NS1AB_TASV2
ID NS1AB_TASV2 Reviewed; 1638 AA.
AC Q9ILI5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 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 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=Q9ILI5-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q9ILI6-1; 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 1125.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; AF206663; AAF60952.1; ALT_SEQ; Genomic_RNA.
DR PRIDE; Q9ILI5; -.
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: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; 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; 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..1638
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327313"
FT CHAIN 1..170
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327314"
FT CHAIN 171..552
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327315"
FT CHAIN 553..797
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327316"
FT CHAIN 798..916
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419593"
FT CHAIN 917..1051
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327317"
FT CHAIN 1052..1638
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327318"
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 DOMAIN 1381..1515
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT COILED 130..222
FT /evidence="ECO:0000255"
FT COILED 758..788
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"
FT SITE 1051..1052
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1638 AA; 187664 MW; 941F4907479B6DB5 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 ECQKKLIEGP VTTKAPTPVP
DWLKIFAWED DILPPEGKTA LPENVTLIGH IPVDKLVSRT KKVQDPLLGL VTPWKQDMYD
STTWTVKAYT KMFEKFHYHD PVDFVEQYAE FVLLCDNMVL REHDYMANSN ITPIMSTEKN
VNSTPAYPKF QAYDSEAEYL EDCGWQEYLD VVSDPETINR RPLWWCFLKN EVLKREKIED
SDIRMILCTD PIFTRIGAMF EQDQNNRMKQ QTEIRSAQVG WTPFFGGLDR RVRRLYGDGD
RYFVEMDWTR YDGTIPKSLF WRIRQIRFFF LHDSHKTPKM RRLYNWYVKN LLEKIILLPT
GEVCQVKKGN PSGQFSTTVD NNMINVWLTT FEVSYLFFKQ RGRLPTEKEL QENCSMICYG
DDRLLSIRKG FVEYEPDTVI DMYKNIFGMW VKRNNIKIQD TPEGLSFCGL TIVKSSTGAY
VGVPNVNKIL STLENPVRRL PDVESLWGKL VSLRILCENA PSNVKHFLDE QISNVEEFAA
RENIQLPEVG PDFYSRIW
