Reviewed, UniProtKB/Swiss-Prot P03313 (POLG_CXB3N)

Names and origin

Protein names	Recommended name:     Genome polyprotein Cleaved into the following 12 chains:     1- Recommended name:             Protein VP0         Alternative name(s):             VP4-VP2     2- Recommended name:             Protein VP4         Alternative name(s):             Virion protein 4             P1A     3- Recommended name:             Protein VP2         Alternative name(s):             Virion protein 2             P1B     4- Recommended name:             Protein VP3         Alternative name(s):             Virion protein 3             P1C     5- Recommended name:             Protein VP1         Alternative name(s):             Virion protein 1             P1D     6- Recommended name:             Picornain 2A                 Short name=Protein 2A                 Short name=P2A               EC=3.4.22.29     7- Recommended name:             Protein 2B                 Short name=P2B     8- Recommended name:             Protein 2C                 Short name=P2C               EC=3.6.1.15     9- Recommended name:             Protein 3A                 Short name=P3A     10- Recommended name:             Protein 3B                 Short name=P3B         Alternative name(s):             VPg     11- Recommended name:             Picornain 3C               EC=3.4.22.28         Alternative name(s):             Protease 3C               Short name=P3C     12- Recommended name:             RNA-directed RNA polymerase 3D-POL                 Short name=P3D-POL               EC=2.7.7.48
Organism	Coxsackievirus B3 (strain Nancy) [Complete proteome]
Taxonomic identifier	103903 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	2185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes By similarity. Capsid proteins interact with host CAR/CXADR or CD55 to provide virion attachment to target cell. VP0 precursor is a component of immature procapsids By similarity. Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription By similarity. Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity. Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. It also inhibits endoplasmic reticulum-to-Golgi transport By similarity. Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease By similarity. RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. NTP + H2O = NDP + phosphate.
Subunit structure	Capsid proteins interact with host CD55 and CXADR.
Subcellular location	Protein VP2: Virion. Host cytoplasm Potential. Protein VP3: Virion. Host cytoplasm Potential. Protein VP1: Virion. Host cytoplasm Potential. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity. Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity. Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity. Protein 3B: Virion Potential. Picornain 3C: Host cytoplasm Potential. RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Post-translational modification	Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity. VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity. Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Sequence similarities	Belongs to the picornaviruses polyprotein family. Contains 2 peptidase C3 domains. Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.

Ontologies

Keywords
Biological process	Host-virus interaction RNA replication
Cellular component	Capsid protein Cytoplasm Cytoplasmic vesicle Membrane Virion
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Covalent protein-RNA linkage Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 332

