NS1A_HASV4
ID NS1A_HASV4 Reviewed; 920 AA.
AC Q3ZN07;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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-4 (HAstV-4).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=35300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Dresden;
RA Barthel J., Rethwilm A., Rohayem J.;
RT "Molecular characterization of human astrovirus type 4.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 699-713, IDENTIFICATION OF VPG, AND FUNCTION OF VPG.
RX PubMed=22787221; DOI=10.1128/jvi.00797-12;
RA Fuentes C., Bosch A., Pinto R.M., Guix S.;
RT "Identification of human astrovirus genome-linked protein (VPg) essential
RT for viral infectivity.";
RL J. Virol. 86:10070-10078(2012).
CC -!- FUNCTION: [Non-structural polyprotein 1A]: Contains the viral protease
CC participating in the cleavage of the polyprotein into functional
CC products. {ECO:0000269|PubMed:22787221}.
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=Q3ZN07-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q3ZN06-1; Sequence=External;
CC -!- PTM: Cleaved presumably by viral and host proteases.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1A family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY720891; AAW51877.1; -; Genomic_RNA.
DR SMR; Q3ZN07; -.
DR Proteomes; UP000009176; 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 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Host membrane; Hydrolase; Membrane;
KW Protease; Ribosomal frameshifting; Thiol protease; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..920
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327330"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327331"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327332"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327333"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419596"
FT CHAIN 756..920
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327334"
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 753..813
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; 103386 MW; 52836952DD2DCD85 CRC64;
MAHGEPYYSS KPDKDFNFGS TMARRQMTPT MVAKLPNFVR NSPQAYDWIV RGLIFPTTGK
TYFQRVVVIT GGLEDGTYGS FVFDGREWVE IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
EEKATLALDV QFLQHENVRL KELIPKPEPR KIQMKWIIVG AVLTFLSLIP GGYAQSQINN
TIFTDMIAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRAHWLRTVF
YYIHYYEMWN IFMFVLAIGT VMRSARPGTD LITLATSHLS GFRMAVLPTI PFHTTMTLWV
MNTLMVCYYF DNLLAITLAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
LTGTTTSLFV VILTCRFIRM ATVFIGTRFE IRDANGKVVA TVPTRIKNVA FDFFQKLKQS
GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HAVGNNTFVN VCYEGLMYEA
KVRYMPEKDI AFITCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PTDFHPVKAP SRVELLKEEI
ERLKAQLNSA AENPATAVTQ QPVVTLEQKS VSDSDVVDLV RTAMEREMKV LRDEINGILA
PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
PDYDDEDYYD EDDDGWGVVG DDVEFDYTEV INFDQAKPTP APRTVKPKTC PEPEAETQPL
DLSQKKEKQL EHEQQVVKST KPQKNEPQPY SQTYGKAPIW ESYDFDWDED DAKFILPAPH
RLTKADEIVL GSKIVKLRTI IETAIKTQNY SALPEAVFEL DKAAYEAGLE GFLQRVKSKN
KAPKNYKGPQ KTKGPKTITH
