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Protein

Non-sulfated chondroitin lyase E66

Gene

P79

Organism
Autographa californica nuclear polyhedrosis virus (AcMNPV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the polyhedra envelope. Plays an essential role in oral infectivity. May digest, with its chondroitin lyase activity, the chondroitin sulfate barrier of the peritrophic matrix of the host midgut to facilitate viral infection in the epithelial cells.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei236Proton acceptor1 Publication1
Active sitei291Proton acceptor1 Publication1
Active sitei299Proton donor1 Publication1
Sitei345Transition state stabilizer1 Publication1
Sitei395Important for catalytic activity1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Protein family/group databases

CAZyiPL23. Polysaccharide Lyase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-sulfated chondroitin lyase E66 (EC:4.2.2.-1 Publication)
Short name:
ODV-E66
Gene namesi
Name:P79
OrganismiAutographa californica nuclear polyhedrosis virus (AcMNPV)
Taxonomic identifieri46015 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageBaculoviridaeAlphabaculovirus
Virus hostiLepidoptera (butterflies and moths) [TaxID: 7088]
Proteomesi
  • UP000008292 Componenti: Genome

Subcellular locationi

  • Virion membrane 1 Publication
  • Host nucleus 1 Publication
  • Host cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi236N → A: Complete loss of non-sulfated chondroitin degrading activity. 1 Publication1
Mutagenesisi291H → A: Complete loss of non-sulfated chondroitin degrading activity. 1 Publication1
Mutagenesisi299Y → F: Complete loss of non-sulfated chondroitin degrading activity. 1 Publication1
Mutagenesisi345R → A: Complete loss of non-sulfated chondroitin degrading activity. 1 Publication1
Mutagenesisi395E → A: Complete loss of non-sulfated chondroitin degrading activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000013292924 – 704Non-sulfated chondroitin lyase E66Sequence analysisAdd BLAST681

Structurei

Secondary structure

1704
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi73 – 93Combined sources21
Turni107 – 109Combined sources3
Turni116 – 118Combined sources3
Helixi120 – 138Combined sources19
Turni143 – 146Combined sources4
Helixi148 – 164Combined sources17
Beta strandi171 – 173Combined sources3
Beta strandi175 – 177Combined sources3
Turni179 – 187Combined sources9
Helixi188 – 199Combined sources12
Turni200 – 202Combined sources3
Helixi206 – 220Combined sources15
Beta strandi222 – 227Combined sources6
Helixi234 – 250Combined sources17
Helixi255 – 259Combined sources5
Helixi262 – 272Combined sources11
Beta strandi275 – 283Combined sources9
Beta strandi288 – 290Combined sources3
Turni291 – 293Combined sources3
Helixi297 – 303Combined sources7
Helixi304 – 306Combined sources3
Helixi307 – 314Combined sources8
Helixi316 – 318Combined sources3
Helixi321 – 329Combined sources9
Helixi340 – 342Combined sources3
Helixi354 – 356Combined sources3
Beta strandi362 – 367Combined sources6
Turni368 – 371Combined sources4
Beta strandi372 – 376Combined sources5
Beta strandi378 – 385Combined sources8
Beta strandi393 – 396Combined sources4
Helixi404 – 409Combined sources6
Beta strandi412 – 415Combined sources4
Turni425 – 429Combined sources5
Beta strandi435 – 440Combined sources6
Beta strandi448 – 451Combined sources4
Beta strandi453 – 455Combined sources3
Beta strandi458 – 466Combined sources9
Beta strandi471 – 478Combined sources8
Helixi480 – 482Combined sources3
Beta strandi486 – 494Combined sources9
Beta strandi497 – 506Combined sources10
Beta strandi517 – 525Combined sources9
Helixi535 – 541Combined sources7
Turni542 – 544Combined sources3
Beta strandi549 – 551Combined sources3
Beta strandi554 – 558Combined sources5
Beta strandi570 – 572Combined sources3
Beta strandi578 – 585Combined sources8
Helixi587 – 591Combined sources5
Beta strandi595 – 603Combined sources9
Beta strandi611 – 614Combined sources4
Beta strandi620 – 624Combined sources5
Beta strandi626 – 634Combined sources9
Beta strandi637 – 642Combined sources6
Beta strandi645 – 650Combined sources6
Beta strandi655 – 658Combined sources4
Helixi659 – 668Combined sources10
Beta strandi676 – 684Combined sources9
Beta strandi687 – 691Combined sources5
Beta strandi699 – 703Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VSMX-ray2.00A67-704[»]
3VSNX-ray2.00A67-704[»]
ProteinModelPortaliQ00704.
SMRiQ00704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi46 – 52Poly-ThrSequence analysis7
Compositional biasi56 – 59Poly-ThrSequence analysis4
Compositional biasi60 – 63Poly-AsnSequence analysis4
Compositional biasi541 – 544Poly-AsnSequence analysis4

