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Non-structural polyprotein p200 (p200) [Cleaved into: Protease p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase/triphosphatase/helicase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]

 POLN_RUBVM              Reviewed;        2116 AA.
Q86500;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
16-JAN-2019, entry version 113.
RecName: Full=Non-structural polyprotein p200;
Short=p200;
Contains:
RecName: Full=Protease/methyltransferase p150;
Short=p150;
EC=3.4.22.- {ECO:0000269|PubMed:12076835, ECO:0000269|PubMed:9557742};
Contains:
RecName: Full=RNA-directed RNA polymerase p90;
Short=p90;
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:11437666};
EC=3.6.1.15 {ECO:0000269|PubMed:8599224};
EC=3.6.4.13;
Rubella virus (strain M33) (RUBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Rubivirus.
NCBI_TaxID=11043;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], MUTAGENESIS OF CYS-1152 AND
GLY-1300, PROTEOLYTIC CLEAVAGE (NON-STRUCTURAL POLYPROTEIN P200), AND
ACTIVE SITE.
PubMed=9656995; DOI=10.1006/viro.1998.9179;
Yao J., Yang D., Chong P., Hwang D., Liang Y., Gillam S.;
"Proteolytic processing of rubella virus nonstructural proteins.";
Virology 246:74-82(1998).
[2]
FUNCTION (PROTEASE/METHYLTRANSFERASE P150).
PubMed=1518855;
Koonin E.V., Gorbalenya A.E., Purdy M.A., Rozanov M.N., Reyes G.R.,
Bradley D.W.;
"Computer-assisted assignment of functional domains in the
nonstructural polyprotein of hepatitis E virus: delineation of an
additional group of positive-strand RNA plant and animal viruses.";
Proc. Natl. Acad. Sci. U.S.A. 89:8259-8263(1992).
[3]
ACTIVE SITE, PROTEOLYTIC CLEAVAGE (NON-STRUCTURAL POLYPROTEIN P200),
AND MUTAGENESIS OF HIS-1248; HIS-1273; HIS-1290; GLY-1300; GLY-1301;
GLY-1302 AND TYR-1316.
PubMed=8676497;
Chen J.P., Strauss J.H., Strauss E.G., Frey T.K.;
"Characterization of the rubella virus nonstructural protease domain
and its cleavage site.";
J. Virol. 70:4707-4713(1996).
[4]
CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE P90), AND FUNCTION
(RNA-DIRECTED RNA POLYMERASE P90).
PubMed=8599224; DOI=10.1006/viro.1996.0125;
Gros C., Wengler G.;
"Identification of an RNA-stimulated NTPase in the predicted helicase
sequence of the Rubella virus nonstructural polyprotein.";
Virology 217:367-372(1996).
[5]
INTERACTION WITH HUMAN RB1 (RNA-DIRECTED RNA POLYMERASE P90).
PubMed=9608663; DOI=10.1023/A:1007998023047;
Atreya C.D., Lee N.S., Forng R.Y., Hofmann J., Washington G.,
Marti G., Nakhasi H.L.;
"The rubella virus putative replicase interacts with the
retinoblastoma tumor suppressor protein.";
Virus Genes 16:177-183(1998).
[6]
FUNCTION (PROTEASE/METHYLTRANSFERASE P150), COFACTOR, PROTEOLYTIC
CLEAVAGE (NON-STRUCTURAL POLYPROTEIN P200), AND CATALYTIC ACTIVITY
(PROTEASE/METHYLTRANSFERASE P150).
PubMed=9557742;
Liu X., Ropp S.L., Jackson R.J., Frey T.K.;
"The rubella virus nonstructural protease requires divalent cations
for activity and functions in trans.";
J. Virol. 72:4463-4466(1998).
[7]
MUTAGENESIS OF CYS-1904, AND INTERACTION WITH HUMAN RB1 (RNA-DIRECTED
RNA POLYMERASE P90).
PubMed=10073691; DOI=10.1099/0022-1317-80-2-327;
Forng R.Y., Atreya C.D.;
"Mutations in the retinoblastoma protein-binding LXCXE motif of
rubella virus putative replicase affect virus replication.";
J. Gen. Virol. 80:327-332(1999).
[8]
ZINC-BINDING (PROTEASE/METHYLTRANSFERASE P150), AND MUTAGENESIS OF
CYS-1152; CYS-1167; CYS-1175; CYS-1178; HIS-1190; HIS-1204; CYS-1225;
CYS-1227; HIS-1236 AND HIS-1273.
