Results | viHumans

UniProt ID

Q9YLR1

Status

Reviewed

Host

Bandicota Bengalensis (lesser Bandicoot Rat) [TaxID: 69079]; Callithrix [TaxID: 9481]; Cercopithecus Hamlyni (Owl-faced Monkey) (Hamlyn's Monkey) [TaxID: 9536]; Chlorocebus Aethiops (Green Monkey) (Cercopithecus Aethiops) [TaxID: 9534]; Homo Sapiens (Human) [TaxID: 9606]; Macaca (macaques) [TaxID: 9539]; Mus Musculus (Mouse) [TaxID: 10090]; Pan Troglodytes (Chimpanzee) [TaxID: 9598]; Saimiri (squirrel Monkeys) [TaxID: 9520]; Sus Scrofa (Pig) [TaxID: 9823]

Gene Name

ORF1

Protein Name

♦Non-structural polyprotein pORF1 [Includes: Methyltransferase (EC 2.1.1.-) (EC 2.7.7.-)
♦ Putative papain-like cysteine protease (PLP) (EC 3.4.22.-)
♦ NTPase/helicase (EC 3.6.4.-)
♦ RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48)]

Organism Name

Hepatitis E Virus Genotype 3 (isolate Human/United States/US2) (HEV-3)

Taxonomic Lineage

Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Hepeviridae> Orthohepevirus> Orthohepevirus A> Hepatitis E Virus (HEV)> Hepatitis E Virus Type 3> Hepatitis E Virus Genotype 3 (isolate Human/United States/US2) (HEV-3)

RefSeq

NC_001434.1 ; L08816.1

PubMed ID

10092008

Pathways Involved

Various pathway(s) in which protein is involved

KEGG

Not Available

Reactome

Not Available

Sequence

							MEAHQFIKAPGITTAIEQAALAAANSALANAVVVRPFLSRVQTEILINLMQPRQLVFRPEVLWNHPIQRVIHNELEQYCRARAGRCLEVGAHPRSINDNP
NVLHRCFLRPVGRDVQRWYSAPTRGPAANCRRSALRGLPPVDRTYCFDGFSRCAFAAETGVALYSLHDLWPADVAEAMARHGMTRLYAALHLPPEVLLPP
GTYHTTSYLLIHDGNRAVVTYEGDTSAGYNHDVSILRAWIRTTKIVGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGSPS
LFPSACSTKSTFHAVPVHIWDXLMLFGATLXDQAFCCSRLMTYLRGISYKVTVGALVANEGWNASEDALTAVITAAYLTICHQRYLRTQAISKGMRRLEV
EHAQKFITRLYSWLFEKSGRDYIPGRQLQFYAQCRRWLSAGFHLXPRXLVFDESVPCRCRTFLKKVAGKFCCFMRWLGQECTCFLEPAEGLVGDQGHDNE
AYEGSEVDPAEPAHLDVSGTYAVHGHQLEALYRALNVPHDIAARASRLTATVELVASPDRLECRTVLGNKTFRTTVVDGAHLEANGPEEYVLSFDASRQS
MGAGSHSLTYELTPAGLQVKISSNGLDCTATFPPGGAPSAAPGEVAAFCSALYRYNRFTQRHSLTGGLWLHPEGLLGIFPPFSPGHIWESANPFCGEGTL
YTRTWSTSGFSSDFSPPEAAAPASAAAPGLPYPTPPVSDIWVLPPPSEESHVDAASVPSVPEPAGLTSPIVLTPPPPPPPVRKPATSPPPRTRRLLYTYP
DGAKVYAGSLXESDCDWLVNASNPGHRPGGGLCHAFYQRFPEAFYSTEFIMREGLAAYTLTPRPIIHAVAPDYRVEQNPKRLEAAYRETCSRRGTAAYPL
LGSGIYQVPVSLSFDAWERNHRPGDELYLTEPAAAWFEANKPAQPALTITEDTARTANLALEIDAATEVGRACAGCTISPGIVHYQFTAGVPGSGKSRSI
QQGDVDVVVVPTRELRNSWRRRGFAAFTPHTAARVTIGRRVVIDEAPSLPPHLLLLHMQRASSVHLLGDPNQIPAIDFEHAGLVPAIRPELAPTSWWHVT
HRCPADVCELIRGAYPKIQTTSRVLRSLFWNEPAIGQKLVFTQAAKAANPGAITVHEAQGATFTETTIIATADARGLIQSSRAHAIVALTRHTEKCVILD
APGLLREVGISDVIVNNFFLAGGEVGHHRPSVIPRGNPDQNLGTLQAFPPSCQISAYHQLAEELGHRPAPVAAVLPPCPELEQGLLYMPQELTVSDSVLV
FELTDIVHCRMAAPSQRKAVLSTLVGRYGRRTKLYEAAHSDVRESLARFIPTIGPVRATTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDC
NKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKEILALLPPNIFYGDAYEESVFAAAVSGAGSCMVFENDFSEFDSTQNNFSLGLECVVMEECGM
PQWLIRLYHLVRSAWILQAPKESLKGFWKKHSGEPGTLLWNTVWNMAIIAHCYEFRDFRVAAFKGDDSVVLCSDYRQXRNAAALIAGCGLKLKVDYRPIG
LYAGVVVAPGLGTLPDVVRFAGRLSEKNWGPGPERAEQLRLAVCDFLRGLTNVAQVCVDVVSRVYGVSPGLVHNLIGMLQTIADGKAHFTENIKPVLDLT
NSIIQRVE
						

