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NS1AB_HASV5
ID   NS1AB_HASV5             Reviewed;        1416 AA.
AC   Q4TWH8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 71.
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-5 (HAstV-5).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=35741;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Goiania/GO/12/94/Brazil;
RX   PubMed=16421636; DOI=10.1007/s00705-005-0704-9;
RA   Silva P.A., Cardoso D.D., Schreier E.;
RT   "Molecular characterization of human astroviruses isolated in Brazil,
RT   including the complete sequences of astrovirus genotypes 4 and 5.";
RL   Arch. Virol. 151:1405-1417(2006).
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=Q4TWH8-1; Sequence=Displayed;
CC       Name=nsp1a;
CC         IsoId=Q4TWH9-1; 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 905.
CC   -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC       {ECO:0000305}.
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DR   EMBL; DQ028633; AAY46273.1; ALT_SEQ; Genomic_RNA.
DR   SMR; Q4TWH8; -.
DR   PRIDE; Q4TWH8; -.
DR   Proteomes; UP000008628; 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   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..1416
FT                   /note="Non-structural polyprotein 1AB"
FT                   /id="PRO_0000327283"
FT   CHAIN           1..175
FT                   /note="Protein p19"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327284"
FT   CHAIN           176..419
FT                   /note="Transmembrane protein 1A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327285"
FT   CHAIN           420..664
FT                   /note="Serine protease p27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327286"
FT   CHAIN           665..755
FT                   /note="VPg"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419588"
FT   CHAIN           756..913
FT                   /note="Protein p20"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327287"
FT   CHAIN           914..1416
FT                   /note="RNA-directed RNA polymerase p57"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000327288"
FT   TRANSMEM        154..174
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          1161..1287
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          752..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          104..146
FT                   /evidence="ECO:0000255"
FT   COILED          587..614
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        779..799
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            913..914
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1416 AA;  161728 MW;  CB75E8DC9B60DE0D CRC64;
     MAHGEPYYSS KPDKDFNFGS TMARRQMTPT MVTKLPKFVR NSPQVYDWIV RGLIFPTTGK
     TYFQRVVVIT GGFEDGTYGS FAFDGREWVE IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
     EEKATLTLDV QFLQHENVRL KELISKPEPR KIQMKWIIVG AVLTFLSLIP GGYAQSQTNN
     TIFTDVIAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRSHWLRTVF
     YYIHYYEMWN IFMFVLAIGT VMRSTRPGTD LITLATSHLS GFRMAVLPTI PFHTTMTLWV
     MNTLMVCYYF DNLLAITMAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
     LTGTTTSLFV VILTCRFVRM ATIFIGTRFE IRDANGKVVA TVPTRIKNAA FDFFQRLKQS
     GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HVVGNNTFVN VCYEGLMYEA
     KVRYMPEKDI AFITCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
     SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PADFHPVKAP SQVELLKEEI
     ERLKAQLNSA AENPSTVITQ QPTATLEQKS VNDSDVVDLV RTAMEREMKI LRDEINGILA
     PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
     PDYDDEDYYD EDDDGWGMVG DDVEFDYTEV INFDQAKPTP APRTTKPKPC PEPEAETQPL
     DLSQKKDKQL EHEQQVVKPT KPQKNDPQPY SQTYGKAPIW ESYDFDWDED DAKFILPAPP
     RLTKADEIVL GSKIVKLRTI IETAIKTQNY SALPEAVFEL DKAAYEAGLE GFLQRVKSKN
     KAPKKLQRAP EDQGAQNYHS LDAWKSLLEP PRERRCVPAN FPLLGHLPID RPIFDDKKPR
     DDLLGLLPEP TWHAFEEYGP TTWGPQAFIK SFDKFFYAEP IDFFSEYPQL CAFADWATYR
     EFRYLEDTRV IHITATEKNT DSTPAYPKMN YFDTEEKYLE SYGWAPYIRE FTRVFKGDKP
     EVLWYLFLKK EIIKEEKIRN SDIRQIVCAD PIYTRIGACL EAHQNALMKQ HTETSVGQCG
     WSPMEGGFKK TMQRLVNKGN KYFIEFDWTR YDGTIPPSLF RHIKEIRWNF INKDQREKYR
     HVHEWYVDNL LNRHVLLPSG EVTLQTRGNP SGQFSTTMDN NMINFWLQAF EFAYFNGPNK
     DLWKTYDTVV YGDDRLSTTP SVPENYEERV IDMYRDIFGM WVKPGKVICR ESIVGLSFCG
     FTVNADLEPV PTSPEKLMAS LLKPYKILPD LESLHGKLLC YQLLAAFMAE DHPFKVYVEH
     CLSRTAKQLR DSGLPARLTE EQLHRIWRGG PKKCDG
 
 
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