PubMed=10846076; DOI=10.1128/JVI.74.13.5949-5956.2000;
Liu X., Yang J., Ghazi A.M., Frey T.K.;
"Characterization of the zinc binding activity of the rubella virus
nonstructural protease.";
J. Virol. 74:5949-5956(2000).
[9]
FUNCTION (PROTEASE/METHYLTRANSFERASE P150), DOMAIN
(PROTEASE/METHYLTRANSFERASE P150), AND PROTEOLYTIC CLEAVAGE
(NON-STRUCTURAL POLYPROTEIN P200).
PubMed=10823845; DOI=10.1128/JVI.74.12.5412-5423.2000;
Liang Y., Yao J., Gillam S.;
"Rubella virus nonstructural protein protease domains involved in
trans-and cis-cleavage activities.";
J. Virol. 74:5412-5423(2000).
[10]
MUTAGENESIS OF GLY-1966; ASP-1967 AND ASP-1968, AND CATALYTIC ACTIVITY
(RNA-DIRECTED RNA POLYMERASE P90).
PubMed=11437666; DOI=10.1006/viro.2001.0939;
Wang X., Gillam S.;
"Mutations in the GDD motif of rubella virus putative RNA-dependent
RNA polymerase affect virus replication.";
Virology 285:322-331(2001).
[11]
FUNCTION (NON-STRUCTURAL POLYPROTEIN P200), PROTEOLYTIC CLEAVAGE
(NON-STRUCTURAL POLYPROTEIN P200), FUNCTION
(PROTEASE/METHYLTRANSFERASE P150), AND FUNCTION (RNA-DIRECTED RNA
POLYMERASE P90).
PubMed=11289813; DOI=10.1006/viro.2001.0862;
Liang Y., Gillam S.;
"Rubella virus RNA replication is cis-preferential and synthesis of
negative- and positive-strand RNAs is regulated by the processing of
nonstructural protein.";
Virology 282:307-319(2001).
[12]
FUNCTION (NON-STRUCTURAL POLYPROTEIN P200), FUNCTION
(PROTEASE/METHYLTRANSFERASE P150), FUNCTION (RNA-DIRECTED RNA
POLYMERASE P90), PROTEOLYTIC CLEAVAGE (NON-STRUCTURAL POLYPROTEIN
P200), AND CATALYTIC ACTIVITY (PROTEASE/METHYLTRANSFERASE P150).
PubMed=12076835; DOI=10.1016/S0168-1702(02)00077-1;
Wang X., Liang Y., Gillam S.;
"Rescue of rubella virus replication-defective mutants using vaccinia
virus recombinant expressing rubella virus nonstructural proteins.";
Virus Res. 86:111-122(2002).
[13]
DOMAIN (PROTEASE/METHYLTRANSFERASE P150), AND MUTAGENESIS OF ASP-1210
AND ASP-1217.
PubMed=17475644; DOI=10.1128/JVI.00605-07;
Zhou Y., Tzeng W.P., Yang W., Zhou Y., Ye Y., Lee H.W., Frey T.K.,
Yang J.;
"Identification of a Ca2+-binding domain in the rubella virus
nonstructural protease.";
J. Virol. 81:7517-7528(2007).
[14]
SUBCELLULAR LOCATION (PROTEASE/METHYLTRANSFERASE P150), DOMAIN
(PROTEASE/METHYLTRANSFERASE P150), AND SUBCELLULAR LOCATION
(RNA-DIRECTED RNA POLYMERASE P90).
PubMed=19539969; DOI=10.1016/j.virol.2009.05.019;
Matthews J.D., Tzeng W.P., Frey T.K.;
"Determinants of subcellular localization of the rubella virus
nonstructural replicase proteins.";
Virology 390:315-323(2009).
[15]
INTERACTION WITH HOST CALM1 (PROTEASE/METHYLTRANSFERASE P150), AND
MUTAGENESIS OF ARG-1165.
PubMed=20086014; DOI=10.1074/jbc.M109.097063;
Zhou Y., Tzeng W.P., Wong H.C., Ye Y., Jiang J., Chen Y., Huang Y.,
Suppiah S., Frey T.K., Yang J.J.;
"Calcium-dependent association of calmodulin with the rubella virus
nonstructural protease domain.";
J. Biol. Chem. 285:8855-8868(2010).
[16]
FUNCTION (PROTEASE/METHYLTRANSFERASE P150), SUBCELLULAR LOCATION
(PROTEASE/METHYLTRANSFERASE P150), AND MUTAGENESIS OF GLU-36; ARG-38;
ASP-39; THR-42; GLN-45; LYS-46; ARG-47 AND ILE-49.
