OE66_NPVAC
ID OE66_NPVAC Reviewed; 704 AA.
AC Q00704; P41451;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 23-FEB-2022, entry version 85.
DE RecName: Full=Non-sulfated chondroitin lyase E66;
DE Short=ODV-E66;
DE EC=4.2.2.- {ECO:0000269|PubMed:21715327};
DE Flags: Precursor;
GN Name=P79;
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L1;
RX PubMed=3292791; DOI=10.1128/jvi.62.8.2773-2781.1988;
RA Crawford A., Miller L.K.;
RT "Characterization of an early gene accelerating expression of late genes of
RT the baculovirus Autographa californica nuclear polyhedrosis virus.";
RL J. Virol. 62:2773-2781(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2;
RX PubMed=8091653; DOI=10.1006/viro.1994.1525;
RA Hong T., Braunagel S.C., Summers M.D.;
RT "Transcription, translation, and cellular localization of PDV-E66: a
RT structural protein of the PDV envelope of Autographa californica nuclear
RT polyhedrosis virus.";
RL Virology 204:210-222(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9108103; DOI=10.1073/pnas.94.8.4050;
RA Hong T., Summers M.D., Braunagel S.C.;
RT "N-terminal sequences from Autographa californica nuclear polyhedrosis
RT virus envelope proteins ODV-E66 and ODV-E25 are sufficient to direct
RT reporter proteins to the nuclear envelope, intranuclear microvesicles and
RT the envelope of occlusion derived virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4050-4055(1997).
RN [5]
RP FUNCTION.
RX PubMed=21440017; DOI=10.1016/j.virusres.2011.03.012;
RA Xiang X., Chen L., Hu X., Yu S., Yang R., Wu X.;
RT "Autographa californica multiple nucleopolyhedrovirus odv-e66 is an
RT essential gene required for oral infectivity.";
RL Virus Res. 158:72-78(2011).
RN [6]
RP FUNCTION.
RX PubMed=21715327; DOI=10.1074/jbc.m111.251157;
RA Sugiura N., Setoyama Y., Chiba M., Kimata K., Watanabe H.;
RT "Baculovirus envelope protein ODV-E66 is a novel chondroitinase with
RT distinct substrate specificity.";
RL J. Biol. Chem. 286:29026-29034(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-704, MUTAGENESIS OF ASN-236;
RP HIS-291; TYR-299; ARG-345 AND GLU-395, AND ACTIVE SITE.
RX PubMed=24512853; DOI=10.1016/j.febslet.2013.10.021;
RA Kawaguchi Y., Sugiura N., Kimata K., Kimura M., Kakuta Y.;
RT "The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus
RT envelope protein.";
RL FEBS Lett. 0:0-0(2013).
CC -!- FUNCTION: Component of the polyhedra envelope. Plays an essential role
CC in oral infectivity. May digest, with its chondroitin lyase activity,
CC the chondroitin sulfate barrier of the peritrophic matrix of the host
CC midgut to facilitate viral infection in the epithelial cells.
CC {ECO:0000269|PubMed:21440017, ECO:0000269|PubMed:21715327}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:9108103}.
CC Host nucleus {ECO:0000269|PubMed:9108103}. Host cytoplasm
CC {ECO:0000269|PubMed:9108103}.
CC -!- SIMILARITY: Belongs to the baculoviridae E66 family. {ECO:0000305}.
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DR EMBL; M96360; AAA81587.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66676.1; -; Genomic_DNA.
DR PIR; F72855; F72855.
DR RefSeq; NP_054075.1; NC_001623.1.
DR PDB; 3VSM; X-ray; 2.00 A; A=67-704.
DR PDB; 3VSN; X-ray; 2.00 A; A=67-704.
DR PDBsum; 3VSM; -.
DR PDBsum; 3VSN; -.
DR SMR; Q00704; -.
DR CAZy; PL23; Polysaccharide Lyase Family 23.
