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Chondroitinase-B (EC 4.2.2.19) (Chondroitin sulfate B lyase) (Chondroitin-B eliminase) (Chondroitin-B lyase)

 CSLB_PEDHD              Reviewed;         506 AA.
Q46079; C6Y218;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 2.
16-JAN-2019, entry version 103.
RecName: Full=Chondroitinase-B;
EC=4.2.2.19;
AltName: Full=Chondroitin sulfate B lyase;
AltName: Full=Chondroitin-B eliminase;
AltName: Full=Chondroitin-B lyase;
Flags: Precursor;
Name=cslB; OrderedLocusNames=Phep_0789;
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM
7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Pedobacter.
NCBI_TaxID=485917;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10618199; DOI=10.1128/AEM.66.1.29-35.2000;
Tkalec A.L., Fink D., Blain F., Zhang-Sun G., Laliberte M.,
Bennett D.C., Gu K., Zimmermann J.J.F., Su H.;
"Isolation and expression in Escherichia coli of cslA and cslB, genes
coding for the chondroitin sulfate-degrading enzymes chondroitinase AC
and chondroitinase B, respectively, from Flavobacterium heparinum.";
Appl. Environ. Microbiol. 66:29-35(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
NCIMB 9290 / NRRL B-14731 / HIM 762-3;
PubMed=21304637; DOI=10.4056/sigs.22138;
Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M.,
Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
Kyrpides N.C., Klenk H.P., Detter J.C.;
"Complete genome sequence of Pedobacter heparinus type strain (HIM
762-3).";
Stand. Genomic Sci. 1:54-62(2009).
[3]
CHARACTERIZATION, AND MUTAGENESIS OF LYS-250; HIS-272; GLU-333;
ARG-363 AND ARG-364.
PubMed=12063249; DOI=10.1074/jbc.M201552200;
Pojasek K., Raman R., Kiley P., Venkataraman G., Sasisekharan R.;
"Biochemical characterization of the chondroitinase B active site.";
J. Biol. Chem. 277:31179-31186(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
GLN-26.
PubMed=10600383; DOI=10.1006/jmbi.1999.3292;
Huang W., Matte A., Li Y., Kim Y.S., Linhardt R.J., Su H., Cygler M.;
"Crystal structure of chondroitinase B from Flavobacterium heparinum
and its complex with a disaccharide product at 1.7 A resolution.";
J. Mol. Biol. 294:1257-1269(1999).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11327856; DOI=10.1021/bi0024254;
Huang W., Boju L., Tkalec A.L., Su H., Yang H.O., Gunay N.S.,
Linhardt R.J., Kim Y.S., Matte A., Cygler M.;
"Active site of chondroitin AC lyase revealed by the structure of
enzyme-oligosaccharide complexes and mutagenesis.";
Biochemistry 40:2359-2372(2001).
-!- FUNCTION: Cleaves the glycosaminoglycan, dermatan sulfate.
-!- CATALYTIC ACTIVITY:
Reaction=Eliminative cleavage of dermatan sulfate containing
(1->4)-beta-D-hexosaminyl and (1->3)-beta-D-glucurosonyl or
(1->3)-alpha-L-iduronosyl linkages to disaccharides containing
4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-
unsaturated dermatan-sulfate disaccharide (Delta-UA-GalNAc-4S).;
EC=4.2.2.19;
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U27584; AAC83384.1; -; Genomic_DNA.
EMBL; CP001681; ACU03011.1; -; Genomic_DNA.
RefSeq; WP_012780957.1; NZ_AQGK01000003.1.
PDB; 1DBG; X-ray; 1.70 A; A=1-506.
PDB; 1DBO; X-ray; 1.70 A; A=1-506.
PDB; 1OFL; X-ray; 1.70 A; A=27-506.
PDB; 1OFM; X-ray; 1.80 A; A=27-506.
PDBsum; 1DBG; -.
PDBsum; 1DBO; -.
PDBsum; 1OFL; -.
PDBsum; 1OFM; -.
SMR; Q46079; -.
STRING; 485917.Phep_0789; -.