PubMed=20696450; DOI=10.1016/j.virol.2010.07.025;
Matthews J.D., Tzeng W.P., Frey T.K.;
"Analysis of the function of cytoplasmic fibers formed by the rubella
virus nonstructural replicase proteins.";
Virology 406:212-227(2010).
[17]
INTERACTION WITH RNA-DIRECTED RNA POLYMERASE P90
(PROTEASE/METHYLTRANSFERASE P150), INTERACTION WITH
PROTEASE/METHYLTRANSFERASE P150 (RNA-DIRECTED RNA POLYMERASE P90),
MUTAGENESIS OF GLU-36; ARG-38; ASP-39; THR-42; GLN-45; LYS-46; ARG-47
AND ILE-49, AND SUBCELLULAR LOCATION (NON-STRUCTURAL POLYPROTEIN
P200).
PubMed=22491463; DOI=10.1128/JVI.06132-11;
Matthews J.D., Tzeng W.P., Frey T.K.;
"Determinants in the maturation of rubella virus p200 replicase
polyprotein precursor.";
J. Virol. 86:6457-6469(2012).
[18]
INTERACTION WITH HOST C1QBP (ROTEASE/METHYLTRANSFERASE P150), DOMAIN
(ROTEASE/METHYLTRANSFERASE P150), AND MUTAGENESIS OF 727-PRO--PRO-730
AND 747-PRO--PRO-750.
PubMed=22238231; DOI=10.1099/vir.0.038901-0;
Suppiah S., Mousa H.A., Tzeng W.P., Matthews J.D., Frey T.K.;
"Binding of cellular p32 protein to the rubella virus P150 replicase
protein via PxxPxR motifs.";
J. Gen. Virol. 93:807-816(2012).
[19]
INTERACTION WITH THE CAPSID PROTEIN (PROTEASE/METHYLTRANSFERASE P150),
AND SUBCELLULAR LOCATION (PROTEASE/METHYLTRANSFERASE P150).
STRAIN=RVi/Japan/Hiroshima/2003;
PubMed=25056903; DOI=10.1128/JVI.01758-14;
Sakata M., Otsuki N., Okamoto K., Anraku M., Nagai M., Takeda M.,
Mori Y.;
"Short self-interacting N-terminal region of rubella virus capsid
protein is essential for cooperative actions of capsid and
nonstructural p150 proteins.";
J. Virol. 88:11187-11198(2014).
-!- FUNCTION: Non-structural polyprotein p200: Probable principal
replicase for the negative-strand DNA, which replicates the 40S
(+) genomic RNA into (-) antigenomic RNA. It cannot replicate the
(-) into (+) until cleaved into p150 and p90 mature proteins.
{ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835}.
-!- FUNCTION: Protease/methyltransferase p150: Protease that cleaves
the precursor polyprotein into two mature products
(PubMed:10823845, PubMed:9557742). Together with RNA-directed RNA
polymerase p90, replicates the 40S genomic and antigenomic RNA by
recognizing replications specific signals. The heterodimer
P150/p90 is probably the principal replicase for positive-strand
genomic RNA and the 24S subgenomic RNA, which codes for structural
proteins (PubMed:11289813, PubMed:12076835). Responsible for the
mRNA-capping of the viral mRNAs. This function is necessary since
all viral RNAs are synthesized in the cytoplasm, and host capping
enzymes are restricted to the nucleus (Probable). Forms fibers
late in the infection that may be involved in cell-to-cell spread
of the virus RNA in the absence of virus particle formation
(PubMed:20696450). {ECO:0000269|PubMed:10823845,
ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835,
ECO:0000269|PubMed:20696450, ECO:0000269|PubMed:9557742,
ECO:0000305|PubMed:1518855}.
-!- FUNCTION: RNA-directed RNA polymerase p90: Together with
protease/methyltransferase p150, replicates the 40S genomic and
antigenomic RNA by recognizing replications specific signals. The
heterodimer P150/p90 is probably the principal replicase for
positive-strand genomic RNA and the 24S subgenomic RNA, which
codes for structural proteins (PubMed:11289813, PubMed:12076835).
