P27410 (POLG_RHDVF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Genome polyprotein

Alternative name(s):
p254

Cleaved into the following 11 chains:

1. Protein p16
2. Protein p23
3. NTPase
   EC=3.6.1.15
   Alternative name(s):
   2C-like protein
   P2C
   p37
4. Precursor p41
5. Protein p29
6. Protein p23/2
7. Protein p18
8. Viral genome-linked protein
   Alternative name(s):
   VPg
   p13
9. 3C-like protease
   Short name=3CLpro
   EC=3.4.22.66
   Alternative name(s):
   Calicivirin
   Thiol protease P3C
   p15
10. RNA-directed RNA polymerase
    EC=2.7.7.48
    Alternative name(s):
    3Dpol
    p58
11. Capsid protein VP60

Gene names

ORF Names:

ORF1

Organism

Rabbit hemorrhagic disease virus (strain Rabbit/Germany/FRG/1989) (Ra/LV/RHDV/GH/1989/GE) (RHDV-FRG)

Taxonomic identifier

314536 [NCBI]

Taxonomic lineage

Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Lagovirus

Virus host

Oryctolagus cuniculus (Rabbit) [TaxID: 9986]

Protein attributes

Sequence length	2344 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	NTPase presumably plays a role in replication By similarity. Ref.2 Ref.11 Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation By similarity. Ref.2 Ref.11 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved By similarity. Ref.2 Ref.11 RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs By similarity. Ref.2 Ref.11 Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm By similarity. Ref.2 Ref.11
Catalytic activity	NTP + H2O = NDP + phosphate. Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Binds to histo-blood group antigens at surface of target cells By similarity.
Subcellular location	Capsid protein VP60: Virion. Host cytoplasm By similarity.
Post-translational modification	Specific enzymatic cleavages by its own cysteine protease yield mature proteins. The protease cleaves itself from the nascent polyprotein autocatalytically. Precursor p41 can be cleaved by viral 3CLpro into protein p19 and VPg, or cleaved by host protease into protein p23/2 and protein p18. Ref.4 Ref.6 Ref.7 Ref.8 Ref.10 VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Miscellaneous	Two differents RNAs lead the expression of the capsid protein. One arises from the cleavage of the polyprotein translated from the genomic RNA and the other from the translation of a subgenomic RNA derived from the (-)RNA template. Capsid protein expressed from the subgenomic mRNA is produced in much larger amounts than the cleaved one By similarity.
Sequence similarities	Contains 1 peptidase C24 domain. Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.

Ontologies

Keywords
Biological process	RNA replication
Cellular component	Host cytoplasm Virion
Coding sequence diversity	Alternative promoter usage
Ligand	ATP-binding Nucleotide-binding
Molecular function	Capsid protein Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Covalent protein-RNA linkage Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell 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: InterPro 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
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform Genome polyprotein (identifier: P27410-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Produced from the genomic RNA.

Isoform Subgenomic capsid protein VP60 (identifier: P27410-2)

Also known as: VP1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1765: Missing.

Note: Produced from the subgenomic RNA.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2344

2344

Genome polyprotein

PRO_0000341645

Chain

1 – 143

143

Protein p16

PRO_0000036959

Chain

144 – 339

196

Protein p23

PRO_0000036960

Chain

340 – 718

379

NTPase

PRO_0000036961

Chain

719 – 1108

390

Precursor p41

PRO_0000341646

Chain

719 – 993

275

Protein p29

PRO_0000036962

Chain

719 – 936

218

Protein p23/2

PRO_0000341647

Chain

937 – 1108

172

Protein p18

PRO_0000341648

Chain

994 – 1108

115

Viral genome-linked protein

PRO_0000036963

Chain

1109 – 1251

143

3C-like protease

PRO_0000036964

Chain

1252 – 1767

516

RNA-directed RNA polymerase

PRO_0000036965

Chain

1768 – 2344

577

Capsid protein VP60

PRO_0000036967

Regions

Domain

492 – 653

162

SF3 helicase

Domain

1120 – 1218

99

Peptidase C24

Domain

1495 – 1619

125

RdRp catalytic

Nucleotide binding

522 – 529

8

ATP Potential

Sites

Active site

1135

1

For 3CLpro activity By similarity

Active site

1159

1

For 3CLpro activity By similarity

Active site

1212

1

For 3CLpro activity By similarity

Site

143 – 144

2

Cleavage; by 3CLpro

Site

339 – 340

2

Cleavage; by 3CLpro

Site

718 – 719

2

Cleavage; by 3CLpro

Site

936 – 937

2

Cleavage; by host

Site

993 – 994

2

Cleavage; by 3CLpro

Site

1108 – 1109

2

Cleavage; by 3CLpro

Site

1251 – 1252

2

Cleavage; by 3CLpro

Site

1767 – 1768

2

Cleavage; by 3CLpro

Amino acid modifications

Modified residue

1014

1

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

Disulfide bond

1584 ↔ 1591

Natural variations

Alternative sequence

1 – 1765

1765

Missing in isoform Subgenomic capsid protein VP60.

