NS1AB_ANV1
ID NS1AB_ANV1 Reviewed; 1512 AA.
AC Q9JGF2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 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 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=Q9JGF2-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=P0C6K7-1; 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 1005.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; AB033998; BAA92848.1; ALT_SEQ; Genomic_RNA.
DR SMR; Q9JGF2; -.
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: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; IPR045836; Astro_VPg.
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; PF19416; Astro_VPg; 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..1512
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327319"
FT CHAIN 1..204
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327320"
FT CHAIN 205..478
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327321"
FT CHAIN 479..730
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327322"
FT CHAIN 718..809
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419594"
FT CHAIN 810..954
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327323"
FT CHAIN 955..1512
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327324"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1257..1390
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 940..981
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"
FT SITE 954..955
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1512 AA; 171273 MW; 195D9D1DC048DCDC 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 CKSKKLNEPP SGGYTPVPDH
LRWNNWQIYM EPLDLRITVP ENYPILGHIA IDKLVERKKK VNDPLLKMLE QPKCEGFTST
TWTRKAYTKS FEKFDYGDAV DFVQDYPELT AFADAAVLAE VGYMEGTHVI PIQETSKNMD
STPAFPKMLD FDSERDYLEA HGMKEYIDTQ LGVQSGKPLW WCFLKNEILK EKKVSEDDIR
IITCSDPVIT RLGASFDSEQ NERMKERTET HHAQVGWTPF FGGLDKRVRR ITSCGRTQVL
ELDWTRFDGT IPVQLFQRMR ELRKFFLTRR SRRRYGKLLD WYNAQLTDRI TLLPTGEVTH
VKKGNPSGQF STTVDNNLVN EWLTAFEFGY QHLENHGIIP TVRDYRANVD FLCYGDDRLL
AFNPSFVNYD PQVTIDMYKN IFGMWVKPEN IKLFDSPTGS SFCGFTLVKP HGQWVGVVNV
NKLLQSLKTP TRRLPDLESL WGKLVSLKIM CYHSDPEAVS YLSNQIRRVE EYARAEGIEL
PEVGPDFYRK IW
