PKG3_ADEG1
ID PKG3_ADEG1 Reviewed; 378 AA.
AC Q64753;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 63.
DE RecName: Full=Packaging protein 3 {ECO:0000255|HAMAP-Rule:MF_04058};
DE AltName: Full=L1-52/55 kDa protein {ECO:0000255|HAMAP-Rule:MF_04058};
DE AltName: Full=Packaging protein 52K {ECO:0000255|HAMAP-Rule:MF_04058};
GN Name=L1 {ECO:0000255|HAMAP-Rule:MF_04058};
OS Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
CC -!- FUNCTION: Involved in viral genome packaging through its interaction
CC with packaging proteins 1 and 2. After proteolytic cleavage by
CC adenovirus protease, L1 52/55k protein is removed from the capsid
CC during viral maturation. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- SUBUNIT: Part of the genome packaging complex composed of packaging
CC proteins 1, 2 and 3; this complex specifically binds to the packaging
CC sequence on the left end of viral genomic DNA and performs packaging of
CC the viral genome. Interacts with hexon-linking protein IIIa; this
CC interaction is required to promote correct genome packaging.
CC {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04058}.
CC Note=Nuclear protein present in empty capsids and assembly
CC intermediates. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- INDUCTION: Expressed in the early phase and late phase of the viral
CC replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- PTM: Cleaved at different sites by the viral protease during virion
CC maturation. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC -!- SIMILARITY: Belongs to the adenoviridae packaging protein 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_04058}.
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DR EMBL; U46933; AAC54906.1; -; Genomic_DNA.
DR RefSeq; NP_043880.1; NC_001720.1.
DR GeneID; 1476560; -.
DR Proteomes; UP000001594; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04058; ADV_PKG3; 1.
DR InterPro; IPR037536; ADV_PKG3.
DR InterPro; IPR004292; L1-like.
DR Pfam; PF03052; Adeno_52K; 1.
PE 3: Inferred from homology;
KW Host nucleus; Late protein; Phosphoprotein; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..378
FT /note="Packaging protein 3"
FT /id="PRO_0000221871"
FT REGION 1..178
FT /note="Interaction with packaging protein 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
SQ SEQUENCE 378 AA; 42121 MW; 68326C65EF3DB755 CRC64;
MHPVLQSVRN ASVSAGGPHQ QQPQQQQHGV SSVRRPPSPP RYPAQHAYPG AGATPTAGRG
DFDGALDPDE GPVACGLAAG AGVDEVRMRE RDAARRATVP EINLFKARRD VVPNGDYERD
LMYHSGQAID IDRQRVLTPE DFKGSEPAFT PAVNHMRAAE LKRAAEQTAF GEELRNTCHQ
TRIRTALLRP EIGAGIYYLY DFVQTYLEHP DGRVKLNPQL VLVAQHAGNT MLAQRLWAIA
EEKNAWLRDL IEMAYMIVND PYLNTEQQLS AICTTVVELS MKYAKLAAKN GYPSMAQMAK
AQEFFYRVMQ AVLDLGVQVG VYNNRPARYR QKRMSEIPQM TDAEYMFGLT QALESRPPQG
ESFADEGPSE SDDEDDFI