NS1A_HASV5
ID NS1A_HASV5 Reviewed; 920 AA.
AC Q4TWH9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 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 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=Q4TWH9-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q4TWH8-1; 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; DQ028633; AAY46272.1; -; Genomic_RNA.
DR SMR; Q4TWH9; -.
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:0008234; F:cysteine-type peptidase 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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045833; Astro_p19.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR022068; Mamastrovirus_p20.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
DR Pfam; PF19414; Astro_p19; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF12285; DUF3621; 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..920
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327335"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327336"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327337"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327338"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419597"
FT CHAIN 756..920
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327339"
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 REGION 752..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 920 AA; 103531 MW; 6EB457F9C65B49F4 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
KAPKNYKGPQ KTKGPKTIIH
