PKG1_ADE05
ID PKG1_ADE05 Reviewed; 449 AA.
AC P03271;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Packaging protein 1 {ECO:0000255|HAMAP-Rule:MF_04057};
DE AltName: Full=Packaging protein IVa2 {ECO:0000255|HAMAP-Rule:MF_04057};
GN Name=IVa2 {ECO:0000255|HAMAP-Rule:MF_04057};
OS Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7343420; DOI=10.1016/0378-1119(81)90074-3;
RA van Beveren C.P., Maat J., Dekker B.M.M., van Ormondt H.;
RT "The nucleotide sequence of the gene for protein IVa2 and of the 5' leader
RT segment of the major late mRNAs of adenovirus type 5.";
RL Gene 16:179-189(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [4]
RP DNA-BINDING.
RX PubMed=7175505; DOI=10.1099/0022-1317-63-1-69;
RA Russell W.C., Precious B.;
RT "Nucleic acid-binding properties of adenovirus structural polypeptides.";
RL J. Gen. Virol. 63:69-79(1982).
RN [5]
RP IDENTIFICATION IN THE PACKAGING COMPLEX.
RX PubMed=22811519; DOI=10.1128/jvi.01463-12;
RA Wu K., Orozco D., Hearing P.;
RT "The adenovirus L4-22K Protein is multifunctional and is an integral
RT component of crucial aspects of infection.";
RL J. Virol. 86:10474-10483(2012).
RN [6]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
RN [7]
RP INTERACTION WITH 33K PROTEIN.
RX PubMed=23388198; DOI=10.1099/vir.0.049346-0;
RA Ahi Y.S., Vemula S.V., Mittal S.K.;
RT "Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-
RT binding protein.";
RL J. Gen. Virol. 94:1325-1334(2013).
RN [8]
RP FUNCTION.
RX PubMed=25954255; DOI=10.3389/fmicb.2015.00318;
RA Ahi Y.S., Vemula S.V., Hassan A.O., Costakes G., Stauffacher C.,
RA Mittal S.K.;
RT "Adenoviral L4 33K forms ring-like oligomers and stimulates ATPase activity
RT of IVa2: implications in viral genome packaging.";
RL Front. Microbiol. 6:318-318(2015).
CC -!- FUNCTION: Component of the packaging machinery which encapsidates the
CC viral DNA into preformed capsids and transcriptional activator of the
CC viral major late promoter (MLP). Binds, along with packaging proteins 2
CC and 3, to the specific packaging sequence on the left end of viral
CC genomic DNA and displays ATPase activity thereby providing the power
CC stroke of the packaging machinery. The activity of packaging protein
CC IVa2 is stimulated by protein 33K which acts as a terminase. May be the
CC protein that pumps DNA into the capsid powered by ATP hydrolysis.
CC Specifically binds to the 5'-CG-3' nucleotides of the repeats making up
CC the packaging sequence. Component of the DEF-A and DEF-B transcription
CC factors that bind downstream elements of the major late promoter (MLP),
CC and stimulate transcription from the MLP after initiation of viral DNA
CC replication. DEF-A is a heterodimer packaging proteins 1 and 2 and DEF-
CC B is a homodimer of packaging protein 1. {ECO:0000255|HAMAP-
CC Rule:MF_04057, ECO:0000269|PubMed:25954255}.
CC -!- SUBUNIT: Homodimer (By similarity). Part of a genome packaging complex
CC composed of packaging proteins 1, 2 and 3; this complex specifically
CC binds to the packaging sequence on the left end of viral genomic DNA
CC and performs packaging of the viral genome (PubMed:22811519). Interacts
CC with protein 33K (PubMed:23388198). {ECO:0000255|HAMAP-Rule:MF_04057,
CC ECO:0000269|PubMed:22811519, ECO:0000269|PubMed:23388198}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04057}. Host
CC nucleus, host nucleoplasm {ECO:0000255|HAMAP-Rule:MF_04057}. Host
CC nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04057}. Note=Located
CC at a unique vertex of the capsid. Present in about 6-8 copies per
CC virion. {ECO:0000255|HAMAP-Rule:MF_04057}.
CC -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000255|HAMAP-Rule:MF_04057}.
CC -!- SIMILARITY: Belongs to the adenoviridae packaging protein 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04057}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02996; CAB40667.1; -; Genomic_DNA.
DR PIR; A03842; Q4ADA5.
DR RefSeq; AP_000201.1; AC_000008.1.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0044815; C:DNA packaging complex; IDA:UniProtKB.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR GO; GO:0046798; C:viral portal complex; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039708; P:nuclear capsid assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0098035; P:viral DNA genome packaging via site-specific sequence recognition; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04057; ADV_PKG1; 1.
DR InterPro; IPR003389; Adeno_IVa2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02456; Adeno_IVa2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; DNA-binding; Host nucleus; Nucleotide-binding;
KW Phosphoprotein; Transcription; Transcription regulation;
KW Viral genome packaging; Viral release from host cell; Virion.
FT CHAIN 1..449
FT /note="Packaging protein 1"
FT /id="PRO_0000221884"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..449
FT /note="DNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04057"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04057"
FT CONFLICT 163
FT /note="H -> Q (in Ref. 3; no nucleotide entry)"
SQ SEQUENCE 449 AA; 50887 MW; 20AD30752DCA96C2 CRC64;
METRGRRPAA LQHQQDQPQA HPGQRAARSA PLHRDPDYAD EDPAPVERHD PGPSGRAPTT
AVQRKPPQPA KRGDMLDRDA VEQVTELWDR LELLGQTLKS MPTADGLKPL KNFASLQELL
SLGGERLLAD LVRENMRVRD MLNEVAPLLR DDGSCSSLNY QLHPVIGVIY GPTGCGKSQL
LRNLLSSQLI SPTPETVFFI APQVDMIPPS ELKAWEMQIC EGNYAPGPDG TIIPQSGTLR
PRFVKMAYDD LILEHNYDVS DPRNIFAQAA ARGPIAIIMD ECMENLGGHK GVSKFFHAFP
SKLHDKFPKC TGYTVLVVLH NMNPRRDMAG NIANLKIQSK MHLISPRMHP SQLNRFVNTY
TKGLPLAISL LLKDIFRHHA QRSCYDWIIY NTTPQHEALQ WCYLHPRDGL MPMYLNIQSH
LYHVLEKIHR TLNDRDRWSR AYRARKTPK