VSP_034381

Experimental info

Mutagenesis

1135

1

H → N: Complete loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1152

1

D → E: Partial loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1152

1

D → G or N: Complete loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1175

1

D → G or E: Complete loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1175

1

D → N: Partial loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1212

1

C → G: Complete loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1212

1

C → S: Partial loss of 3CLpro activity in vitro. Ref.3

Mutagenesis

1227

1

H → L or N: Complete loss of 3CLpro activity in vitro. Ref.3

Secondary structure

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2344

Helix Strand Turn

Details...

Beta strand

1257 – 1263

7

Beta strand

1266 – 1271

6

Beta strand

1282 – 1287

6

Helix

1293 – 1295

3

Beta strand

1300 – 1302

3

Helix

1305 – 1307

3

Helix

1315 – 1324

10

Helix

1325 – 1327

3

Helix

1337 – 1353

17

Turn

1354 – 1356

3

Helix

1364 – 1370

7

Beta strand

1379 – 1381

3

Helix

1385 – 1387

3

Beta strand

1391 – 1393

3

Helix

1396 – 1410

15

Beta strand

1418 – 1423

6

Beta strand

1440 – 1444

5

Helix

1446 – 1465

20

Turn

1466 – 1469

4

Beta strand

1470 – 1472

3

Helix

1482 – 1493

12

Beta strand

1495 – 1502

8

Helix

1505 – 1508

4

Helix

1511 – 1522

12

Helix

1529 – 1539

11

Beta strand

1543 – 1545

3

Beta strand

1547 – 1551

5

Helix

1564 – 1586

23

Helix

1594 – 1597

4

Beta strand

1600 – 1603

4

Beta strand

1606 – 1611

6

Helix

1613 – 1617

5

Helix

1619 – 1628

10

Beta strand

1633 – 1637

5

Helix

1647 – 1649

3

Beta strand

1655 – 1660

6

Beta strand

1663 – 1668

6

Helix

1670 – 1678

9

Beta strand

1679 – 1689

11

Helix

1698 – 1712

15

Helix

1716 – 1729

14

Turn

1730 – 1732

3

Helix

1740 – 1750

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform Genome polyprotein [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 1454C248F81E9212	FASTA	2,344	257,068
	10 20 30 40 50 60 MAAMSRLTGM TTAILPEKKP LDFFLDLRDK TPPCCIRATG RLAWPVFPGQ NGKEGPLETC 70 80 90 100 110 120 NKCGKWLNGF GNFGLEDLGD VCLCSIAQQK HKFGPVCLCN RVYIHDCGRW RRRSRFLKHY 130 140 150 160 170 180 KALNKVIPCA YQFDESFPTP IFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV 190 200 210 220 230 240 DEPCLTSRDT SLLDSIASDN TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV 250 260 270 280 290 300 TWYTKLGNIT EKGKQWAKKV VYGARKVTDP LKTLASILLV GLHNVIAVDT TVMLSTFKPV 310 320 330 340 350 360 NLLAILMDWN NDLTGFITTL VRLLELYGVV QATVNLIIEG VKSFWDKVVC ATDRCFDLLK 370 380 390 400 410 420 RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNSVIT TFMKGAGKLT TFAGVVGAIR 430 440 450 460 470 480 TLWITINQHM VAKDLTSVQQ KVMTVVKMAN EAATLDQLEI VSCLCSDLET TLTNRCTLPS 490 500 510 520 530 540 YNQHLGILNA SQKVISDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG 550 560 570 580 590 600 CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK 610 620 630 640 650 660 NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVMIVEARN KAVESWQATR HGSKPGKSCY 670 680 690 700 710 720 SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVK SQVTPREYKY SELLDLIKSE HPDVASFEGA 730 740 750 760 770 780 NKFNFVYPDA QYDQALLMWK QYFVMYGCVA RLAKNFVDDI PYNQVHISRA SDPKIEGCVE 790 800 810 820 830 840 YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT 850 860 870 880 890 900 TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGTLVRTLT