UBIL_NPVAC
ID UBIL_NPVAC Reviewed; 77 AA.
AC P16709;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=viral Ubiquitin;
DE Flags: Precursor;
GN Name=vUbi;
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=E2;
RX PubMed=3944847; DOI=10.1128/jvi.57.2.563-571.1986;
RA Guarino L.A., Summers M.D.;
RT "Functional mapping of a trans-activating gene required for expression of a
RT baculovirus delayed-early gene.";
RL J. Virol. 57:563-571(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2153300; DOI=10.1073/pnas.87.1.409;
RA Guarino L.A.;
RT "Identification of a viral gene encoding a ubiquitin-like protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:409-413(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2219715; DOI=10.1016/0042-6822(90)90266-t;
RA Guarino L.A., Smith M.W.;
RT "Nucleotide sequence and characterization of the 39K gene region of
RT Autographa californica nuclear polyhedrosis virus.";
RL Virology 179:1-8(1990).
RN [4]
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 [5]
RP INTERACTION WITH IE0 AND VUBI, AND SUBCELLULAR LOCATION.
RX PubMed=29142135; DOI=10.1128/jvi.01713-17;
RA Biswas S., Willis L.G., Fang M., Nie Y., Theilmann D.A.;
RT "Autographa californica Nucleopolyhedrovirus AC141 (Exon0), a potential E3
RT ubiquitin ligase, interacts with viral Ubiquitin and AC66 to facilitate
RT nucleocapsid egress.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Viral ubiquitin that may play a role in the viral
CC ubiquitination of nucleocapsid proteins to direct the egress of the
CC nucleocapsid out of the nucleus, therefore mediating the formation of
CC budded virus (BV). {ECO:0000269|PubMed:29142135}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:29142135}. Host
CC cytoplasm {ECO:0000269|PubMed:29142135}. Note=Localizes in the ring
CC zone of the host nucleus, and also in the cytoplasm.
CC {ECO:0000269|PubMed:29142135}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; M30305; AAA46751.1; -; Genomic_DNA.
DR EMBL; M37122; AAA46685.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66665.1; -; Genomic_DNA.
DR PIR; A34813; UQNVAC.
DR PIR; C72854; C72854.
DR RefSeq; NP_054064.1; NC_001623.1.
DR PDB; 6KNA; NMR; -; A=1-76.
DR PDBsum; 6KNA; -.
DR SMR; P16709; -.
DR PRIDE; P16709; -.
DR GeneID; 1403867; -.
DR KEGG; vg:1403867; -.
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:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Isopeptide bond; Late protein;
KW Modulation of host ubiquitin pathway by viral ubl;
KW Modulation of host ubiquitin pathway by virus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="viral Ubiquitin"
FT /id="PRO_0000035981"
FT PROPEP 77
FT /evidence="ECO:0000305"
FT /id="PRO_0000035982"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CONFLICT 20
FT /note="A -> E (in Ref. 2; AAA46751)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6KNA"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6KNA"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:6KNA"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6KNA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6KNA"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6KNA"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:6KNA"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6KNA"
SQ SEQUENCE 77 AA; 8653 MW; EF9C11D902ABC35A CRC64;
MQIFIKTLTG KTITAETEPA ETVADLKQKI ADKEGVPVDQ QRLIFAGKQL EDSKTMADYN
IQKESTLHMV LRLRGGY
