NS1A_HASV1
ID NS1A_HASV1 Reviewed; 935 AA.
AC P0C6K4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 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 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=P0C6K4-1; Sequence=Displayed;
CC Name=nsp1ab;
CC IsoId=Q67726-1; 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; Z25771; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C6K4; -.
DR PRIDE; P0C6K4; -.
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:0008234; F:cysteine-type peptidase 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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045833; Astro_p19.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR022068; Mamastrovirus_p20.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
DR Pfam; PF19414; Astro_p19; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF12285; DUF3621; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Host membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Ribosomal frameshifting; Thiol protease; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..935
FT /note="Non-structural polyprotein 1A"
FT /id="PRO_0000327325"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327326"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327327"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327328"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419595"
FT CHAIN 756..935
FT /note="Protein p20'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327329"
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 756..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..935
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 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"
SQ SEQUENCE 935 AA; 105182 MW; CFFC0E822502F893 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 VKSKNKAPKN YKGPQKTKGP KTTTH