DrugBank; DB04492; 2-(Acetylamino)-2-Deoxy-4-O-Sulfo-Alpha-D-Galactopyranose.
DrugBank; DB03863; 2-O-Methyl Fucose.
DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid.
DrugBank; DB04515; 6-Deoxy-2-O-Methyl-Alpha-L-Galactopyranose.
DrugBank; DB01872; Acetylgalactosamine-4-Sulfate.
DrugBank; DB03389; alpha-D-Xylopyranose.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB03088; Pyroglutamic Acid.
CAZy; PL6; Polysaccharide Lyase Family 6.
PRIDE; Q46079; -.
EnsemblBacteria; ACU03011; ACU03011; Phep_0789.
KEGG; phe:Phep_0789; -.
KO; K19053; -.
OMA; RNDIGRC; -.
OrthoDB; 1055328at2; -.
BioCyc; MetaCyc:MONOMER-15800; -.
BioCyc; PHEP485917:G1GFH-804-MONOMER; -.
BRENDA; 4.2.2.19; 2286.
SABIO-RK; Q46079; -.
EvolutionaryTrace; Q46079; -.
Proteomes; UP000000852; Chromosome.
GO; GO:0033999; F:chondroitin B lyase activity; IEA:UniProtKB-EC.
CDD; cd14251; PL-6; 1.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR039513; PL-6.
Pfam; PF14592; Chondroitinas_B; 1.
SUPFAM; SSF51126; SSF51126; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycoprotein; Lyase;
Pyrrolidone carboxylic acid; Reference proteome; Signal.
SIGNAL 1 25
CHAIN 26 506 Chondroitinase-B.
/FTId=PRO_0000024928.
ACT_SITE 250 250
ACT_SITE 272 272
ACT_SITE 333 333
MOD_RES 26 26 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:10600383}.
CARBOHYD 234 234 O-linked (Man...) serine.
MUTAGEN 250 250 K->A: Complete loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 272 272 H->A: Partial loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 333 333 E->A: Partial loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 363 363 R->A: No effect.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 364 364 R->A: Partial loss of activity and
altered product profile.
{ECO:0000269|PubMed:12063249}.
CONFLICT 195 195 A -> G (in Ref. 1; AAC83384).
{ECO:0000305}.
HELIX 31 40 {ECO:0000244|PDB:1DBG}.
STRAND 46 49 {ECO:0000244|PDB:1DBG}.
STRAND 51 55 {ECO:0000244|PDB:1DBG}.
STRAND 58 61 {ECO:0000244|PDB:1DBG}.
STRAND 71 77 {ECO:0000244|PDB:1DBG}.
STRAND 80 86 {ECO:0000244|PDB:1DBG}.
STRAND 88 91 {ECO:0000244|PDB:1DBG}.
STRAND 93 100 {ECO:0000244|PDB:1DBG}.
STRAND 102 106 {ECO:0000244|PDB:1DBG}.
TURN 110 112 {ECO:0000244|PDB:1DBG}.
STRAND 120 123 {ECO:0000244|PDB:1DBG}.
STRAND 125 127 {ECO:0000244|PDB:1DBG}.
STRAND 129 132 {ECO:0000244|PDB:1DBG}.
STRAND 134 137 {ECO:0000244|PDB:1DBG}.
STRAND 145 148 {ECO:0000244|PDB:1DBG}.
STRAND 161 164 {ECO:0000244|PDB:1DBG}.
STRAND 166 168 {ECO:0000244|PDB:1DBG}.
STRAND 172 174 {ECO:0000244|PDB:1DBG}.
STRAND 176 179 {ECO:0000244|PDB:1DBG}.
STRAND 199 202 {ECO:0000244|PDB:1DBG}.
STRAND 204 207 {ECO:0000244|PDB:1DBG}.
STRAND 211 213 {ECO:0000244|PDB:1DBG}.
STRAND 217 220 {ECO:0000244|PDB:1DBG}.
STRAND 231 234 {ECO:0000244|PDB:1DBG}.
STRAND 236 240 {ECO:0000244|PDB:1DBG}.
