NS1AB_MASV1
ID NS1AB_MASV1 Reviewed; 1381 AA.
AC Q80KJ7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 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 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=Q80KJ7-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q80KJ8-1; 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 865.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB 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; AAO32082.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_795335.1; NC_004579.1.
DR GeneID; 29200741; -.
DR KEGG; vg:29200741; -.
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: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; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR045835; Astro_1A.
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; PF19415; Astro_1A; 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..1381
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327295"
FT CHAIN 1..195
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327296"
FT CHAIN 196..436
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327297"
FT CHAIN 437..662
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327298"
FT CHAIN 666..752
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419590"
FT CHAIN 753..867
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327299"
FT CHAIN 868..1381
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327300"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
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 DOMAIN 1122..1254
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 856..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..160
FT /evidence="ECO:0000255"
FT COILED 703..732
FT /evidence="ECO:0000255"
FT COMPBIAS 861..879
FT /note="Basic and acidic residues"
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"
FT SITE 867..868
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1381 AA; 156954 MW; 51B926928D22E51C 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 QKPKKREEGP ERGPINPDEM RLDHWEKMMA PPDAGRRLVP
DDYPVIGKLP INRPISDWDE PVDDLLNLLP PAPDSSAYGP AVWGPEAYVK SFEKFTYAKP
RDSIKRDFPR EWKFACQVLR REFDFLEGSV IMDITATSKN ADSTCAYPKC NYWKTEAEYL
SERGYQDYVS EYKRIHGGAR PKVLWLLFLK KEILKVKKIN DSDIRQIVCA DPIFARIGNA
FEEHQNTLMK HRTATRMPQC GWTPFFNGFK RRIERLLSRK NSVFIEFDWT RYDGTIPREI
FAKIKSFRFS CLAEEFQTDA NRAMYQWYCD SLLDRYVLMP SGEVTRQTKG NPSGQISTTM
DNNLCNVFFQ AFEYAYIHPE KSIEELRESW DRCDSLIYGD DRLTTFDHVP PDYVDRVVHM
YKDVFGMWVK PEKVIVSDTP VGLSFCGFTV GPDLMPVPTD CDKLVASLVT PTKKLQDIVA
LYSKVLCYRI LGHNLSDEHE FKRYVRVALE VLARHIRNLG GEEPVHVTER LLDKLWRGGP
K
