NS1AB_HASV5
ID NS1AB_HASV5 Reviewed; 1416 AA.
AC Q4TWH8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 71.
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 Human astrovirus-5 (HAstV-5).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=35741;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Goiania/GO/12/94/Brazil;
RX PubMed=16421636; DOI=10.1007/s00705-005-0704-9;
RA Silva P.A., Cardoso D.D., Schreier E.;
RT "Molecular characterization of human astroviruses isolated in Brazil,
RT including the complete sequences of astrovirus genotypes 4 and 5.";
RL Arch. Virol. 151:1405-1417(2006).
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=Q4TWH8-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q4TWH9-1; 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 905.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; DQ028633; AAY46273.1; ALT_SEQ; Genomic_RNA.
DR SMR; Q4TWH8; -.
DR PRIDE; Q4TWH8; -.
DR Proteomes; UP000008628; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
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; IPR045835; Astro_1A.
DR InterPro; IPR045833; Astro_p19.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022068; Mamastrovirus_p20.
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; PF19415; Astro_1A; 1.
DR Pfam; PF19414; Astro_p19; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF12285; DUF3621; 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..1416
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327283"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327284"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327285"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327286"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419588"
FT CHAIN 756..913
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327287"
FT CHAIN 914..1416
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327288"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1161..1287
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 752..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..146
FT /evidence="ECO:0000255"
FT COILED 587..614
FT /evidence="ECO:0000255"
FT COMPBIAS 779..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 489
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 551
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 175..176
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 419..420
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 664..665
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 755..756
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 913..914
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1416 AA; 161728 MW; CB75E8DC9B60DE0D CRC64;
MAHGEPYYSS KPDKDFNFGS TMARRQMTPT MVTKLPKFVR NSPQVYDWIV RGLIFPTTGK
TYFQRVVVIT GGFEDGTYGS FAFDGREWVE IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
EEKATLTLDV QFLQHENVRL KELISKPEPR KIQMKWIIVG AVLTFLSLIP GGYAQSQTNN
TIFTDVIAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRSHWLRTVF
YYIHYYEMWN IFMFVLAIGT VMRSTRPGTD LITLATSHLS GFRMAVLPTI PFHTTMTLWV
MNTLMVCYYF DNLLAITMAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
LTGTTTSLFV VILTCRFVRM ATIFIGTRFE IRDANGKVVA TVPTRIKNAA FDFFQRLKQS
GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HVVGNNTFVN VCYEGLMYEA
KVRYMPEKDI AFITCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PADFHPVKAP SQVELLKEEI
ERLKAQLNSA AENPSTVITQ QPTATLEQKS VNDSDVVDLV RTAMEREMKI LRDEINGILA
PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
PDYDDEDYYD EDDDGWGMVG DDVEFDYTEV INFDQAKPTP APRTTKPKPC PEPEAETQPL
DLSQKKDKQL EHEQQVVKPT KPQKNDPQPY SQTYGKAPIW ESYDFDWDED DAKFILPAPP
RLTKADEIVL GSKIVKLRTI IETAIKTQNY SALPEAVFEL DKAAYEAGLE GFLQRVKSKN
KAPKKLQRAP EDQGAQNYHS LDAWKSLLEP PRERRCVPAN FPLLGHLPID RPIFDDKKPR
DDLLGLLPEP TWHAFEEYGP TTWGPQAFIK SFDKFFYAEP IDFFSEYPQL CAFADWATYR
EFRYLEDTRV IHITATEKNT DSTPAYPKMN YFDTEEKYLE SYGWAPYIRE FTRVFKGDKP
EVLWYLFLKK EIIKEEKIRN SDIRQIVCAD PIYTRIGACL EAHQNALMKQ HTETSVGQCG
WSPMEGGFKK TMQRLVNKGN KYFIEFDWTR YDGTIPPSLF RHIKEIRWNF INKDQREKYR
HVHEWYVDNL LNRHVLLPSG EVTLQTRGNP SGQFSTTMDN NMINFWLQAF EFAYFNGPNK
DLWKTYDTVV YGDDRLSTTP SVPENYEERV IDMYRDIFGM WVKPGKVICR ESIVGLSFCG
FTVNADLEPV PTSPEKLMAS LLKPYKILPD LESLHGKLLC YQLLAAFMAE DHPFKVYVEH
CLSRTAKQLR DSGLPARLTE EQLHRIWRGG PKKCDG