DR GeneID; 1403878; -.
DR KEGG; vg:1403878; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.70.98.100; -; 1.
DR InterPro; IPR006934; Baculo_ODV-E66.
DR InterPro; IPR043082; Baculo_ODV-E66_core.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR012970; Lyase_8_alpha_N.
DR Pfam; PF04850; Baculo_E66; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Lyase; Membrane;
KW Reference proteome; Signal; Viral envelope protein; Virion.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..704
FT /note="Non-sulfated chondroitin lyase E66"
FT /evidence="ECO:0000255"
FT /id="PRO_0000132929"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:24512853"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:24512853"
FT ACT_SITE 299
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:24512853"
FT SITE 345
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:24512853"
FT SITE 395
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:24512853"
FT MUTAGEN 236
FT /note="N->A: Complete loss of non-sulfated chondroitin
FT degrading activity."
FT /evidence="ECO:0000269|PubMed:24512853"
FT MUTAGEN 291
FT /note="H->A: Complete loss of non-sulfated chondroitin
FT degrading activity."
FT /evidence="ECO:0000269|PubMed:24512853"
FT MUTAGEN 299
FT /note="Y->F: Complete loss of non-sulfated chondroitin
FT degrading activity."
FT /evidence="ECO:0000269|PubMed:24512853"
FT MUTAGEN 345
FT /note="R->A: Complete loss of non-sulfated chondroitin
FT degrading activity."
FT /evidence="ECO:0000269|PubMed:24512853"
FT MUTAGEN 395
FT /note="E->A: Complete loss of non-sulfated chondroitin
FT degrading activity."
FT /evidence="ECO:0000269|PubMed:24512853"
FT CONFLICT 249
FT /note="I -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 73..93
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 179..187
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 425..429
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 471..478
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 497..506
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 535..541
FT /evidence="ECO:0007829|PDB:3VSM"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 595..603
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 626..634
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:3VSM"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 676..684
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:3VSM"
FT STRAND 699..703
FT /evidence="ECO:0007829|PDB:3VSM"
SQ SEQUENCE 704 AA; 79075 MW; B6B069F07157236D CRC64;
MSIVLIIVIV VIFLICFLYL SNSNNKNDAN KNNAFIDLNP LPLNATTATT TTAVATTTTN
NNNSIVAFRQ NNIQELQNFE RWFKNNLSYS FSQKAEKVVN PNRNWNDNTV FDNLSPWTSV
PDFGTVCHTL IGYCVRYNNT SDTLYQNPEL AYNLINGLRI ICSKLPDPPP HQQAPWGPVA
DWYHFTITMP EVFMNITIVL NETQHYDEAA SLTRYWLGLY LPTAVNSMGW HRTAGNSMRM
GVPYTYSQIL RGYSLAQIRQ EQGIQEILNT IAFPYVTQGN GLHVDSIYID HIDVRAYGYL
INSYFTFAYY TYYFGDEVIN TVGLTRAIEN VGSPEGVVVP GVMSRNGTLY SNVIGNFITY
PLAVHSADYS KVLTKLSKTY YGSVVGVTNR LAYYESDPTN NIQAPLWTMA RRIWNRRGRI
INYNANTVSF ESGIILQSLN GIMRIPSGTT STQSFRPTIG QTAIAKTDTA GAILVYAKFA
EMNNLQFKSC TLFYDHGMFQ LYYNIGVEPN SLNNTNGRVI VLSRDTSVNT NDLSFEAQRI
NNNNSSEGTT FNGVVCHRVP ITNINVPSLT VRSPNSSVEL VEQIISFQTM YTATASACYK
LNVEGHSDSL RAFRVNSDEN IYVNVGNGVK ALFNYPWVMV KENNKVSFMS ANEDTTIPFS
VIMNSFTSIG EPALQYSPSN CFVYGNGFKL NNSTFDLQFI FEIV