A helicase activity is probably also present (PubMed:8599224).
{ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835,
ECO:0000269|PubMed:8599224}.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00539, ECO:0000269|PubMed:11437666};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000269|PubMed:8599224};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Zn(2+) is necessary for the protease activity. The protease
can also function efficiently with Cd(2+) and Co(2+).
{ECO:0000269|PubMed:9557742};
-!- SUBUNIT: RNA-directed RNA polymerase p90: Interacts with human
RB1/retinoblastoma protein (PubMed:9608663, PubMed:10073691).
Protease/methyltransferase p150: Interacts with RNA-directed RNA
polymerase p90 (PubMed:22491463). Protease/methyltransferase p150:
Interacts with host CALM1; this interaction is necessary for the
protease activity and viral infectivity (PubMed:20086014).
Protease/methyltransferase p150: Interacts with host C1QBP
(PubMed:22238231). Protease/methyltransferase p150: Interacts with
the capsid protein (PubMed:25056903). RNA-directed RNA polymerase
p90: Interacts with protease/methyltransferase p150
(PubMed:22491463). {ECO:0000269|PubMed:10073691,
ECO:0000269|PubMed:20086014, ECO:0000269|PubMed:22238231,
ECO:0000269|PubMed:22491463, ECO:0000269|PubMed:25056903,
ECO:0000269|PubMed:9608663}.
-!- SUBCELLULAR LOCATION: Non-structural polyprotein p200: Host
membrane {ECO:0000269|PubMed:19539969}. Host cytoplasm, host
perinuclear region {ECO:0000269|PubMed:22491463}. Host cytoplasm
{ECO:0000269|PubMed:19539969}. Note=Localizes to cytoplasmic foci
at 24 hpi. {ECO:0000269|PubMed:19539969}.
-!- SUBCELLULAR LOCATION: Protease/methyltransferase p150: Host
membrane {ECO:0000269|PubMed:19539969,
ECO:0000269|PubMed:25056903}. Host cytoplasm, host perinuclear
region {ECO:0000269|PubMed:20696450, ECO:0000269|PubMed:22491463}.
Host cytoplasm {ECO:0000269|PubMed:19539969,
ECO:0000269|PubMed:25056903}. Note=At 36 hpi, localizes to the
host cytoplasm, probably in vesicles inside host vacuoles of
endosomal and lysosomal origin (By similarity). At 72 hpi,
localizes to filamentous structures in the host cytoplasm
(PubMed:25056903). {ECO:0000250|UniProtKB:P13889,
ECO:0000269|PubMed:25056903}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase p90: Host
membrane {ECO:0000269|PubMed:19539969}. Host cytoplasm
{ECO:0000269|PubMed:19539969}. Note=Localizes to the cytoplasm and
to the cytoplasmic fibers formed by protease/methyltransferase
p150. {ECO:0000269|PubMed:19539969}.
-!- DOMAIN: Protease/methyltransferase p150: The N-terminus has a
methyltransferase activity for mRNA-capping. The C-terminus
harbors a protease active in cis or in trans which specifically
cleaves and releases the two mature proteins (PubMed:10823845).
Both the N-terminus and C-terminus are required for fiber
formation. The N-terminus is involved in associating with
membranes (PubMed:19539969). An EF-hand Ca(2+)-binding motif is
present in the protease (PubMed:17475644). Also contains 3 SH3-
binding motifs that are responsible for the interaction with host
C1QBP (PubMed:22238231). {ECO:0000269|PubMed:10823845,
ECO:0000269|PubMed:17475644, ECO:0000269|PubMed:19539969,
ECO:0000269|PubMed:22238231}.
-!- PTM: Non-structural polyprotein p200: Specific enzymatic cleavage
by its own cysteine protease yield mature proteins p150 and p90.
{ECO:0000269|PubMed:10823845, ECO:0000269|PubMed:11289813,
ECO:0000269|PubMed:12076835, ECO:0000269|PubMed:8676497,
ECO:0000269|PubMed:9557742, ECO:0000269|PubMed:9656995}.
-!- MISCELLANEOUS: Rubella virus in utero infection has frequently
severe consequences on normal fetal development, collectively
known as congenital rubella syndrome (CRS) (Probable). The
teratogenicity of the virus is possibly due to the interaction
between the p90 protein and the human RB1/retinoblastoma protein
(PubMed:9608663). {ECO:0000303|PubMed:9608663, ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA51087.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; X72393; CAA51087.1; ALT_SEQ; Genomic_RNA.
