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NS1A_HASV8
ID   NS1A_HASV8              Reviewed;         921 AA.
AC   Q9IFX3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
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-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 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=Q9IFX3-1; Sequence=Displayed;
CC       Name=nsp1ab;
CC         IsoId=Q9IFX2-1; 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; AF260508; AAF85962.1; -; Genomic_RNA.
DR   SMR; Q9IFX3; -.
DR   MEROPS; S01.109; -.
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: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   Ribosomal frameshifting; Thiol protease; Transmembrane;
KW   Transmembrane helix; Viral RNA replication.
FT   CHAIN           1..921
FT                   /note="Non-structural polyprotein 1A"
FT                   /id="PRO_0000327340"
FT   CHAIN           1..176
FT                   /note="Protein p19"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327341"
FT   CHAIN           177..420
FT                   /note="Transmembrane protein 1A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327342"
FT   CHAIN           421..665
FT                   /note="Serine protease p27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327343"
FT   CHAIN           666..756
FT                   /note="VPg"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419598"
FT   CHAIN           757..921
FT                   /note="Protein p20'"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327344"
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   REGION          753..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   921 AA;  103493 MW;  445175FC4EEE8571 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
     NKAPKNYKGP QKTKGPKTTT H
 
 
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