Length

1708

Alternate Sequence

Not Available

Non-standard residue

Not Available

Date of last Sequence modification

01-05-1999

Protein Existence

Inferred from homology

Amino Acid composition

Amino Acid	Count	% Frequency	Amino Acid	Count	% Frequency
Alanine (A)			Leucine (L)
Arginine (R)			Lysine (K)
Asparagine (N)			Methionine (M)
Aspartic Acid (D)			Phenylalanine (F)
Cysteine (C)			Proline (P)
Glutamine (Q)			Serine (S)
Glutamic Acid (E)			Threonine (T)
Glycine (G)			Tryptophan (W)
Histidine (H)			Tyrosine (Y)
Isoleucine (I)			Valine (V)

Sum of Absolute Deviation from Amino Acid Occurrence Frequencies

Aliphatic Index

Instability Index

Secondary Structure features

% Number of Residues in Helices	% Number of Residues in Strands	% Number of Residues in Coils

Structural Difficulty(SD) index

Role(s)

♦Methyltransferase displays a cytoplasmic capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GMP, GpppG, and GpppA were poor substrates for the methyltransferase. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure. Cap analogs such as m(7)GTP, m(7)GDP, et(2)m(7)GMP, and m(2)et(7)GMP inhibit the methyltransferase reaction (By similarity).
♦ RNA-directed RNA polymerase plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA, probably to initiate replication (By similarity).
♦ Helicase region exhibits NTPase and RNA unwinding activities. Hydrolyzes all rNTPs efficiently and unwinds only RNA duplexes with 5' overhangs showing 5'-to-3' polarity (By similarity).

EC

2.1.1.- , 2.7.7.- , 3.4.22.- , 3.6.4.- , 2.7.7.48

Experimentally known GO terms

GO:0003723 ; GO:0003968 ; GO:0004386 ; GO:0005524 ; GO:0006351 ;
GO:0006396 ; GO:0008174 ; GO:0008234 ; GO:0019082 ; GO:0039694

Subcellular Location

Not Available

Domain(s)

♦DOMAIN 56 240 Alphavirus-like MT.
♦ DOMAIN 790 936 Macro.
♦ DOMAIN 949 1097 (+)RNA virus helicase ATP-binding.
♦ DOMAIN 1098 1231 (+)RNA virus helicase C-terminal.
♦ DOMAIN 1469 1580 RdRp catalytic.

Motif(s)

Not Available

Methods of 3D structure generation

Predicted/Modelled

Experimetally known structure

Not Available

Active Site(s)

Not Available

Predicted 3D Structures

Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.

Experimentally known Ligand(s)

Not Available

Virtually Screened Ligands

Virtual screening has been performed using RASPD

						Million Molecules

					
Best 20 Hit molecules 
Not Available