PIR; S38480; S38480.
ProteinModelPortal; Q86500; -.
IntAct; Q86500; 22.
Proteomes; UP000007143; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR002588; Alphavirus-like_MT_dom.
InterPro; IPR002589; Macro_dom.
InterPro; IPR039658; Macro_domain_protein.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008738; Peptidase_C27.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR022245; Rubi_NSP_C.
InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
PANTHER; PTHR11106; PTHR11106; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF05407; Peptidase_C27; 1.
Pfam; PF00978; RdRP_2; 1.
Pfam; PF12601; Rubi_NSP_C; 1.
Pfam; PF01443; Viral_helicase1; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51743; ALPHAVIRUS_MT; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
ATP-binding; Calcium; Complete proteome; Helicase; Host cytoplasm;
Host membrane; Hydrolase; Membrane; Metal-binding; Nucleotide-binding;
Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
Thiol protease; Transferase; Viral RNA replication; Zinc.
CHAIN 1 2116 Non-structural polyprotein p200.
/FTId=PRO_0000249224.
CHAIN 1 1301 Protease/methyltransferase p150.
/FTId=PRO_0000041224.
CHAIN 1302 2116 RNA-directed RNA polymerase p90.
/FTId=PRO_0000041225.
DOMAIN 57 247 Alphavirus-like MT. {ECO:0000255|PROSITE-
ProRule:PRU01079}.
DOMAIN 806 985 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1109 1274 Peptidase C27. {ECO:0000255}.
DOMAIN 1193 1228 EF-hand. {ECO:0000269|PubMed:17475644}.
DOMAIN 1320 1468 (+)RNA virus helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00990}.
DOMAIN 1469 1609 (+)RNA virus helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00990}.
DOMAIN 1870 1981 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1352 1359 NTP. {ECO:0000255|PROSITE-
ProRule:PRU00990}.
REGION 36 49 Required for efficient proteolysis and
P150-P90 interaction.
REGION 1152 1183 Interaction with host CALM1.
{ECO:0000269|PubMed:20086014}.
REGION 1700 1900 Involved in P150-P90 interaction.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MOTIF 727 732 PxxPxR; class II SH3-binding.
{ECO:0000269|PubMed:22238231}.
MOTIF 747 752 PxxPxR; class II SH3-binding.
{ECO:0000269|PubMed:22238231}.
MOTIF 761 766 PxxPxR; class II SH3-binding.
{ECO:0000269|PubMed:22238231}.
MOTIF 1902 1906 Human RB1 binding.
{ECO:0000269|PubMed:10073691}.
ACT_SITE 1152 1152 For cysteine protease activity.
{ECO:0000269|PubMed:9656995}.
ACT_SITE 1273 1273 For cysteine protease activity.
{ECO:0000269|PubMed:8676497}.
METAL 1175 1175 Zinc. {ECO:0000269|PubMed:10846076}.
METAL 1178 1178 Zinc. {ECO:0000269|PubMed:10846076}.
METAL 1227 1227 Zinc. {ECO:0000269|PubMed:10846076}.
METAL 1273 1273 Zinc. {ECO:0000269|PubMed:10846076}.
SITE 1301 1302 Cleavage; autocatalytic.
{ECO:0000269|PubMed:8676497,
ECO:0000269|PubMed:9656995}.
MUTAGEN 36 36 E->A: Loss of P150-P90 interaction. No
effect on processing efficiency or fiber
formation. {ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 38 38 R->A: No effect on P150-P90 interaction.
No effect on processing efficiency or
fiber formation.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 39 39 D->A: No effect on P150-P90 interaction.
No effect on processing efficiency or
fiber formation.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 42 42 T->A: Slight loss of P150-P90
interaction. No effect on processing
efficiency or fiber formation.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 45 45 Q->A: Slight loss of P150-P90
interaction. No effect on processing
efficiency or fiber formation.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 46 46 K->A: No effect on P150-P90 interaction.
Inhibits fiber formation by p150.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 47 47 R->A: No effect on P150-P90 interaction.
No effect on processing efficiency or
fiber formation.
{ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 49 49 I->A: Loss of P150-P90 interaction. No
effect on processing efficiency or fiber
formation. {ECO:0000269|PubMed:20696450,
ECO:0000269|PubMed:22491463}.
