NS1AB_HASV8
ID NS1AB_HASV8 Reviewed; 1417 AA.
AC Q9IFX2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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 Human astrovirus-8 (HAstV-8).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=43358;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Yuc-8;
RX PubMed=11086120; DOI=10.1099/0022-1317-81-12-2891;
RA Mendez-Toss M., Romero-Guido P., Munguia M.E., Mendez E., Arias C.F.;
RT "Molecular analysis of a serotype 8 human astrovirus genome.";
RL J. Gen. Virol. 81:2891-2897(2000).
RN [2]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=14557623; DOI=10.1128/jvi.77.21.11378-11384.2003;
RA Mendez E., Salas-Ocampo M.P., Munguia M.E., Arias C.F.;
RT "Protein products of the open reading frames encoding nonstructural
RT proteins of human astrovirus serotype 8.";
RL J. Virol. 77:11378-11384(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=Q9IFX2-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q9IFX3-1; Sequence=External;
CC -!- PTM: Cleaved presumably by viral and host proteases.
CC -!- MISCELLANEOUS: [Isoform nsp1ab]: Generated by a ribosomal frameshift at
CC position 900.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; AF260508; AAF85963.1; ALT_SEQ; Genomic_RNA.
DR PIR; C49529; C49529.
DR PRIDE; Q9IFX2; -.
DR Proteomes; UP000008629; 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: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 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; IPR045833; Astro_p19.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022068; Mamastrovirus_p20.
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; PF19414; Astro_p19; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF12285; DUF3621; 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 1: Evidence at protein level;
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..1417
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327289"
FT CHAIN 1..176
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327290"
FT CHAIN 177..420
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327291"
FT CHAIN 421..665
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327292"
FT CHAIN 666..756
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419589"
FT CHAIN 757..914
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327293"
FT CHAIN 915..1417
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327294"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1162..1288
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 753..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..143
FT /evidence="ECO:0000255"
FT COILED 588..615
FT /evidence="ECO:0000255"
FT COMPBIAS 780..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 490
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 552
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 176..177
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 420..421
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 665..666
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 756..757
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 914..915
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1417 AA; 161559 MW; 94F6E43DBE61548B CRC64;
MMALGEPYYS SKPDKDFNFG STMARRQMTP TMVTKLPKFV RNSPQAYDWI VRGLIFPTTG
KTYFQRVVVI TGGLEDGTYG SYAFNGSEWV EIYPIEHLNL MSSLKLIHKA NALQERLRLS
QEEKATLALD VQFLQHENVR LKELIPKPEP RKIQMKWIIV GAVLTFLSLI PGGYAQSQTN
NTIFTDMIAA CKYSTETLTE NLDLRIKLAL ANITINDKLD AVRQILNFAF VPRAHWLRTV
FYYIHYYEMW NIFMFVLAIG TVMRSARPGT DLITLATSHL SGFRMAVLPT IPFHTTMTLW
VMNTLMVCYY FDNLLAITMA ILAPILGIIF LCFMEDSNYV SQIRGLIATA VLIAGGHACL
TLTGTTTSLF VVILTCRFIR MATVFIGTRF EIRDANGKVV ATVPTRIKNV AFDFFQKLKQ
SGVRVGVNDF VVIKPGALCI IDTPEGKGTG FFSGNDIVTA AHVVGNNTFV SVCYEGLVYE
AKVRYMPEKD IAFITCPGDL HPTARLKLSK NPDYSCVTVM AYVNEDLVVS TATAMVHGNT
LSYAVRTQDG MSGAPVCDKY GRVLAVHQTN TGYTGGAVII DPADFHPVKA PSQVELLKEE
IERLKAQLNS AAENPVTVVT QQPIVTLEQK SVSDSDVVDL VRTAMEREMK VLRDEINGIL
APFLQKKKGK TKHGRGRVRR NLRKGVKLLT EEEYRELLEK GLDRETFLDL IDRIIGERSG
YPDYDDEDYY DEDDDGWGMV GDDVEFDYTE VINFDQAKPT PAPRTTKPKP CPEPKIEAQP
LDLSQKKEKQ PEHEQQVAKP TKPQKIEPQP YSQTYGKAPI WESYDFDWDE DDAKFILPAP
HRLTKADEIV LGSKIVKLRT IIETAIKTQN YSALPEAVFE LDKAAYEAGL EGFLQRVKSK
KQGPKKLQRA PEDQGAQNYH SLDAWKSLLE PPRERRCVPA NFPLLGHLPI NRPIFDDKKP
RDDLLGLLPE PTWHAFEEYG PTTWGPQAFV KSFDKFFYAE PIDFFSEYPQ LCAFADWATY
REFRYLEDTR VIHITATEKN TDSTPAYPKM NYFDTEEDYL EAHGWAPYIR EFTRVFKGDK
PEVLWYLFLK KEIIKEEKIR NSDIRQIVCA DPIYTRIGAC LEAHQNALMK QHTDTSVGQC
GWSPMEGGFK KTMQRLVNKG NKHFIEFDWT RYDGTIPPAL FKHIKEIRWN FINKDQREKY
RHVHEWYVDN LLNRHVLLPS GEVTLQTRGN PSGQFSTPMD NNMVNFWLQA FEFAYFNGPD
KDLWKTYDTV VYGDDRLSTT PSVPDNYEER VITMYRDIFG MWVKPGKVIC RDSIVGLSFC
GFTVNENLEP VPTSPEKLMA SLLKPYKILP DLESLHGKLL CYQLLAAFMA EDHPFKVYVE
HCLSRTAKQL RDSGLPARLT EEQLHRIWRG GPKKCDG
