleaved presumably by viral and host proteases. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform nsp1ab]: Generated by a ribosomal frameshift at
CC position 830.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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; Y15937; CAB95003.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_059945.2; NC_002469.1.
DR PRIDE; Q9JH66; -.
DR GeneID; 1449587; -.
DR KEGG; vg:1449587; -.
DR Proteomes; UP000007786; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF19415; Astro_1A; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1351
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327301"
FT CHAIN 1..172
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327302"
FT CHAIN 173..407
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327303"
FT CHAIN 408..640
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327304"
FT CHAIN 641..721
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419591"
FT CHAIN 722..826
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327305"
FT CHAIN 827..1351
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327306"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1085..1217
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..144
FT /evidence="ECO:0000255"
FT COILED 579..635
FT /evidence="ECO:0000255"
FT COMPBIAS 687..702
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 481
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 544
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 172..173
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 407..408
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 640..641
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 721..722
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 826..827
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1351 AA; 154740 MW; FB0A954B26292C54 CRC64;
MNVYDKVLQF GSKKARARGM ALNKLSRNRL EDIYAGSGPL VFGFGPIDMV DPGSLNPSIK
TLDTVYVAAV QPDNQYVVHH FVPGRNEWVE TDASTHQPTA LVGVLVQDHK AKTREVEDLK
SQLSQLRMEH EILRHEYERL KLKSPIVKPF KPLKVLLFSL LLGLLFAGVT NGARTGTCYA
YDEEKDTCLY WEWKDSREVA WYDSYVTEAL AIYNRACVYV RSKEFMTYLS LVFQTVFNWY
FCATALAVYY MARAENPIVM FVTLALATLS QFQLLAVAVL PLLDFSATMG LWLSMVVFYM
SQQISILVSF CVLVLSVMIG TFMADSEYAM MIKGHAVVFA IVCYSHVAMI LNIPPWVVSL
TMVCYRLWRV CFVFPAERLE IRSADGKVLH TVPTHPNWTA KVTRFVQSLR KGLRTSVAPT
ARIVPDGIAI VEAREGVGTC FRVKNNLVTS KHVVGSDDAV KIRWGAQEDM ARVTYRHPTK
DIALMALPTN LQTMPAYKFA KAITDGPIVM TAFDEANLLL VAVTEGVRVE DHMTYSVATR
NGMSGAPITT VDGRVIAVHQ TNTGFTGGAV IFVPEDIPEV RKISKREQEL EDRVKQLEGM
LNMDQAYVDS NLIVDLVREA VQREMKVLRT ELANLGGFSQ KKKGKNKSTK RKRKAVWTEE
EYKAMLEKGF TRDQLRIMAD AIRDQYYDDE DEQSEEEAGY PDWSDPGDST DIENEWFGYE
QSWKELEPAK SGVVVNTLPK DLVFKYSLDN YPISKQDIQA VAKELKIYEK AISDIISTSV
STDGKWKDDV DAQKILQELD GLWWGINHTL WEHGLMPFTQ RRKRVQQPKK LQRGPEDPGP
EECKLDYWEQ LVEPSKEKFL VPPEYPLLGV VPLDRPISDF DAPVDNLLAL LPEPESPDLG
FEPAVWGPEA YVKSFEKFDF ADPDPNIEKN YPREWAFANL VLHREFDFLA DSVVKDITAT
SKNSESTPGF PKTYWWKTEA EYLAKRGYAD YVSEWNRIRG GARPNVLWYL FLKKEILKST
KVRDADIRQI ICSDPIFARI GCCFEEDQNE RMKRRTKTRM PQCGWSPFFG GFNDRIQRLV
AKGNPYWIEF DWTRYDGTIP SQIFKHIKNF RFSMLAKEYQ TPELRNMYHW YVDNILRRYV
CMPSGEITIQ HKGNPSGQVS TTMDNNLVNV FLQAFEYAYL HPEKSMDELR KDWESYDSLI
YGDDRLTTSP SVPNDYVTRV VAMYKDIFGM WVKPEKVKVS HSPVGLSFCG FVITHQDGQY
LPVPAEEAKL LASLLRPTKK LENMDALYGK LLCYRILNHN LPNDNKFRNY ILVALEVMAR
HYSSRGEEPP FYVTESMLDK LWRGGPKFDY G