STRAND 242 253 {ECO:0000244|PDB:1DBG}.
STRAND 255 258 {ECO:0000244|PDB:1DBG}.
STRAND 260 263 {ECO:0000244|PDB:1DBG}.
STRAND 265 272 {ECO:0000244|PDB:1DBG}.
STRAND 277 280 {ECO:0000244|PDB:1DBG}.
STRAND 282 285 {ECO:0000244|PDB:1DBG}.
STRAND 287 290 {ECO:0000244|PDB:1DBG}.
STRAND 295 297 {ECO:0000244|PDB:1DBG}.
STRAND 299 301 {ECO:0000244|PDB:1DBG}.
STRAND 303 306 {ECO:0000244|PDB:1DBG}.
STRAND 308 314 {ECO:0000244|PDB:1DBG}.
TURN 316 319 {ECO:0000244|PDB:1DBG}.
STRAND 320 325 {ECO:0000244|PDB:1DBG}.
STRAND 338 344 {ECO:0000244|PDB:1DBG}.
STRAND 346 349 {ECO:0000244|PDB:1DBG}.
STRAND 351 358 {ECO:0000244|PDB:1DBG}.
HELIX 361 370 {ECO:0000244|PDB:1DBG}.
STRAND 380 385 {ECO:0000244|PDB:1DBG}.
STRAND 387 389 {ECO:0000244|PDB:1DBG}.
STRAND 398 400 {ECO:0000244|PDB:1DBG}.
STRAND 408 413 {ECO:0000244|PDB:1DBG}.
STRAND 415 419 {ECO:0000244|PDB:1DBG}.
STRAND 422 424 {ECO:0000244|PDB:1DBG}.
HELIX 431 433 {ECO:0000244|PDB:1DBO}.
HELIX 452 458 {ECO:0000244|PDB:1DBG}.
HELIX 467 469 {ECO:0000244|PDB:1DBG}.
HELIX 482 485 {ECO:0000244|PDB:1DBG}.
HELIX 490 502 {ECO:0000244|PDB:1DBG}.
SEQUENCE 506 AA; 56337 MW; 454B93EC0AACD2A3 CRC64;
MKMLNKLAGY LLPIMVLLNV APCLGQVVAS NETLYQVVKE VKPGGLVQIA DGTYKDVQLI
VSNSGKSGLP ITIKALNPGK VFFTGDAKVE LRGEHLILEG IWFKDGNRAI QAWKSHGPGL
VAIYGSYNRI TACVFDCFDE ANSAYITTSL TEDGKVPQHC RIDHCSFTDK ITFDQVINLN
NTARAIKDGS VGGPAMYHRV DHCFFSNPQK PGNAGGGIRI GYYRNDIGRC LVDSNLFMRQ
DSEAEIITSK SQENVYYGNT YLNCQGTMNF RHGDHQVAIN NFYIGNDQRF GYGGMFVWGS
RHVIACNYFE LSETIKSRGN AALYLNPGAM ASEHALAFDM LIANNAFINV NGYAIHFNPL
DERRKEYCAA NRLKFETPHQ LMLKGNLFFK DKPYVYPFFK DDYFIAGKNS WTGNVALGVE
KGIPVNISAN RSAYKPVKIK DIQPIEGIAL DLNALISKGI TGKPLSWDEV RPYWLKEMPG
TYALTARLSA DRAAKFKAVI KRNKEH


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Pathways :
WP1030: Selenium metabolism Selenoproteins
WP108: Selenium metabolism/Selenoproteins
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WP1640: Cysteine and methionine metabolism
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WP1705: Sulfur metabolism
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WP28: Selenium Metabolism and Selenoproteins
WP390: Serine-isocitrate lyase pathway
WP668: Octadecanoid Pathway
WP579: Sulfate assimilation pathway II

Related Genes :
[cslB Phep_0789] Chondroitinase-B (EC 4.2.2.19) (Chondroitin sulfate B lyase) (Chondroitin-B eliminase) (Chondroitin-B lyase)
[chonabc] Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC)
[] Chondroitin sulfate ABC endolyase (EC 4.2.2.20) (Chondroitin ABC endoeliminase) (Chondroitin ABC lyase I) (Chondroitin sulfate ABC lyase I) (ChS ABC lyase I) (Chondroitinase ABC I) (cABC I) (Endochondroitinase ABC) (Condoliase)
[ChABCII] Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC) (Fragment)
[chonabc BT_3324] Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC)
[CHST3] Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Chondroitin 6-sulfotransferase) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0)