331

Protein VP0 Potential

PRO_0000311047

Chain

2 – 69

68

Protein VP4 Potential

PRO_0000039582

Chain

70 – 332

263

Protein VP2 Potential

PRO_0000039583

Chain

333 – 570

238

Protein VP3 Potential

PRO_0000039584

Chain

571 – 851

281

Protein VP1 Potential

PRO_0000039585

Chain

852 – 1001

150

Picornain 2A Potential

PRO_0000039586

Chain

1002 – 1100

99

Protein 2B Potential

PRO_0000039587

Chain

1101 – 1429

329

Protein 2C Potential

PRO_0000039588

Chain

1430 – 1518

89

Protein 3A Potential

PRO_0000039589

Chain

1519 – 1540

22

Protein 3B Potential

PRO_0000039590

Chain

1541 – 1723

183

Picornain 3C Potential

PRO_0000039591

Chain

1724 – 2185

462

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000039592

Regions

Topological domain

2 – 1495

1494

Cytoplasmic Potential

Topological domain

1496 – 1511

16

In membrane Potential

Topological domain

1512 – 2185

674

Cytoplasmic Potential

Domain

1205 – 1361

157

SF3 helicase

Domain

1950 – 2066

117

RdRp catalytic

Nucleotide binding

1229 – 1236

8

ATP Potential

Sites

Active site

872

1

For picornain 2A activity By similarity

Active site

890

1

For picornain 2A activity By similarity

Active site

961

1

For picornain 2A activity By similarity

Active site

1580

1

For picornain 3C activity Potential

Active site

1611

1

For picornain 3C activity Potential

Active site

1687

1

For picornain 3C activity By similarity

Site

69 – 70

2

Cleavage Potential

Site

332 – 333

2

Cleavage; by picornain 3C Potential

Site

851 – 852

2

Cleavage; by picornain 2A Potential

Site

1001 – 1002

2

Cleavage; by picornain 3C Potential

Site

1100 – 1101

2

Cleavage; by picornain 3C Potential

Site

1429 – 1430

2

Cleavage; by picornain 3C Potential

Site

1518 – 1519

2

Cleavage; by picornain 3C Potential

Site

1540 – 1541

2

Cleavage; by picornain 3C Potential

Site

1723 – 1724

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1521

1

O-(5'-phospho-RNA)-tyrosine By similarity

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict

16

1

R → G in AAA74400. Ref.2

Sequence conflict

177

1

V → D in AAA74400. Ref.2

Sequence conflict

469

1

P → L in AAA74400. Ref.2

Sequence conflict

487

1

I → V in AAA74400. Ref.2

Sequence conflict

510

1

F → Y in AAA74400. Ref.2

Sequence conflict

516

1

Y → C in AAA74400. Ref.2

Sequence conflict

566

1

Q → E in AAA74400. Ref.2

Sequence conflict

593

1

T → N in AAA74400. Ref.2

Sequence conflict

650

1

K → E in AAA74400. Ref.2

Sequence conflict

854 – 865

12

FGQQS…VYVGN → IWTTIRGSVCGD in AAA74400. Ref.2

Sequence conflict

873

1

L → S in AAA74400. Ref.2

Sequence conflict

1097

1

A → P in AAA74400. Ref.2

Sequence conflict

1280

1

Q → H in AAA74400. Ref.2

Sequence conflict

1437

1

I → F in AAA74400. Ref.2

Sequence conflict

1503

1

V → M in AAA74400. Ref.2

Sequence conflict

1616

1

K → E in AAA74400. Ref.2

Sequence conflict

1624

1

R → G in AAA74400. Ref.2

Sequence conflict

1627

1

R → G in AAA74400. Ref.2

Sequence conflict

1630

1

L → V in AAA74400. Ref.2

Sequence conflict

1718

1

Y → N in AAA74400. Ref.2

Sequence conflict

1734

1

D → V in AAA74400. Ref.2

Sequence conflict

1758

1

E → V Ref.2

Sequence conflict

1758

1

E → V Ref.3

Sequence conflict

1824

1

V → R Ref.2

Sequence conflict

1824

1

V → R Ref.3

Sequence conflict

1867

1

C → R Ref.2

Sequence conflict

1867

1

C → R Ref.3

Sequence conflict

1880

1

Y → H Ref.2

Sequence conflict

1880

1

Y → H Ref.3

Sequence conflict

2001

1

D → N Ref.2

Sequence conflict

2001

1

D → N Ref.3

Sequence conflict

2095

1

A → V Ref.2

Sequence conflict

2095

1

A → V Ref.3

Sequence conflict

2115

1

V → A Ref.2

Sequence conflict

2115

1

V → A Ref.3

Sequence conflict

2175

1

S → T Ref.2

Sequence conflict

2175

1

S → T Ref.3

Sequence conflict

2178

1

R → G Ref.2

Sequence conflict

2178

1

R → G Ref.3

Secondary structure

1

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2185

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

26 – 29

4

Helix

36 – 38

3

Turn

43 – 44

2

Helix

50 – 52

3

Turn

53

1

Turn

63 – 64

2

Turn

80 – 81

2

Beta strand

83 – 87

5

Turn

88 – 89

2

Beta strand

90 – 94

5

Turn

103 – 104

2

Turn

113 – 115

3

Helix

126 – 128

3

Turn

129

1

Beta strand

133 – 140

8

Turn

142 – 143

2

Beta strand

147 – 150

4

Turn

152 – 154

3

Turn

156 – 157

2

Helix

159 – 167

9

Beta strand

168 – 180

13

Beta strand

188 – 197

10

Turn

198

1

Turn

206 – 207

2

Helix

212 – 215

4

Helix

241 – 243

3

Turn

244 – 247

4

Helix

250 – 255

6

Beta strand

258 – 262

5

Turn

263 – 265

3

Beta strand

268 – 273

6

Turn

284 – 286

3

Beta strand

290 – 301

12

Turn

304 – 305

