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R1AB_BEV
ID   R1AB_BEV                Reviewed;        6857 AA.
AC   P0C6V7; P18458; Q1WFM5; Q65826; Q65827;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=nsp1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE   Contains:
DE     RecName: Full=3C-like serine proteinase;
DE              Short=3CLSP;
DE              EC=3.4.21.-;
DE     AltName: Full=M-PRO;
DE     AltName: Full=nsp3;
DE     AltName: Full=p27;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE   Contains:
DE     RecName: Full=Non-structural protein 5;
DE              Short=nsp5;
DE   Contains:
DE     RecName: Full=Non-structural protein 6;
DE              Short=nsp6;
DE   Contains:
DE     RecName: Full=Non-structural protein 7;
DE              Short=nsp7;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE     AltName: Full=nsp10;
DE     AltName: Full=p100;
DE   Contains:
DE     RecName: Full=Helicase;
DE              Short=Hel;
DE              EC=3.6.4.12;
DE              EC=3.6.4.13;
DE     AltName: Full=nsp11;
DE     AltName: Full=p67;
DE   Contains:
DE     RecName: Full=Exoribonuclease;
DE              Short=ExoN;
DE              EC=3.1.13.-;
DE     AltName: Full=nsp12;
DE   Contains:
DE     RecName: Full=Non-structural protein 13;
DE              Short=nsp13;
DE   Contains:
DE     RecName: Full=Uridylate-specific endoribonuclease;
DE              EC=3.1.-.-;
DE     AltName: Full=NendoU;
DE     AltName: Full=nsp14;
DE   Contains:
DE     RecName: Full=Putative 2'-O-methyl transferase;
DE              EC=2.1.1.-;
DE     AltName: Full=nsp15;
GN   Name=rep; ORFNames=1a-1b;
OS   Berne virus (BEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC   Renitovirus; Equine torovirus.
OX   NCBI_TaxID=11156;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-4569, CHARACTERIZATION OF 3C-LIKE
RP   PROTEINASE M-PRO, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX   PubMed=16571831; DOI=10.1128/jvi.80.8.4157-4167.2006;
RA   Smits S.L., Snijder E.J., de Groot R.J.;
RT   "Characterization of a torovirus main proteinase.";
RL   J. Virol. 80:4157-4167(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-252.
RX   PubMed=1856694; DOI=10.1099/0022-1317-72-7-1635;
RA   Snijder E.J., den Boon J.A., Horzinek M.C., Spaan J.M.;
RT   "Characterization of defective interfering RNAs of Berne virus.";
RL   J. Gen. Virol. 72:1635-1643(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4219-6857.
RC   STRAIN=Isolate P138/72;
RX   PubMed=2388833; DOI=10.1093/nar/18.15.4535;
RA   Snijder E.J., den Boon J.A., Bredenbeek P.J., Horzinek M.C., Rijnbrand R.,
RA   Spaan W.J.M.;
RT   "The carboxyl-terminal part of the putative Berne virus polymerase is
RT   expressed by ribosomal frameshifting and contains sequence motifs which
RT   indicate that toro- and coronaviruses are evolutionarily related.";
RL   Nucleic Acids Res. 18:4535-4542(1990).
CC   -!- FUNCTION: The 3C-like serine proteinase is responsible for the majority
CC       of cleavages.
CC   -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC       RNA and DNA duplex-unwinding activities with 5' to 3' polarity.
CC       {ECO:0000250}.
CC   -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC       5' direction. {ECO:0000250}.
CC   -!- FUNCTION: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
CC       which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
CC       {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6V7-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6F3-1; Sequence=External;
CC   -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC       association of the replication complex and thereby alter the
CC       architecture of the host cell membrane. {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo by its own protease yield
CC       mature proteins. 3CL-PRO is autocatalytically processed (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC       ribosomal frameshifting at the 1a-1b genes boundary.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA36600.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA36601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ310701; ABC26008.1; -; Genomic_RNA.
DR   EMBL; X56016; CAA39493.1; -; Genomic_RNA.
DR   EMBL; X52374; CAA36600.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; X52374; CAA36601.1; ALT_SEQ; Genomic_RNA.
DR   PIR; S11237; S11237.
DR   PIR; S11238; S11238.
DR   PRIDE; P0C6V7; -.
