NS1AB_HASV4
ID NS1AB_HASV4 Reviewed; 1415 AA.
AC Q3ZN06;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 74.
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-4 (HAstV-4).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=35300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Dresden;
RA Barthel J., Rethwilm A., Rohayem J.;
RT "Molecular characterization of human astrovirus type 4.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 699-713, IDENTIFICATION OF VPG, AND FUNCTION OF VPG.
RX PubMed=22787221; DOI=10.1128/jvi.00797-12;
RA Fuentes C., Bosch A., Pinto R.M., Guix S.;
RT "Identification of human astrovirus genome-linked protein (VPg) essential
RT for viral infectivity.";
RL J. Virol. 86:10070-10078(2012).
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 (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: [VPg]: Protein covalently attached to the 5' extremity of the
CC genomic and subgenomic RNAs. {ECO:0000305|PubMed:22787221}.
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=Q3ZN06-1; Sequence=Displayed;
CC Name=nsp1a;
CC IsoId=Q3ZN07-1; 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 900.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000305}.
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DR EMBL; AY720891; AAW51878.1; ALT_SEQ; Genomic_RNA.
DR SMR; Q3ZN06; -.
DR Proteomes; UP000009176; 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; Direct protein sequencing; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1415
FT /note="Non-structural polyprotein 1AB"
FT /id="PRO_0000327277"
FT CHAIN 1..175
FT /note="Protein p19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327278"
FT CHAIN 176..419
FT /note="Transmembrane protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327279"
FT CHAIN 420..664
FT /note="Serine protease p27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327280"
FT CHAIN 665..755
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419587"
FT CHAIN 756..912
FT /note="Protein p20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327281"
FT CHAIN 913..1415
FT /note="RNA-directed RNA polymerase p57"
FT /evidence="ECO:0000255"
FT /id="PRO_0000327282"
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 1160..1286
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 104..142
FT /evidence="ECO:0000255"
FT COILED 587..616
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 912..913
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1415 AA; 161278 MW; 64A20504EF1736A5 CRC64;
MAHGEPYYSS KPDKDFNFGS TMARRQMTPT MVAKLPNFVR NSPQAYDWIV RGLIFPTTGK
TYFQRVVVIT GGLEDGTYGS FVFDGREWVE IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
EEKATLALDV QFLQHENVRL KELIPKPEPR KIQMKWIIVG AVLTFLSLIP GGYAQSQINN
TIFTDMIAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRAHWLRTVF
YYIHYYEMWN IFMFVLAIGT VMRSARPGTD LITLATSHLS GFRMAVLPTI PFHTTMTLWV
MNTLMVCYYF DNLLAITLAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
LTGTTTSLFV VILTCRFIRM ATVFIGTRFE IRDANGKVVA TVPTRIKNVA FDFFQKLKQS
GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HAVGNNTFVN VCYEGLMYEA
KVRYMPEKDI AFITCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PTDFHPVKAP SRVELLKEEI
ERLKAQLNSA AENPATAVTQ QPVVTLEQKS VSDSDVVDLV RTAMEREMKV LRDEINGILA
PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
PDYDDEDYYD EDDDGWGVVG DDVEFDYTEV INFDQAKPTP APRTVKPKTC PEPEAETQPL
DLSQKKEKQL EHEQQVVKST KPQKNEPQPY SQTYGKAPIW ESYDFDWDED DAKFILPAPH
RLTKADEIVL GSKIVKLRTI IETAIKTQNY SALPEAVFEL DKAAYEAGLE GFLQRVKSKK
GSKKLQRAPE DQGAQNYHSL DAWKSLLEPP RERRCVPANF PLLGHLPINR PIFDDKKPRD
DLLGLLPEPT WHAFEEYGPT TWGPQAFIKS FDKFFYAEPI DFFSEYPQLC AFADWATYRE
FRYLEDTRVI HITATEKNTD STPAYPKMNY FDTEENYLEA HGWAPYIREF TRVFKGDKPE
VLWYLFLKKE IIKEEKIRNS DIRQIVCADP IYTRIGACLE AHQNALMKQH TDTSVGQCGW
SPMEGGFKKT MQRLVNKGNK HFIEFDWTRY DGTIPPALFK HIKEIRWNFI NKDQREKYKH
VHEWYVDNLL NRHVLLPSGE VTLQTRGNPS GQFSTTMDNN MVNFWSQAFE FAYFNGPDKD
LWKTYDTVVY GDDRLSTTPS VPDDYEERVI NMYRDIFGMW VKPGKVICRD SIVGLSFCGF
TVNENLEPVP TSPEKLMASL LKPYKILPDL ESLHGKLLCY QLLAAFMAED HPFKVYVEHC
LSRTAKQLRD SGLPARLTEE QLHRIWRGGP KKCDG