Sequence similaritiesi

Belongs to the baculoviridae E66 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
InterProiIPR006934. Baculo_ODV-E66.
IPR008929. Chondroitin_lyas.
IPR012329. Lyase_8_N.
[Graphical view]
PfamiPF04850. Baculo_E66. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00704-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVLIIVIV VIFLICFLYL SNSNNKNDAN KNNAFIDLNP LPLNATTATT
60 70 80 90 100
TTAVATTTTN NNNSIVAFRQ NNIQELQNFE RWFKNNLSYS FSQKAEKVVN
110 120 130 140 150
PNRNWNDNTV FDNLSPWTSV PDFGTVCHTL IGYCVRYNNT SDTLYQNPEL
160 170 180 190 200
AYNLINGLRI ICSKLPDPPP HQQAPWGPVA DWYHFTITMP EVFMNITIVL
210 220 230 240 250
NETQHYDEAA SLTRYWLGLY LPTAVNSMGW HRTAGNSMRM GVPYTYSQIL
260 270 280 290 300
RGYSLAQIRQ EQGIQEILNT IAFPYVTQGN GLHVDSIYID HIDVRAYGYL
310 320 330 340 350
INSYFTFAYY TYYFGDEVIN TVGLTRAIEN VGSPEGVVVP GVMSRNGTLY
360 370 380 390 400
SNVIGNFITY PLAVHSADYS KVLTKLSKTY YGSVVGVTNR LAYYESDPTN
410 420 430 440 450
NIQAPLWTMA RRIWNRRGRI INYNANTVSF ESGIILQSLN GIMRIPSGTT
460 470 480 490 500
STQSFRPTIG QTAIAKTDTA GAILVYAKFA EMNNLQFKSC TLFYDHGMFQ
510 520 530 540 550
LYYNIGVEPN SLNNTNGRVI VLSRDTSVNT NDLSFEAQRI NNNNSSEGTT
560 570 580 590 600
FNGVVCHRVP ITNINVPSLT VRSPNSSVEL VEQIISFQTM YTATASACYK
610 620 630 640 650
LNVEGHSDSL RAFRVNSDEN IYVNVGNGVK ALFNYPWVMV KENNKVSFMS
660 670 680 690 700
ANEDTTIPFS VIMNSFTSIG EPALQYSPSN CFVYGNGFKL NNSTFDLQFI

FEIV
Length:704
Mass (Da):79,075
Last modified:November 1, 1995 - v2
Checksum:iB6B069F07157236D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti249I → M (PubMed:3292791).Curated1
Sequence conflicti249I → M (PubMed:8091653).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96360 Genomic DNA. Translation: AAA81587.1.
L22858 Genomic DNA. Translation: AAA66676.1.
PIRiF72855.
RefSeqiNP_054075.1. NC_001623.1.

Genome annotation databases

GeneIDi1403878.
KEGGivg:1403878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96360 Genomic DNA. Translation: AAA81587.1.
L22858 Genomic DNA. Translation: AAA66676.1.
PIRiF72855.
RefSeqiNP_054075.1. NC_001623.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VSMX-ray2.00A67-704[»]
3VSNX-ray2.00A67-704[»]
ProteinModelPortaliQ00704.
SMRiQ00704.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL23. Polysaccharide Lyase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1403878.
KEGGivg:1403878.

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
InterProiIPR006934. Baculo_ODV-E66.
IPR008929. Chondroitin_lyas.
IPR012329. Lyase_8_N.
[Graphical view]
PfamiPF04850. Baculo_E66. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiOE66_NPVAC
AccessioniPrimary (citable) accession number: Q00704
Secondary accession number(s): P41451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.