GAATFSDDPV 910 920 930 940 950 960 STTIICSNCT IQLHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL ISGFSWRQIA 970 980 990 1000 1010 1020 HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA 1030 1040 1050 1060 1070 1080 RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SIMFRSWWTR RQLRPEEDQV TIVGRSGVRN 1090 1100 1110 1120 1130 1140 EVIRTRVRQT PRGPKTLDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS 1150 1160 1170 1180 1190 1200 CSEIVTCSPT TDLCLVKGES IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA 1210 1220 1230 1240 1250 1260 YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL IDLTITKGVY ETSNFFCGEP 1270 1280 1290 1300 1310 1320 IDYRGITAHR LVGAEPRPPV SGTRYAKVPG VPDEYKTGYR PANLGRSDPD SDKSLMNIAV 1330 1340 1350 1360 1370 1380 KNLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQA NLNFKAAFNT LDLSTSCGPF 1390 1400 1410 1420 1430 1440 VPGKKIDHVK DGVMDQVLAK HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL 1450 1460 1470 1480 1490 1500 LWGCDVGVAV CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TSKASDFLCL 1510 1520 1530 1540 1550 1560 DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI VQTKRGLPSG 1570 1580 1590 1600 1610 1620 MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF YTYGDDGVYA MTPMMVSLLP 1630 1640 1650 1660 1670 1680 AIIENLRDYG LSPTAADKTE FIDVCPLNKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS 1690 1700 1710 1720 1730 1740 KTTSRHMVIE ETYDLAKEER GVQLEELQVA AAAHGQEFFN FVCRELERQQ AYTQFSVYSY 1750 1760 1770 1780 1790 1800 DAARKILADR KRVVSVVPDD EFVNVMEGKA RAAPQGEAAG TATTASVPGT TTDGMDPGVV 1810 1820 1830 1840 1850 1860 ATTSVITAEN SSASIATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA PGSILYTVQH 1870 1880 1890 1900 1910 1920 SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVR AVIPPGIEIG PGLEVRQFPH 1930 1940 1950 1960 1970 1980 VVIDARSLEP VTITMPDLRP NMYHPTGDPG LVPTLVLSVY NNLINPFGGS TSAIQVTVET 1990 2000 2010 2020 2030 2040 RPSEDFEFVM IRAPSSKTVD SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN 2050 2060 2070 2080 2090 2100 RHWNLNGSTY GWSSPRFGDI DHRRGSASYS GSNATNVLQF WYANAGSAID NPISQVAPDG 2110 2120 2130 2140 2150 2160 FPDMSFVPFN GPGIPAAGWV GFGAIWNSNS GAPNVTTVQA YELGFATGAP GNLQPTTNTS 2170 2180 2190 2200 2210 2220 GAQTVAKSIY AVVTGTAQNP AGLFVMASGI ISTPNASAIT YTPQPDRIVT TPGTPAAAPV 2230 2240 2250 2260 2270 2280 GKNTPIMFAS VVRRTGDVNA TAGSANGTQY GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW 2290 2300 2310 2320 2330 2340 QLTFASGFME IGLSVDGYFY AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTANG FSYV
	Isoform Subgenomic capsid protein VP60 (VP1) [UniParc]. Checksum: 20857900C4107D20	FASTA	579	60,257
	10 20 30 40 50 60 MEGKARAAPQ GEAAGTATTA SVPGTTTDGM DPGVVATTSV ITAENSSASI ATAGIGGPPQ 70 80 90 100 110 120 QVDQQETWRT NFYYNDVFTW SVADAPGSIL YTVQHSPQNN PFTAVLSQMY AGWAGGMQFR 130 140 150 160 170 180 FIVAGSGVFG GRLVRAVIPP GIEIGPGLEV RQFPHVVIDA RSLEPVTITM PDLRPNMYHP 190 200 210 220 230 240 TGDPGLVPTL VLSVYNNLIN PFGGSTSAIQ VTVETRPSED FEFVMIRAPS SKTVDSISPA 250 260 270 280 290 300 GLLTTPVLTG VGNDNRWNGQ IVGLQPVPGG FSTCNRHWNL NGSTYGWSSP RFGDIDHRRG 310 320 330 340 350 360 SASYSGSNAT NVLQFWYANA GSAIDNPISQ VAPDGFPDMS FVPFNGPGIP AAGWVGFGAI 370 380 390 400 410 420 WNSNSGAPNV TTVQAYELGF ATGAPGNLQP TTNTSGAQTV AKSIYAVVTG TAQNPAGLFV 430 440 450 460 470 480 MASGIISTPN ASAITYTPQP DRIVTTPGTP AAAPVGKNTP IMFASVVRRT GDVNATAGSA 490 500 510 520 530 540 NGTQYGTGSQ PLPVTIGLSL NNYSSALMPG QFFVWQLTFA SGFMEIGLSV DGYFYAGTGA 550 560 570 STTLIDLTEL IDVRPVGPRP SKSTLVFNLG GTANGFSYV

