NS1A_ANV1
ID NS1A_ANV1 Reviewed; 1005 AA.
AC P0C6K7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Avian nephritis virus 1 (ANV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus.
OX NCBI_TaxID=336960;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=G-4260;
RX PubMed=10954549; DOI=10.1128/jvi.74.18.8487-8493.2000;
RA Imada T., Yamaguchi S., Mase M., Tsukamoto K., Kubo M., Morooka A.;
RT "Avian nephritis virus (ANV) as a new member of the family Astroviridae and
RT construction of infectious ANV cDNA.";
RL J. Virol. 74:8487-8493(2000).
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=P0C6K7-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q9JGF2-1; 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; AB033998; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C6K7; -.
DR Proteomes; UP000007440; 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; IPR045836; Astro_VPg.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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..1005
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327365"
FT CHAIN 1..204
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327366"
FT CHAIN 205..478
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327367"
FT CHAIN 479..730
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327368"
FT CHAIN 718..809
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419603"
FT CHAIN 810..1005
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327369"
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 940..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 556
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 621
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 204..205
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 478..479
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 730..731
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 809..810
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1005 AA; 112460 MW; BC4C9243E26C8F40 CRC64;
MASAGPTGAG ARPPKAFTAQ AGLAKLVNPA GLNSILARGK EKFGGTQAWK ELMGCDVIFA
RSISHWYGIK GTTYYELTVA LGQPLYKPVT DPELTEEEKA VMTAVQSRFA QSNSSVVLTR
TLLNKTCELK DRIRELTDEL GQTEVHLARE KVKAAALKLE NRKLFVENQE LKDQLEKERT
KHGWKGLKTL CLWIFLATLI GGYITGSNAA CTLVDVPSPM KVGYDTFKQM CIHKDSYLPD
GAFDKESLAL ECSKQMDYMD CKEVITDSIS GKTSFAGMLR DVFRVDEIVT AIRTVVRFAM
DFSLAYPICV MFVLILTRNK KHAIISACCA LVAKCCGLRL LPFTLVLTYA PSETAIAGCI
YGLGYISIPL VTFLHWVGLV LKAILVPDDC YIGTRVSHAL AWSIMLPMWI ITQELMAFTE
FPLELQIVTT VVVCTAGFGF RYLTGTVTIT EPDGTVKKYK RIFNAKSAIG TISTVFFEKA
KAIRGVIPSF PSKADNIVKI EVDVDGGSAG VGFRLGNYIY TAGHVVGEAK IAKITWKGLT
SQAKVLGHIE LPLFTDTLAR LEIPKPFQQL PVFRLAKSSE NDYVQMVCFD NQLQNVVTFS
GWANIDGDYL NAPFETYAGT SGSPIINRDG RMLGVHFGSN AVVSQGFVIT RLFATEPAVK
QCKSDEDLAD EIVRKVMGGI RISFASLTSE LEKQRDELNA LKQMVNDLID TDLVALEKKK
GKTKRTVRGQ KHKTKAISKA AFMKTKVLTE EEYRRLEEEG FTKDEIKDIV DNLREQAWLD
YQNQLDEEGD DDWYEQMEED QRINDQIDQN IERDLEDRGE WYGQRKITFK QRAMLRFIQL
GRQQQVATVS FPDGYEDRAE ELYNKVVTTE DLPEGETSEA ALSLPNKIVH QAGKRLNFKH
VKIHPDKTFM KSGVTQIEEK PEGDIILKAK TTTLAPKEEP VIQQVEQQPQ VEQQQQPQQP
VVEEKKRTPP PKPQRKPKTG AKAKCLDCGE TFVERQDFHV CKSKN
