NS1A_MASV1
ID NS1A_MASV1 Reviewed; 874 AA.
AC Q80KJ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Mink astrovirus 1 (MAstV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=1239574;
OH NCBI_TaxID=452646; Neovison vison (American mink) (Mustela vison).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14573813; DOI=10.1099/vir.0.19267-0;
RA Mittelholzer C., Hedlund K.O., Englund L., Dietz H.H., Svensson L.;
RT "Molecular characterization of a novel astrovirus associated with disease
RT in mink.";
RL J. Gen. Virol. 84:3087-3094(2003).
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=Q80KJ8-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q80KJ7-1; 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; AY179509; AAO32081.1; -; Genomic_RNA.
DR RefSeq; NP_795334.1; NC_004579.1. [Q80KJ8-1]
DR SMR; Q80KJ8; -.
DR GeneID; 1482922; -.
DR KEGG; vg:1482922; -.
DR Proteomes; UP000007773; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
DR Pfam; PF19416; Astro_VPg; 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..874
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327345"
FT CHAIN 1..195
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327346"
FT CHAIN 196..436
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327347"
FT CHAIN 437..662
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327348"
FT CHAIN 666..752
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419599"
FT CHAIN 753..874
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327349"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 855..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 506
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 569
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 195..196
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 436..437
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 662..663
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 752..753
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 874 AA; 97914 MW; B2DEA14BE5CC9AED CRC64;
MANNTTSALH PRGSGQRCVY DTVLRFGDPD ARRRGFQLDE VSHNKLCDIF DSGPLHFAFG
DLKVMKVAGG VVTPHKTVVK TVYVSGVQEG NDYVTFAFTP GPNEWREVDP RIDKRTALVG
VLVQEHKKLD SDLKESRREL SQLKLEHSLL RHDYERLVRE KPGPAMRTFK FSAVIFYAFF
LGFLLMSAVK GEVYGRCLDS ELNLNGNPEV CLHWEEVKSF SLQVALADFW NMTLDYYATV
APQSPLMDLA LGYFPYFANW HMAAFLVGTA HVVAAERPLY MLVTLVLATL SRFQLVALAA
VPMLDMPSSI GLWVTMVLFA IDQAFAILAS VLISVLLLIL CLAMNDVDYG ALLRGCVTLV
SATVFSHLVS FLHAPGWFTI IAILIYRIPK VLSYVSAERV DIKGPDGKIK ETQNANPSWI
TKMSGLKNFF QRAFRQKVRT GVNPTTRIIP NSLVVIDAKD GRGTGFRVRN YLVTAGHVVG
ADTTVRVRWA DVTSFAHVVY RVPNKDIVLL TLPAEYNSLH SYKLAKEVVD GTVVVVSNGD
GGALSVGISE GVIVGESMTY AINTADGMSG SPLTTTDGRL IGVHQQNTGF TGGAVIFRDT
DFPQPKKPQR EADLEAKVAE LEKALAAYTQ SATGEDIVGL VRVAIQREME VLRKELSNEF
GQAKGKTKHK RRIMAAARSG GKRKPGKVWT EEEYKKLLEE GFTRDQLREM AEAAREADDD
FDDYEEEKNE VDYPVWSDHD SDEEIDRDWF GQNLPTWSSA WSDFEPELDP DVTKTLPCHL
EDKFSLKHYI ITEADLKHFG QEMKEYMDHL DAVIKTHTEK GKWCPNTNTE EILKDLNAMW
FKLNHTMWKN GVAPFMQRKK QKPKNGKRAP KGAQ
