NS1AB_TASV1
ID NS1AB_TASV1 Reviewed; 1611 AA.
AC Q9JH69;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 83.
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 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 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=Q9JH69-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q9JH70-1; 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 1099.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; Y15936; CAB95006.3; ALT_SEQ; Genomic_RNA.
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: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; -; 1.
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; Reference proteome;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1611
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327307"
FT CHAIN 1..168
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327308"
FT CHAIN 169..508
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327309"
FT CHAIN 509..795
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327310"
FT CHAIN 796..915
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419592"
FT CHAIN 916..1027
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327311"
FT CHAIN 1028..1611
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327312"
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 375..395
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 DOMAIN 1352..1486
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT COILED 124..187
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"
FT SITE 1027..1028
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1611 AA; 183203 MW; F3827B808E34A58F 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 HAVTTCSKKL DSHPEPSRVF QPLDFGLGIF DWRFDLQPIR HHVAVPMNVE
VLGYIPVDRL VERRNVITDP LLKLVEPWRQ ETYGPAVWTI KAYNKMFEKF FYSEPLEFAQ
LDSSILNLAD SYCLQEHDYM SGSQIVPITS TEKNLDSTPG YPKFKVFSTE REYLSTCGWD
EYKTVWQVGP REKPLWWCFL KTEVLKLAKI EQDDIRMILC TDPVFTRIGA AFEQHQNSLM
KLETENHHAQ VGWSPFFGGI HRRATRLYGE HRYYVELDWT RFDGTIPPEL FRRIKLMRFF
LLDPKYKTPE NRDRYNWYVE NLIDKVVLLP TGEVCKIYGG NPSGQFSTTV DNNFVNVWLT
VFELAYLFYK EHNRLPTICE IKKHTDWICY GDDRLLAVDK RFINSYDTAA VIAMYKDVFG
MWVKPDNIKV FPSLEGVSFC GMVWTKRKGQ YVGKPNVDKI LSTLSDPVSR LPDIQSLWGK
LVSLRLLCEN ESDEVVDYLD KQIESVSRHA KEAGIALPKI GPDFYAEIWI D
