NS1A_OASV1
ID NS1A_OASV1 Reviewed; 844 AA.
AC Q9JH67;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Non-structural polyprotein 1A;
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';
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 1A]: Contains the viral protease
CC participating in the cleavage of the polyprotein into functional
CC products.
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 -!- 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=nsp1a;
CC IsoId=Q9JH67-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q9JH66-1; Sequence=External;
CC -!- PTM: Cleaved presumably by viral and host proteases.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1A family.
CC {ECO:0000305}.
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DR EMBL; Y15937; CAB95002.1; -; Genomic_RNA.
DR RefSeq; NP_059944.1; NC_002469.1. [Q9JH67-1]
DR SMR; Q9JH67; -.
DR GeneID; 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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 3: Inferred from homology;
KW Coiled coil; Host membrane; Hydrolase; Membrane; Protease;
KW Ribosomal frameshifting; Thiol protease; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..844
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327350"
FT CHAIN 1..172
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327351"
FT CHAIN 173..407
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327352"
FT CHAIN 408..640
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327353"
FT CHAIN 641..721
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419600"
FT CHAIN 722..844
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327354"
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 REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..143
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"
SQ SEQUENCE 844 AA; 95455 MW; 4A8735C8C56ACB6C 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 RRKRVQQPKN SKGALKTRAP
KSAN