MUTAGEN 727 730 PPPP->APPA: Complete loss of interaction
with host C1QBP; when assiciated with
Ala-747 and Ala-749.
{ECO:0000269|PubMed:22238231}.
MUTAGEN 747 750 PPAP->APAA: Complete loss of interaction
with host C1QBP; when assiciated with
Ala-727 and Ala-729.
{ECO:0000269|PubMed:22238231}.
MUTAGEN 1152 1152 C->S: Complete loss of protease activity.
{ECO:0000269|PubMed:9656995}.
MUTAGEN 1152 1152 C->S: No effect on Zn(2+) binding;
complete loss of protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1165 1165 R->D: Complete loss of interaction of
p150 with host CALM1.
{ECO:0000269|PubMed:20086014}.
MUTAGEN 1165 1165 R->Q: Decreased interaction of p150 with
host CALM1.
{ECO:0000269|PubMed:20086014}.
MUTAGEN 1167 1167 C->S: No effect on Zn(2+) binding;
complete loss of protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1175 1175 C->S: Complete loss of Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1178 1178 C->S: Complete loss of Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1190 1190 H->L: No effect on Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1204 1204 H->L: No effect on Zn(2+) binding;
complete loss of protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1210 1210 D->A: 20 fold decreased infectivity. Loss
of Ca(2+) binding.
{ECO:0000269|PubMed:17475644}.
MUTAGEN 1217 1217 D->A: 20 fold decreased infectivity. Loss
of Ca(2+) binding.
{ECO:0000269|PubMed:17475644}.
MUTAGEN 1225 1225 C->S: No effect on Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1227 1227 C->S: Complete loss of Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1236 1236 H->S: No effect on protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1248 1248 H->L: No effect on protease activity.
{ECO:0000269|PubMed:8676497}.
MUTAGEN 1273 1273 H->L: Complete loss of protease activity.
{ECO:0000269|PubMed:8676497}.
MUTAGEN 1273 1273 H->S: Complete loss of Zn(2+) binding and
protease activity.
{ECO:0000269|PubMed:10846076}.
MUTAGEN 1290 1290 H->L: No effect on protease activity.
{ECO:0000269|PubMed:8676497}.
MUTAGEN 1300 1300 G->A: Partial loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1300 1300 G->S: Complete loss of polyprotein
cleavage. {ECO:0000269|PubMed:9656995}.
MUTAGEN 1300 1300 G->V: Complete loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1301 1301 G->A: Almost complete loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1301 1301 G->V: Complete loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1302 1302 G->A: Partial loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1302 1302 G->V: Complete loss of proteolytic
cleavage of non-structural polyprotein
p200. {ECO:0000269|PubMed:8676497}.
MUTAGEN 1316 1316 Y->M: No effect on proteolytic cleavage
of non-structural polyprotein p200.
{ECO:0000269|PubMed:8676497}.
MUTAGEN 1904 1904 C->G: Partial loss of human RB1 binding
and 47% loss of virus replication.
{ECO:0000269|PubMed:10073691}.
MUTAGEN 1904 1904 C->R: Complete loss of human RB1 binding
and virus replication.
{ECO:0000269|PubMed:10073691}.
MUTAGEN 1966 1966 G->A: Reduces virus infectivity.
{ECO:0000269|PubMed:11437666}.
MUTAGEN 1967 1967 D->A: Complete loss of virus replication.
{ECO:0000269|PubMed:11437666}.
MUTAGEN 1968 1968 D->A: Complete loss of virus replication.
{ECO:0000269|PubMed:11437666}.
