NS1A_TASV2
ID NS1A_TASV2 Reviewed; 1125 AA.
AC Q9ILI6;
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 2 (TAstV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus.
OX NCBI_TaxID=246343;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10846102; DOI=10.1128/jvi.74.13.6173-6177.2000;
RA Koci M.D., Seal B.S., Schultz-Cherry S.;
RT "Molecular characterization of an avian astrovirus.";
RL J. Virol. 74:6173-6177(2000).
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=Q9ILI6-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q9ILI5-1; 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; AF206663; AAF18462.2; -; Genomic_RNA.
DR RefSeq; NP_987086.1; NC_005790.1. [Q9ILI6-1]
DR SMR; Q9ILI6; -.
DR GeneID; 2943321; -.
DR Proteomes; UP000007235; 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; 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 Ribosomal frameshifting; Thiol protease; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1125
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327360"
FT CHAIN 1..170
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327361"
FT CHAIN 171..552
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327362"
FT CHAIN 553..797
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327363"
FT CHAIN 798..916
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419602"
FT CHAIN 917..1125
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327364"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 131..218
FT /evidence="ECO:0000255"
FT ACT_SITE 600
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 632
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 697
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 170..171
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 552..553
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 797..798
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 916..917
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1125 AA; 127666 MW; 2FBF0F1EA38EA4B5 CRC64;
MAQAGRSGDA FASLDQRRER QEEQAQSGLD KVFYFQGVVE LFNRMKIAYG RTPAWTALMK
CNAIYLKDFK TAVGVEGTRY GLFFAEEVTK PTWSPDIGAN LITLGEKACL DAQNAKYERL
QASLKTTSGL VHQVMEKTRE AKENLEKANK IQEQLDKVIE SNKALHRKIQ ERNREKMQEY
MVRLHNTQKD RDDWVQRCSR LEQENVTLQK RLKEKENALV SVGWDLLGWI VISVLVFGLI
SLADAQNLTP PAKIVITPGQ AEFMDLAKLE KIQVRKYRLD SCELPPEKGC VLYKDYLTTR
PVSFLELMAK CSKPDWVSES SYNETTLMEE CIQIFGAEWC EGKLVDLVPR KCGEQHVLVN
IIEQIEKTRE VVTLIYGKVM SYRLDMWITS IFSLVLAGNK EKLFKMAPFI FVAWFLNIPV
FLTCVAVNIF PVVSLPFILF QIFMPQFVLV NAFLLWLTLT LTAFYWSEGP KILMEISYAL
VYTIGFVLWS LGLAVGVTLK LTMVHQILMF CVVAAAICGT KFACTTITVQ HPDGTTAKYT
RVGKLKNNVV NQCKKVVTTL QTRGVIPATP AKTASIVIVE GKNGTGVGFR FMNYILTAEH
VVQGSDIATL KNGSVSVKSK VIKTIPIFES VDNVAVLKLP PELNSVKPIK LAKKVQSDYL
TLTAYDPNFQ HAATFTGWCI IDGNWLNNSF DTKFGNSGAP YCDHDGRLVG IHLGTQGVLS
QGIVIVDALK NTFQLADQCR PQNFDMDEFL EKVIAGTKVS HAAILKELEE LREEVQFLKK
KCVTYDDYWL CQTIFGQAKG KTKKTVRGRK HLVTKRALGK GHFMKMRMLT DEEYQNMIEK
GFSAEEIREA VNALREQAWL NYCIDNDVDD EGEEDWYDDM VETDRVNQEI DEAIERAMED
RGEFYQKKSR LTFVEQAMMH LIQVSKERSQ TAKLEVQKEN EAQLVKMFER CVTDENTPEG
TTSIAALSTE DDVRLVEGKV IDFTKAKNIP VDGEIRREII PGTKCTEIST GPENKKNILK
KKDTHIAEGK VETKSSQQPV DVKDDKPVAL EQRKPRACKW CGSSQKHDYR ECRFQREKRF
CVYCAAMHSM FEGHIRPIEC TSCKKSFSGI EKLEDHVVSG ECQKN