DR   Proteomes; UP000006571; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21162; NendoU_tv_PToV-like; 1.
DR   CDD; cd21413; unc_tv_SF1_Hel-like; 1.
DR   CDD; cd21403; ZBD_tv_SF1_Hel-like; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 3.40.220.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR044371; Macro_X_NSP3-like.
DR   InterPro; IPR043609; NendoU_nidovirus.
DR   InterPro; IPR044397; NendoU_PToV-like.
DR   InterPro; IPR044863; NIRAN.
DR   InterPro; IPR039573; NS2A-like.
DR   InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR   InterPro; IPR009461; NSP16_CoV-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR044355; SF1_Hel_unc_tv.
DR   InterPro; IPR044336; SF1_Hel_ZBD_tv.
DR   Pfam; PF05213; Corona_NS2A; 1.
DR   Pfam; PF19215; CoV_NSP15_C; 1.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF142877; SSF142877; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51653; CV_ZBD; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51958; NENDOU; 1.
DR   PROSITE; PS51947; NIRAN; 1.
DR   PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR   PROSITE; PS51953; NIV_EXON; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endonuclease; Exonuclease; Helicase; Host membrane; Hydrolase;
KW   Membrane; Metal-binding; Methyltransferase; Nuclease; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; Reference proteome; Repeat;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW   Transferase; Transmembrane; Transmembrane helix; Viral RNA replication;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..6857
FT                   /note="Replicase polyprotein 1ab"
FT                   /id="PRO_0000106126"
FT   CHAIN           1..2873
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283842"
FT   CHAIN           2874..3251
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283843"
FT   CHAIN           3252..3543
FT                   /note="3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283845"
FT   CHAIN           3544..3802
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283846"
FT   CHAIN           3803..3979
FT                   /note="Non-structural protein 5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283847"
FT   CHAIN           3980..4161
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283848"
FT   CHAIN           4162..4246
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283849"
FT   CHAIN           4247..4399
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283850"
FT   CHAIN           4400..5410
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283851"
FT   CHAIN           5411..5968
FT                   /note="Helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283852"
FT   CHAIN           5969..6298
FT                   /note="Exoribonuclease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283853"
FT   CHAIN           6299..6442
FT                   /note="Non-structural protein 13"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283854"
FT   CHAIN           6443..6592
FT                   /note="Uridylate-specific endoribonuclease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283855"
FT   CHAIN           6593..6857
FT                   /note="Putative 2'-O-methyl transferase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283856"