[CHST7] Carbohydrate sulfotransferase 7 (EC 2.8.2.-) (EC 2.8.2.17) (Chondroitin 6-sulfotransferase 2) (C6ST-2) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5) (GST-5) (N-acetylglucosamine 6-O-sulfotransferase 4) (GlcNAc6ST-4) (Gn6st-4)
[DSE SART2] Dermatan-sulfate epimerase (DS epimerase) (EC 5.1.3.19) (Chondroitin-glucuronate 5-epimerase) (Squamous cell carcinoma antigen recognized by T-cells 2) (SART-2)
[CHST15 BRAG GALNAC4S6ST KIAA0598] Carbohydrate sulfotransferase 15 (EC 2.8.2.33) (B-cell RAG-associated gene protein) (hBRAG) (N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase) (GalNAc4S-6ST)
[CSPG4 MCSP] Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (Melanoma chondroitin sulfate proteoglycan) (Melanoma-associated chondroitin sulfate proteoglycan)
[Chst7 Gst5] Carbohydrate sulfotransferase 7 (EC 2.8.2.-) (EC 2.8.2.17) (Chondroitin 6-sulfotransferase 2) (C6ST-2) (mC6ST-2) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5) (GST-5) (N-acetylglucosamine 6-O-sulfotransferase 4) (GlcNAc6ST-4) (Gn6st-4)
[Cspg4 Ng2] Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (HSN tumor-specific antigen)
[Cspg4 An2 Kiaa4232 Ng2] Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (Proteoglycan AN2)
[hepB Phep_2408] Heparin and heparin-sulfate lyase (Heparin lyase) (EC 4.2.2.7) (Heparin-sulfate lyase) (EC 4.2.2.8) (Heparinase II) (HepII)
[CSPG5 CALEB] Chondroitin sulfate proteoglycan 5 (Acidic leucine-rich EGF-like domain-containing brain protein) [Cleaved into: Chondroitin sulfate proteoglycan 5, 38 kDa form; Chondroitin sulfate proteoglycan 5, 80 kDa form]
[cpg-2 B0280.5] Chondroitin proteoglycan-2 (Cytokinesis protein B0280.5)
[ACAN AGC1 CSPG1 MSK16] Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP) (Chondroitin sulfate proteoglycan core protein 1) (Chondroitin sulfate proteoglycan 1) [Cleaved into: Aggrecan core protein 2]
[Chst15 Brag Galnac4s6st Kiaa0598] Carbohydrate sulfotransferase 15 (EC 2.8.2.33) (B-cell RAG-associated gene protein) (N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase) (GalNAc4S-6ST)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Chst7] Carbohydrate sulfotransferase 7 (EC 2.8.2.-) (EC 2.8.2.17) (Chondroitin 6-sulfotransferase 2) (C6ST-2) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5) (GST-5) (N-acetylglucosamine 6-O-sulfotransferase 4) (GlcNAc6ST-4) (Gn6st-4)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Ptprz1 Ptprz Ptpz] Receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta) (EC 3.1.3.48) (3F8 chondroitin sulfate proteoglycan) (3H1 keratan sulfate proteoglycan) (Phosphacan)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[hepC Phep_3797] Heparin-sulfate lyase (EC 4.2.2.8) (Heparin-sulfate eliminase) (Heparinase III) (HepIII) (Heparitin-sulfate lyase)
[gbs1889] Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180) (Unsaturated glucuronyl hydrolase) (SagUGL)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[dinB dinP b0231 JW0221] DNA polymerase IV (Pol IV) (EC 2.7.7.7) (Translesion synthesis polymerase IV) (TSL polymerase IV)

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