NS1AB_HASV1
ID NS1AB_HASV1 Reviewed; 1436 AA.
AC Q67726;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
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-1 (HAstV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=12456;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8021608; DOI=10.1099/0022-1317-75-7-1785;
RA Willcocks M.M., Brown T.D., Madeley C.R., Carter M.J.;
RT "The complete sequence of a human astrovirus.";
RL J. Gen. Virol. 75:1785-1788(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8254779; DOI=10.1128/jvi.68.1.77-83.1994;
RA Lewis T.L., Greenberg H.B., Herrmann J.E., Smith L.S., Matsui S.M.;
RT "Analysis of astrovirus serotype 1 RNA, identification of the viral RNA-
RT dependent RNA polymerase motif, and expression of a viral structural
RT protein.";
RL J. Virol. 68:77-83(1994).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=11799197; DOI=10.1128/jvi.76.4.2003-2008.2002;
RA Geigenmuller U., Chew T., Ginzton N., Matsui S.M.;
RT "Processing of nonstructural protein 1a of human astrovirus.";
RL J. Virol. 76:2003-2008(2002).
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=Q67726-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=P0C6K4-1; Sequence=External;
CC -!- PTM: Cleaved presumably by viral and host proteases.
CC -!- MISCELLANEOUS: [Isoform nsp1ab]: Generated by a ribosomal frameshift at
CC position 919.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; Z25771; CAA81033.1; -; Genomic_RNA.
DR PIR; C49529; C49529.
DR MEROPS; S01.109; -.
DR PRIDE; Q67726; -.
DR Proteomes; UP000001650; 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; Reference proteome;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1436
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327271"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327272"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327273"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327274"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419586"
FT CHAIN 756..933
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327275"
FT CHAIN 934..1436
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327276"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
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 DOMAIN 1181..1307
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 756..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..142
FT /evidence="ECO:0000255"
FT COILED 587..620
FT /evidence="ECO:0000255"
FT COMPBIAS 779..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 489
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 551
FT /note="Charge relay system; for serine protease activity"
FT /evidence="ECO:0000250"
FT SITE 175..176
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 419..420
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 664..665
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 755..756
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 933..934
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1436 AA; 163874 MW; CEC41D44BCACD32F CRC64;
MAYGEPYYSS KPDKDFNFGS TMARRQMTPT MVTKLPKFVR NSPQAYDWIV RGLIFPTIGK
TYFQRVVVIT GGLEDGTYGS FAFDGKEWVG IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
EEKATLALDV QFLQHENVRL KEMIPKPEPR KIQMKWIIMG AVLTFLSLIP GGYAHSQTNN
TIFTDMIAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRAHWLRTVF
YYIHYYEMWN IFMFVLAIGT VMRSARPGTD LVTLATSHLS GFRMAVLPTI PFHTTMTLWV
MNTLMVCYYF DNLLAITLAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
LTGTTTSLFV VILTCRFIRM ATVFIGTRFE IRDANGKVVA TVPTRIKNVA FDFFQKLKQS
GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HVVGNNTFVN VCYEGLMYEA
KVRYMPEKDI AFLTCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PADFHPVKAP SQVELLKEEI
ERLKAQLNSA TENATTVVTQ QPSAALEQKS VSDSDVVDLV RTAMEREMKV LRDEINGILA
PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
PDYDDEDYYD EDDDGWGMVG DDVEFDYTEV INFDQAKPIP APRTTKQKIC PEPEVESQPL
DLSQKKEKQS EYEQQVVKST KPQQLEHEQQ VVKPIKPQKS EPQPYSQTYG KAPIWESYDF
DWDEDDAKFI LPAPHRLTKA DEIVLGSKIV KLRTIIETAI KTQNYSALPE AVFELDKAAY
EAGLEGFLQR VKSKNKAPEK QGPKKLQRAP EDQGAQNYHS LDAWKLLLEP PRERRCVPAN
FPLLGHLPIN RPIFDDKKPR DDLLGLLPEP TWHAFEEYGP TTWGPQAFIK SFDKFFYAEP
IDFFSEYPQL CAFADWATYR EFRYLEDTRV IHITATEKNT DSTPAYPKMN YFDTEENYLE
AHGWAPYIRE FTRVYKGDKP EVLWYLFLKK EIIKEEKIRN SDIRQIVCAD PIYTRIGACL
EAHQNALMKQ HTDTSVGQCG WSPMEGGFKK TMQRLVNKGN KHFIEFDWTR YDGTIPPALF
KHIKEIRWNF INKDQREKYR HVHEWYVNNL LNRHVLLPSG EVTLQTRGNP SGQFSTTMDN
NMVNFWLQAF EFAYFNGPDR DLWKTYDTVV YGDDRLSTTP SVPDDYEERV ITMYRDIFGM
WVKPGKVICR DSIVGLSFCG FTVNENLEPV PTSPEKLMAS LLKPYKILPD LESLHGKLLC
YQLLAAFMAE DHPFKVYVEH CLSRTAKQLR DSGLPARLTE EQLHRIWRGG PKKCDG