FT   TRANSMEM        2303..2323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2330..2350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2385..2405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2535..2555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2639..2659
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2664..2684
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2889..2909
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3057..3077
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3106..3126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3142..3162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3556..3575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3580..3602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3611..3631
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3640..3660
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3663..3683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3698..3718
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3723..3738
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1679..1860
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          4566..4797
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          5105..5256
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          5411..5492
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5633..5812
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5813..5972
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5970..6183
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          6451..6591
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6593..6857
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   REGION          2158..2191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2303..2683
FT                   /note="HD1"
FT   REGION          2889..3162
FT                   /note="HD2"
FT   REGION          3555..3738
FT                   /note="HD3"
FT   ACT_SITE        3304
FT                   /note="Charge relay system; for 3C-like serine proteinase
FT                   activity"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        3347
FT                   /note="Charge relay system; for 3C-like serine proteinase
FT                   activity"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        3416
FT                   /note="Charge relay system; for 3C-like serine proteinase
FT                   activity"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        5984
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5986
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6085
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6487
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6504
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6536
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6633
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6709
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6737
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6771
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         5417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5451
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5460
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5479
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5483
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         6149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   SITE            2873..2874
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            3251..3252
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT   SITE            3543..3544
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT   SITE            3802..3803
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            3979..3980
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            4161..4162
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            4246..4247
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            4399..4400
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            5410..5411
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            5968..5969
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            6298..6299
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            6442..6443
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   SITE            6592..6593
FT                   /note="Cleavage; by 3C-like serine proteinase"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        251..252
FT                   /note="RR -> KK (in Ref. 2; CAA39493)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   6857 AA;  784289 MW;  9B6D3B9DE488C854 CRC64;
     MSTSSSILDI PSKMFRILKN NTRETEQHLS SSTLDLISKS QLLAQCFDTQ EIMASLSKTV
     RSILESQNLE HKSTLTPYNS SQSLQLLVMN TSCTQFKWTT GSTSSVKALL EKELCRGLVP
     LNDITPKSNY VELSLLTPSI LIGNETSTTT TLPEIPLDME QSIISCVENT LLKEVQALSG
     QESCQEYFLS ANYQSLIPPQ VLLNLMKMSS VVDLSPLTLP NTRLWLKLSP FHGGTSVSYA
     TQIKGYANCA RREEKCLKNR LTKKQKNQEK GSFDARSVIT LGGKMYRYKV VVLRCEDQSD
     NLSELQFEPQ VEYTMDMVPH CWKELVKKRL IRAKGTWDLS CVEDLDLDHV EVRGDSLLHR
     SSVVHDLTSI VDDTLQEKLF SRTWLRQSLK YSGNILQRLS SLFATEGLKK ITLVNSDITP
     VQVGDKWLNF VDFGKSTVFF VKTLNNIHLA MTRQRESCNY IHEKFGRVRW LGAKPEQGAI
     VKVFAWCLNK KEFKFRDNQL KQYVCRQGVI KHEPCEYLNV EVLDEFVALN NDLNCVQKIK
     TYLAAYFGLK KVKLTQKNFM TPLITKKQEL VFQPCNCPNH QFYVAQFDKH VTLGLGRKDG
     ILFAEQVPSY AIILAVGFGT VETQLVTHYY SEMRRVYHPL DFQSNTFVFD HQGVMLEDIS
     PADYNDVGEE DYQLEYSGGF DQPFQNYHSD DEDQAFPDFE DERHPDEENW ARPIISSGES
     SVVSSRPSSP LVYSSLVPVA SPFGYMNGIR VFDICLADDL DFLQIHGQCP CARCKGLYFY
     QPIRPRGFTI FENVVEFFSF VEKCEVFEEI GPFFKMIEYS MLYNEYNIFY GLGKKIYQSD
     LVLPVKHLDQ LWKRAQLDID VVSEFENFKN SLQNINNVVY IAPYFNDQGE WNDIFDGYEF
     NLNDNQFWFQ AKPVYDLVCY IYQGFFSDSR PLEKLYQKLC LDYHTSAMLH TQTHLKYCYV
     ALLHSERAFQ MSINLDSLDN EQLHFLATMG MGDASLVGPT YLSEYHSNFN WYSIMSKACH
     YVKLEQLVGL TYQEKRLMIL SRVQEFYEQQ HRGPIQLILS PLKVVNLPPI TCTEGYCYQP
     VTRLFDTCVM PDIMKKLSRK RTSVSDVFGI LADYFKRTLS YRCFKVHEFC GIERQQEFSD
     MTTLKLVTDW CQDTYYFYNE YATMTDVEPK VQVSSDYYLK IPSEVVEHIR QFLPHNVNVG
     LMNYVSSNCD FDQCKFEFCL SGKGYVLGNM FFNRCAIQYV KTNLFIVLFK SRPLLYITQE
     SIYLSDFNVL QAQCLTGEFC LDFEPVQGKT LFGVYFTNGQ RYGQQWETLP RFSLKPLNSP
     RKRVPTQPFE ELAEVCIFKQ KLKLTQLHND CSVTPRVCSI PQTITATFQP YYCLENFYGV
     KAPKVIVSGH LATHYVKLTH KISKCVLVTK LAVARAFYFT PTSMGSHYHL DPMEGISFGK