References

[1]	"Rabbit hemorrhagic disease virus -- molecular cloning and nucleotide sequencing of a calicivirus genome." Meyers G., Wirblich C., Thiel H.-J. Virology 184:664-676(1991) [PubMed: 1840711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles." Meyers G., Wirblich C., Thiel H.-J. Virology 184:677-686(1991) [PubMed: 1887589] [Abstract] Cited for: FUNCTION OF VPG.
[3]	"Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus." Boniotti B., Wirblich C., Sibilia M., Meyers G., Thiel H.J., Rossi C. J. Virol. 68:6487-6495(1994) [PubMed: 8083986] [Abstract] Cited for: MUTAGENESIS OF HIS-1135; ASP-1152; ASP-1175; CYS-1212 AND HIS-1227.
[4]	"3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity." Wirblich C., Sibilia M., Boniotti M.B., Rossi C., Thiel H.-J., Meyers G. J. Virol. 69:7159-7168(1995) [PubMed: 7474137] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[5]	"Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein." Sibilia M., Boniotti M.B., Angoscini P., Capucci L., Rossi C. J. Virol. 69:5812-5815(1995) [PubMed: 7637026] [Abstract] Cited for: SUBGENOMIC ORIGIN OF VP60.
[6]	"Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus." Konig M., Thiel H.J., Meyers G. J. Virol. 72:4492-4497(1998) [PubMed: 9557747] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[7]	"Rabbit hemorrhagic disease virus: genome organization and polyprotein processing of a calicivirus studied after transient expression of cDNA constructs." Meyers G., Wirblich C., Thiel H.J., Thumfart J.O. Virology 276:349-363(2000) [PubMed: 11040126] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[8]	"Identification of a new cleavage site of the 3C-like protease of rabbit haemorrhagic disease virus." Joubert P., Pautigny C., Madelaine M.-F., Rasschaert D. J. Gen. Virol. 81:481-488(2000) [PubMed: 10644847] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[9]	"Characterisation of the RNA-dependent RNA polymerase from Rabbit hemorrhagic disease virus produced in Escherichia coli." Lopez Vazquez A.L., Martin Alonso J.M., Parra F. Arch. Virol. 146:59-69(2001) [PubMed: 11266218] [Abstract] Cited for: CHARACTERIZATION OF RNA-DIRECTED RNA POLYMERASE.
[10]	"Rabbit hemorrhagic disease virus: identification of a cleavage site in the viral polyprotein that is not processed by the known calicivirus protease." Thumfart J.O., Meyers G. Virology 304:352-363(2002) [PubMed: 12504575] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[11]	"The coat protein of Rabbit hemorrhagic disease virus contains a molecular switch at the N-terminal region facing the inner surface of the capsid." Barcena J., Verdaguer N., Roca R., Morales M., Angulo I., Risco C., Carrascosa J.L., Torres J.M., Caston J.R. Virology 322:118-134(2004) [PubMed: 15063122] [Abstract] Cited for: FUNCTION OF CAPSID PROTEIN VP60.
[12]	"Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase." Ng K.K.S., Cherney M.M., Vazquez A.L., Machin A., Martin-Alonso J.M., Parra F., James M.N.G. J. Biol. Chem. 277:1381-1387(2002) [PubMed: 11677245] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1252-1767.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M67473 Genomic RNA. Translation: AAA47285.1.

PIR

RRWWRH. A41039.

RefSeq

NP_062875.1. NC_001543.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KHV	X-ray	2.50	A/B	1252-1767	[»]
1KHW	X-ray	2.70	A/B	1252-1767	[»]

ProteinModelPortal

P27410.

SMR

P27410. Positions 1256-1752.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1491968.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR004005. Calicivirus_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR000317. Peptidase_C24.
IPR001205. RNA-dir_pol_picornavirus.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]

Pfam

PF00915. Calici_coat. 1 hit.
PF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]

PRINTS

PR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

POLG_RHDVF

Accession

Primary (citable) accession number: P27410

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program