SEQUENCE 2116 AA; 230910 MW; 04DD4C97B704EC8E CRC64;
MEKLLDEVLA PGGPYNLTVG SWVRDHVRSI VEGAWEVRDV VTAAQKRAIV AVIPRPVFTQ
MQVSDHPALH AISRYTRRHW IEWGPKEALH VLIDPSPGLL REVARVERRW VALCLHRTAR
KLATALAETA SEAWHADYVC ALRGAPSGPF YVHPEDVPHG GRAVADRCLL YYTPMQMCEL
MRTIDATLLV AVDLWPVALA AHVGDDWDDL GIAWHLDHDG GCPADCRGAG AGPTPGYTRP
CTTRIYQVLP DTAHPGRLYR CGPRLWTRDC AVAELSWEVA QHCGHQARVR AVRCTLPIRH
VRSLQPSARV RLPDLVHLAE VGWWRWFSLP RPVFQRMLSY CKTLSPDAYY SERVFKFKNA
LSHSITLAGN VLQEGWKGTC AEEDALCAYV AFRAWQSNAR LAGIMKSAKR CAADSLSVAG
WLDTIWDAIK RFFGSVPLAE RMEEWEQDAA VAAFDRGPLE DGGRHLDTVQ PPKSPPRPEI
AATWIVHAAS ADRHCACAPR CDVPRERPSA PAGPPDDEAL IPPWLFAERR ALRCREWDFE
ALRARADTAA APAPLAPRPA RYPTVLYRHP AHHGPWLTLD EPGGADAALV LCDPLGQPLR
GPERHYAAGA HMCAQARGLQ AFVRVVPPPE RPWADGGARA WAKFFRGCAW AQRLLGEPAV
MHLPYTDGDV PKLIALALRT LAQQGAALAL SVRDLPRGTA FEANAVTAAV RAGPGQLAAT
SPPPGDPPPP RRARRSQRHS DARGTPPPAP VRDPPRPQPS PPAPPRVGDP VPPTTAEPAD
RARHAELEVV YEPSGPPTST KADPDSDIVE SYARAAGPVH LRVRDIMDPP PGCKVVVNAA
NEGLLAGSGV CGAIFANATA ALAADCRRLA PCPIGEAVAT PGHGCGYTHI IHAVAPRRPR
DPAALEEGEA LLERAYRSIV ALAAARRWAR VACPLLGAGV YGWSAAESLR AALAATRAEP
AERVSLHICH PDRATLTHAS VLVGAGLAAR RVSPPPTEPL ASCPAGDPGR PAQRSASPPA
TPLGDATAPE PRGCQGCELC RYTRVTNDRA YVNLWLERDR GATSWAMRIP EVVVYGPEHL
ATHFPLNHYS VLKPAEVRPP RGMCGSDMWR CRGWQGMPQV RCTPSNAHAA LCRTGVPPRV
STRGGELDPN TCWLRAAANV AQAARACGAY TSAGCPKCAY GRALSEARTH EDFAALSQWW
SASHADASPD GTGDPLDPLM ETVGCACSRV WVGSEHEAPP DHLLVSLHRA PNGPWGVVLE
VRARPEGGNP TGHFVCAVGG GPRRVSDRPH LWLAVPLSRG GGTCAATDEG LAQAYYDDLE
VRRLGDDAMA RAALASIQRP RKGPYNIRVW NMAAGAGKTT RILAAFTRED LYVCPTNALL
HEIQAKLRAR DIDIKNAATY ERALTKPLAA YRRIYIDEAF TLGGEYCAFV ASQTTAEVIC
VGDRDQCGPH YANNCRTPVP DRWPTGRSRH TWRFPDCWAA RLRAGLDYDI EGERTGTFAC
NLWDGRQVDL HLAFSRETVR RLHEAGIRAY TVREAQGMSV GTACIHVGRD GTDVALALTR
DLAIVSLTRA SDALYLHELE DGLLRAAGLS AFLDAGALAE LKEVPAGIDR VVAVEQAPPP
LPPADGIPEA QDVPPFCPRT LEELVFGRAG HPHYADLNRV TEGEREVRYM RISRHLLNKN
HTEMPGTERV LSAVCAVRRY RAGEDGSTLR TAVARQHPRP FRQIPPPRVT AGVAQEWRMT
YLRERIDLTD VYTQMGVAAR ELTDRYTRRY PEIFAGMCTA QSLSVPAFLK ATLKCVDAAL
GPRDTEDCHA AQGKAGLEIR AWAKEWVQVM SPHFRAIQKI IMRALRPQFL VAAGHTEPEV
DAWWQAHYTT NAIEVDFTEF DMNQTLATRD VELEISAALL GLPCAEDYRA LRAGSYCTLR
ELGSTETGCE RTSGEPATLL HNTTVAMCMA MRMVPKGVRW AGIFQGDDMV IFLPEGARNA
ALKWTPAEVG LFGFHIPVKH VSTPTPSFCG HVGTAAGLFH DVMHQAIKVL CRRFDPDVLE
EQQVALLDRL RGVYAALPDT VAANAAYYDY SAERVLAIVR ELTAYARGRG LDHPATIGAL
EEIQTPYARA NLHDAD


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