2

Beta strand

310 – 326

17

Turn

340 – 343

4

Turn

347 – 348

2

Turn

358 – 359

2

Turn

375

1

Helix

376 – 379

4

Turn

380

1

Turn

390

1

Helix

391 – 395

5

Helix

397 – 400

4

Beta strand

402 – 405

4

Beta strand

413 – 418

6

Turn

421 – 423

3

Turn

425 – 429

5

Helix

431 – 436

6

Turn

437 – 438

2

Beta strand

439 – 443

5

Beta strand

446 – 452

7

Turn

456 – 457

2

Beta strand

461 – 467

7

Helix

477 – 480

4

Turn

481 – 482

2

Beta strand

484 – 489

6

Beta strand

495 – 500

6

Turn

516 – 517

2

Beta strand

521 – 528

8

Turn

534 – 535

2

Beta strand

539 – 548

10

Turn

550 – 551

2

Beta strand

553 – 557

5

Turn

561 – 562

2

Helix

604 – 606

3

Helix

614 – 617

4

Turn

631 – 632

2

Helix

634 – 638

5

Beta strand

642 – 650

9

Beta strand

657 – 661

5

Turn

665 – 666

2

Helix

668 – 674

7

Turn

675 – 676

2

Beta strand

677 – 694

18

Beta strand

708 – 714

7

Turn

716 – 717

2

Turn

724 – 725

2

Helix

727 – 730

4

Beta strand

736 – 740

5

Turn

741 – 742

2

Beta strand

747 – 750

4

Beta strand

765 – 768

4

Turn

769 – 771

3

Beta strand

772 – 775

4

Helix

777 – 779

3

Turn

780

1

Beta strand

785 – 790

6

Beta strand

799 – 817

19

Turn

845 – 846

2

Sequences

	Sequence		Length	Mass (Da)
	P03313-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 1B5ECE3DA47338FF	FASTA	2,185	243,453
	10 20 30 40 50 60 MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPVKDI 70 80 90 100 110 120 MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV VVGYGVWPDY LKDSEATAED 130 140 150 160 170 180 QPTQPDVATC RFYTLDSVQW QKTSPGWWWK LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ 190 200 210 220 230 240 CNASKFHQGC LLVVCVPEAE MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV 250 260 270 280 290 300 VYNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL 310 320 330 340 350 360 DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD FQSPSAMPQY 370 380 390 400 410 420 DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY QIPVRSNEGS GTQVFGFPLQ 430 440 450 460 470 480 PGYSSVFSRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGAPTKRVDA 490 500 510 520 530 540 MLGTHVIWDV GLQSSCVLCI PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC 550 560 570 580 590 600 YIMCFVSACN DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA 610 620 630 640 650 660 LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK NSGAKRYAEW 670 680 690 700 710 720 VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ NQDAQILTHQ IMYVPPGGPV 730 740 750 760 770 780 PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI PFLSIGNAYS NFYDGWSEFS RNGVYGINTL 790 800 810 820 830 840 NNMGTLYARH VNAGSTGPIK STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT 850 860 870 880 890 900 TRQSITTMTN TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG 910 920 930 940 950 960 CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL LAAGFSEPGD 970 980 990 1000 1010 1020 CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN 1030 1040 1050 1060 1070 1080 QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP 1090 1100 1110 1120 1130 1140 WRWLKQKVSQ YYGIPMAERQ NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV 1150 1160 1170 1180 1190 1200 REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR 1210 1220 1230 1240 1250 1260 VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD 1270 1280 1290 1300 1310 1320 PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA 1330 1340 1350 1360 1370 1380 STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVKTCD DECCPVNFKK 1390 1400 1410 1420 1430 1440 CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS 1450 1460 1470 1480 1490 1500 VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF 1510 1520 1530 1540 1550 1560 VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT 1570 1580 1590 1600 1610 1620 EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK ELVDKDGTNL ELTLLKLNRN 1630 1640 1650 1660 1670 1680 EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF 1690 1700 1710 1720 1730 1740 PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI 1750 1760 1770 1780 1790 1800 NTPSKTKLEP SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA 1810 1820 1830 1840 1850 1860 VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTKD 1870 1880 1890 1900 1910 1920 LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT 1930 1940 1950 1960 1970 1980 FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKMLLEKLG 1990 2000 2010 2020 2030 2040 YTHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI 2050 2060 2070 2080 2090 2100 DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR 2110 2120 2130 2140 2150 2160 YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI 2170 2180 RSVPVGRCLT LPAFSTLRRK WLDSF

