NS1A_TASV1
ID NS1A_TASV1 Reviewed; 1099 AA.
AC Q9JH70;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Turkey astrovirus 1 (TAstV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus.
OX NCBI_TaxID=364370;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
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=Q9JH70-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q9JH69-1; 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; Y15936; CAB95005.1; -; Genomic_RNA.
DR PRIDE; Q9JH70; -.
DR Proteomes; UP000000676; 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; -; 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 SUPFAM; SSF50494; SSF50494; 1.
PE 3: Inferred from homology;
KW Coiled coil; Host membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Ribosomal frameshifting; Thiol protease; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1099
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327355"
FT CHAIN 1..168
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327356"
FT CHAIN 169..508
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327357"
FT CHAIN 509..795
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327358"
FT CHAIN 796..915
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419601"
FT CHAIN 916..1099
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327359"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 550
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 582
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 647
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 168..169
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 508..509
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 795..796
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 915..916
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1099 AA; 123391 MW; 6B7FCD38015435ED CRC64;
MAAAAASALG ASAPKALAPA DGPIVAGLDK LVNLEGVHDL FEAMRGAYGE DPAWKGLMSC
DVVYLKDITT AIGVKDTSVG IFRKFSDGCS WCPTGAECFL SMKDLAYMKA QSAKAQRLTA
SLATTSNLIA RAMRAESELK RARDEERKVD ARYKDILEHS LAARKALQKE LDETRERELH
LLKELGKRSS IRTKAFSFFD WLFMAVVFFL FLHYTSAECV KPDFGCLVVN SNLPVPSLTF
HDVMARCYNT FGNIVLSSQI DAARLREECE QSANKFLGTH IGDPAHKVWC ENRLETLIPV
ECDSSEFLEI FTSNLNAFMV SVSQFYKTIS YYKLDALVTF AFSAALATNK LKMVMVLPLL
LVALYLNVPP ITVTIASVIF QPLILPFVGF QLVFPNFLPY NLFVAWVWMV CQAFFSSDGV
KLLVSVSTAL VQVVFLAVWS ISVIVLQQLS IPMVAQILLF VATLTVSVGV KFANSTITVV
HPDGNTEKVS RVTLVRQSMA KRISQIKQSL TIRGVIPSGP NRFDSIVVVE GQGGSGVGWR
FMNSIFTAGH VVQGSKFVTI KSESTQVKVK VKRVIDLFEC VDTLVEIPLT KEFQHIKPLR
LAKKVEDSYL QLCAFKPDMV EKASYQGWCT IDSGFIFNSF NTQFGNSGAP YVDSDGRLVG
MHLGSQGVIS QGVVLVDTLK TQFLAQQSQI DDQLMERIIE GTKVSHAAIL TELDRMRTKV
EEVALVSARV NQLESQLKDL YEFSSNSIKC LSDDIEKMVC AQLFDEINLQ SVMEKISALP
PTEKLAKLVE VFVEQKKKGK TKRTARGGKH ALGKKYLSKA HFSRMRMLTE EEYNKMVEDG
FSPDEIKEVV DQLREQAWQN YLIDNDIGED DDLDWYDDML EDERLNEEID RRVEAALEDR
GELAYQKIRR TFVDQALIHL ITLKKGNWQT TKVECQPERE EAYKEQFQKA VKQEDLTEGT
SYAIYSAGDA TILIENKEID HTEIKPVTTG AKTVQEYPKD ARTTVATFDD NKKDIVKTKR
TTEIVLEQRK KTCRTCGETR PHNHKMCRDR HTRRFCFWCG VVHSDVEGHS RDLKCPKCSA
GFANLREMEQ HAVTTCSKN