     RATVQFEPVG LIKDVNLLVY QFGSHVSIQF FPEAPCIVAD GHYPSKYSGV WLGYLPSVEE
     CKIAQVNHRV YVPTILRTSK SAPFHIIQNG DMGRGPITVT YHYAKNFDNK SLTPMFKMFQ
     QVFEKSKDDI FKAFNTMSLE QKKVLSHFCG EFDEAYTLQT MSDEISFESS AYPDVVACSL
     AYILGYEMCL TVKVNAKNEK LDIGSQCERV FVDYDVKKNE WTLSPEEGED SDDNLDLPFE
     QYYEFKIGQT NVVLVQDDFK SVFEFLKSEQ GVDYVVNPAN SQLKHGGGIA KVISCMCGPK
     LQAWSNNYIT KNKTVPVTKA IKSPGFQLGK KVNIIHAVGP RVSDGDVFQK LDQAWRSVFD
     LCEDQHTILT SMLSTGIFGC TVNDSFNTFL SNVARLDKSL VVFVVTNMVE QYNQAFAVIK
     MYQQYHGLPN FGNTCWFNAL YQLLKSFSEK EQCVNDLLNC FDDFYDCPTS QCVEWVCEQL
     GVQFGQQQDA VEMLMKVFDV FKCDVRVGFD CLSRLQQVNC GFCVEVPAQA VLMFSGKDQC
     GHWTAARKIV DKWYTFDDNH VVQKDPVWQN VVLVLRDRGI FRSADFERKP ARRRRVSHRV
     PRDTLSQDAI TYIEDLRFSS GTCLSRYFVE SVESFVSGDN VSEVSDEQTC VEVAIEESDG
     HVEQICQSSV DCVGMPESFQ FTFSMPLQTF VQECDQKCED DFSQEHVECD QQFEPVEQVG
     QGGQQDGQVD QQIKESEQVV EPSAPSGQES PQALLQQVVD EVVYQIEQVK CDQKQDQDSV
     QCDEIEEINS RGEQTVQQQL QPILGHDLNE NEGPTLSVGA GKLVRCRSLA VTESNLSTSN
     TIFVWSEVLT HQYIGFKTDL MGLTYNIKFK LICYVLFLWF GVLCCTSHNT PFYMRLCIYL
     VLLWLSLMIW NASQINVKTG WNELYVLKLL TSIKLPNIVK FRCELVQWFV LKCLFVSFYV
     YDYVVKVCVS IFQMPQLRPF TWPFIKLGFV DTFLSHHILA FPEKVANQST LPTCGDKRYY
     VYVPSWCRAS FTSLVMRARE LTSTGRSKTL DNWHYQCCSK TAKPLSCFNV REFVFDQDCK
     HEAYGFLSSL CVYLLFYSGF LTFWLPLFCY YYVLFMCTFK NLPVDITKPI KWTVLQQVVN
     DVLSLVTKPL FGRPVCPPLT TYLTSTTADE AVKVSRSLLG RFCTPLGFQQ PVMNVENGVT
     VSNFGFFNPL MWPLFVVVLL DNRFIWFFNV LSYVMMPVFV IILFYFYLKK ICGCINFKGL
     SKCCTKHFNQ FSKPLVAAGV HGNRTNFTYQ PMQEHWCDRH SWYCPKEEHY MTPDMAVYIK
     NYYNLACAPT ADLVWCDYTK SAPTMTWSNF KYSSYKAKET VLCAPSSHAD SMLMAWYALL
     HNVRFTVNPN VVDLPPAVNT IYVSSDSEDS VQDKSQPDVK LRPKKPKGNF KKQSVAYFSR
     EPVDIWYYTT LVIVMGVLFM FMYSCLMVGQ YVVMPRDKFF GVNPTGYSYV NAPPYLHAAP
     PVLQNSDGMI LATQLKVPSI TYSVYRLLSG HLYFTKLIVS DNECTPPFGA ARLSNEFSCN
     GFTYVLPAHL RFFNRYVMLI HPDQLHMLPF EVEYGSHTRV CYTTGSNSVE CLPTFEIISP
     YVFVFIVVIF TVIFLILIRL YIVMYSYFKV FTYVVFKLLF VNIIMVLFVV CLPPLVPGVV
     FVLALWLCDS VMFLLYLAFL SLFILPWFYV LFFLFMVGGF VFWWMMRSAD VVHLTTDGLT
     FNGTFEQISK CVFPLNPLIV NRMLLDCQMS HSDLVEKSKL KTTEGKLANE MMKVFMTGET
     SYYQPSNFSF QSVFSKATSP FTLHARPPMP MFKLYVHFTG SCVGSTSTGT GFAIDDNTIV
     TAKHLFEYDD LKPTHVSVEI VTRSHSARSA SIIWKEPDVK GWTFKGENAY IQVENLKDFY
     IEDFKYLPFQ QIEKDFYKRM EPVTIYSVKY GSEFATQAWQ TVNGHFVCYN TEGGDSGAPL
     VCNGRIVGVH QGLCDNFKTT LASDFEGKMM TEVKGHHVDP PVYYKPIIIS AAYNKFVAGE
     DSSVGDGKNY HKFENEDFAC MCKELESVTF GDQLRRYCYN LPQFLEPLQY FHVPSFWQPF
     KKQSVSNNVS WVVEHLHFIF SIYFLICDFV AYWWLDDPFS VVLPLFFIVQ LLSTVFLKNV
     LFWTTSYLIT LAVTFYIHSE VAESMFLLGF LSDRVVNRMS LIIVVAIMCL FVVVRVVVNV
     KRAIFVFVVS VVLIFVHICL GIVQFNSFVN VVLFDVYAVF TALLTPQPVV AIIMLLLFDT
     KMLMSFAFIV IVLSFRVFKD YKFVKVLHNF CNFDFVLSQV SLFRYRHRNQ GNDPTHYEAL
     WLFLKELYYG IQDAKYEVFS PQAGSYNVKF LTDMTEQDQL EAVEQVQRRL QRFNIVQDKA
     SPRLVLYSKT IEFIKDQIQQ QRAVGANPFI ITTLTSNDIG LDNVEVHNPA NFKPEDLQAH
     MWFFSKSPVF IGQVPIPTNV QTAAVLDTTY NCQDLTADEK NNVAATLQIQ NAAITLSLFE
     KCTQFLESEL GEVPTLMWQA EDVADIKHLE SQIENLRKVL DGMQFGTTEY KATRKQLNIC
     QSQLDQAKAF ERKLAKFLEK VDQQQAITNE TAKQLSAFKN LVKQVYESYM SSLKVKVLEA
     NDASCLLTST DLPRKLVLMR PITGVDGIKI VEKANGCEIT AFGTTFNTGH GSNLAGLAYS
     TTQPLSAYPF IFNLEGIFKQ QANIGYKTVE CNMSSHNGSV LYKGKVVAVP SDDNPDFVVC