References

[1]	"Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA: two initial 5' uridine residues are regained during plus-strand RNA synthesis." Klump W.M., Bergmann I., Mueller B.C., Ameis D., Kandolf R. J. Virol. 64:1573-1583(1990) [PubMed: 2157045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Genome of coxsackievirus B3." Lindberg A.M., Staalhandske P.O.K., Pettersson U. Virology 156:50-63(1987) [PubMed: 3027968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Replicase gene of coxsackievirus B3." Staalhandske P.O.K., Lindberg A.M., Pettersson U. J. Virol. 51:742-746(1984) [PubMed: 6088796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1724-2185.
[4]	"Coxsackieviruses B1, B3, and B5 use decay aCCelerating factor as a receptor for cell attachment." Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D. J. Virol. 69:3873-3877(1995) [PubMed: 7538177] [Abstract] Cited for: INTERACTION WITH HOST CD55.
[5]	"The coxsackie-adenovirus receptor (CAR) is used by reference strains and clinical isolates representing all six serotypes of coxsackievirus group B and by swine vesicular disease virus." Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A., Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N., Gauntt C.J., Liu P.P. Virology 271:99-108(2000) [PubMed: 10814575] [Abstract] Cited for: INTERACTION WITH HOST CXADR.
[6]	"Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment." Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L., Melchers W.J., van Kuppeveld F.J. J. Virol. 80:11852-11860(2006) [PubMed: 17005635] [Abstract] Cited for: FUNCTION OF PROTEIN 3A.
[7]	"Structure determination of coxsackievirus B3 to 3.5-A resolution." Muckelbauer J.K., Kremer M., Minor I., Tong L., Zlotnick A., Johnson J.E., Rossmann M.G. Acta Crystallogr. D 51:871-887(1995) [PubMed: 15299757] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-851.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33854 Genomic RNA. Translation: AAA42931.1.
K02709 Genomic RNA. Translation: AAA42932.1.
M16572 Genomic RNA. Translation: AAA74400.1.

PIR

GNNYB3. A26354.
GNNYBT. A34664.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1COV	X-ray	3.50	4	-	[»]
2VB0	X-ray	2.40	A	1541-1723	[»]
2ZTX	X-ray	1.72	A	1541-1723	[»]
2ZTY	X-ray	1.72	A	1541-1723	[»]
2ZTZ	X-ray	2.00	A/B	1541-1723	[»]
2ZU1	X-ray	1.38	A/B	1541-1723	[»]
2ZU3	X-ray	1.75	A	1541-1723	[»]
3CDU	X-ray	2.10	A	1724-2185	[»]
3CDW	X-ray	2.50	A	1724-2185	[»]
			H	1519-1540	[»]

ModBase

Search...

Protein family/group databases

MEROPS

C03.011.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR004004. Helicase/Pol/Pept_Calicivir.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR014838. P3A.
IPR000199. Pept_C3_picorn.
IPR000081. Peptidase_C3.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA_pol_P3D.
IPR007094. RNA_pol_PSvir.
[Graphical view]

Pfam

PF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]

PRINTS

PR00918. CALICVIRUSNS.

ProDom

PD001125. Pept_C3_picorn. 1 hit.
PD001306. Peptidase_C3_2. 1 hit.
PD001274. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

PROSITE

PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

POLG_CXB3N

Accession

Primary (citable) accession number: P03313
Secondary accession number(s): Q66322 , Q66323, Q66324, Q66325, Q66326, Q66327, Q66328, Q83744

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 111 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)