     GKGYKLDCGI NVLMIPSIVR YITLNLTDHL QKQSLKPRRR LQYRQQGVRL GGVNLGEHQA
     FSNELISTVG YTTWVSSTVC RDNTHKHPWF VQIPVNEKDP EWFMHNTQLK DNQWVVDLKP
     THWLVNADTG EQLFALSLTD EQALKAEAIL QKWSPITQDV ECWFKDLKGY YTVSGFQPLW
     PVCPVNICNV RLDPVFKPQS IVYADDPTHF LSLPVVNKNF LAAFYDLQEG FPGKKQVAPH
     ISLTMLKLSD EDIEKVEDIL DEMVLPNSWV TITNPHMMGK HYVCDVEGLD SLHDEVVSVL
     REHGIACDQK RLWKPHLTIG ELNDVSFDKF KDFAISCKLE DCDFVKLGAP KANARYEFIT
     TLPLGDFKLL RGAWSACRHL CFQNGAYQSS RSKHYIDLAT EYNAGIVKVN KSNTHSVEYQ
     SKRFMIKRVK DQSEFALAKT AFLPSIIPHH MEKQNGEWFL IRGPTSQWSL GDLVYAIWLG
     DQDYLSECGF VFNPSRDEFL DDANQRSFLA NLLEPAILNF SHIYWQVKMC KVPYKLTLDN
     VDLNGQLYDF GDYPCPNSVD NQSALFVLAE VWSMTRRPFP VAFARLLANE MEIPTDYQMF
     FQNILLSGSY LDKALCLNNV RPFLSDPANL TTTPFFSQHN GVWTHFYNPI YGLVECNLDE
     FAELPEVLQQ LVTVQGPITN NMTPAISVGE GVYAANVPSA SATKQKIPFY DVGLCQELTD
     AGVDCGEAFK YFYYLSNPAG ALADVCYYDY QGTGFYSPKL LAGVYDFMKR VTECYRINER
     FTYEQAKPRK SSMGINITGY QQDAVYRALG PENIARLFEY AQKAPLPFCT KIITKFALSA
     KARARTVSSC SFIASTIFRF AHKPVTSKMV EVAQNSGGFC LIGVSKYGLK FSKFLKDKYG
     AIEGFDVFGS DYTKCDRTFP LSFRALTAAL LYELGEWDEK SWLYLNEVNS YMLDTMLCDG
     MLLNKPGGTS SGDATTAHSN TFYNYMVHYV VAFKTILSDL SEGNKVMRIA AHNAYTTGDY
     QVFNTLLEDQ FQTNYFLNFL SDDSFIFSKP EALKIFTCEN FSNKLQTILH TKVDQTKSWS
     TKGHIEEFCS AHIIKTDGEY HFLPSRGRLL ASLLILDKLS DVDIYYMRFV AILCESAVYS
     RYQPEFFNGL FQVFLDKVQQ FRKDYCCDPC PPQLLEREFY ENLVFTSNSE VGIVDCYLEN
     FKLQCEFKQQ ANFDKVCFCC PNPAVSVCEE CYVPLPLCAY CYYVHVVISN HSKVEDKFKC
     FCGQDNIREL YIVLNNSICM YQCKNCVESD RLRISLLSDV DQIVRLPGFK SNSASIAKNG
     VAQLLTSVDN VDVSLDWNYQ ESVQQNVARI VYHSANMTQM SIEVVYVSFT LVRNDGSSAI
     LDIPNFKCPD TSYCLFYKPG KSGVLKFTGK GTLTSCYDNK NLTWFKVTCP DFNQPWRLAT
     CFVIQQHDVV YPPIKATQYE NVTFVMGPPG TGKTTFVYDT YLSKASSSNR FVYCAPTHRL
     VGDMDEKVDG AVVVSAYNDR TYRNPVWNKD DSYGVLLCTH NTLPFIKSAV LIADEVSLIP
     PHVMIKILSM GFKKVVLLGD PFQLSPVYKN HKVHFKYDTF YLLQLATQKR YLTACYRCPP
     QILSAFSKPY CDVGVDLVSF NNKPGKFDII VSKQLANIQD FSVLSVLSKE YPGYVILVNY
     RAAVDYAMQN GLGDVTTIDS SQGTTAANHL LVLFGASNFS KTVNRVIVGC SRSTTHLVVV
     CCPELFKHFQ PILNWPEPKY RYFGMEKQSD FNIIPEVSSL VFCDIEFWHY KADPNSKTRT
     VYPGQIAVVT SQTLQLYLGV FDDTGYKSAL RGLPKDVYVP PNWVWMRKHY PSYEQHAYNM
     QRLFKFIIDT TFGQPWFILY SCSNDLKSLK FYVEFDTCYF CSCGEMAICL MRDGNYKCRN
     CYGGMLISKL VNCKYLDVQK ERVKLQDAHD AICQQFHGDS HEALCDAVMT KCLYLASYEA
     AFKDTIHVKY KDLCLEIQYK ITSSFVRYDS VHKRYLYRDH GAMYYFRTPR SPMQNVYKYE
     VGSHAEYSIN ICTSYEGCQS FGKTCTKCIH IHCIVEQFMA DERFKEFILV SVVKSDYVEQ
     ALSPAAKALM LTVTKVEDKS FYISNGVRYD LYDYDLSKSV MRVVNSNVKP LPLYSVIVGL
     GINCTVGCVL PNVPMKLKDE LLITDVPLST LRLDLQTWYY ISWPTLSNKN SRWKLAGAQV
     YDCSVHIYIE ATGEQPLYYL QQGKGESLFE LPDTLFSTGR LYNLDHDAAQ NFNVKQLAIE
     TMPNNHHVFS GDFTEVGTDI GGVHHVVALN GYKGSIIPNY VKPIATGLIN VGRAVKRTTL
     VDVCANQLYE KVKQQLEGVK VSKVIFVNID FQDVQFMVFA NGEDDIQTFY PQKDFVRSYY
     EWPNILPQIE SHYDLKNYGQ NPTFMPQPVN FAKYTQICTF IQDHVKVARN ALVWHLGAAG
     VDGCSPGDIV LSSFFKECLV YSWDIKDYST LLDKHSYDCN FRPNLIVSDI YNVSSNVSEV
     LDDCVHRLAL GGTIVFKTTE SSRPDIQLSQ FTKYFSAVQF FTAGVNTSSS EVFVVLKYKL
     YSEPIGEELC SPNILSRIAA YRNKLCIVPN FKVFSTSFSY KYSGVKFVQK CFYVSVPRQF
     CASGLIQEVP MLCQMEH
 
 
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