ID D3JIS0_ADE18 Unreviewed; 448 AA.
AC D3JIS0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 28-JUN-2023, entry version 29.
DE RecName: Full=Packaging protein 1 {ECO:0000256|HAMAP-Rule:MF_04057};
DE AltName: Full=Packaging protein IVa2 {ECO:0000256|HAMAP-Rule:MF_04057};
GN Name=IVa2 {ECO:0000256|HAMAP-Rule:MF_04057,
GN ECO:0000313|EMBL:ACZ92147.1};
OS Human adenovirus A serotype 18 (HAdV-18) (Human adenovirus 18).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=10528 {ECO:0000313|EMBL:ACZ92147.1, ECO:0000313|Proteomes:UP000139114};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACZ92147.1, ECO:0000313|Proteomes:UP000139114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D.C. {ECO:0000313|EMBL:ACZ92147.1};
RX PubMed=20542532; DOI=10.1016/j.virol.2010.05.013;
RA Walsh M.P., Seto J., Tirado D., Chodosh J., Schnurr D., Seto D.,
RA Jones M.S.;
RT "Computational analysis of human adenovirus serotype 18.";
RL Virology 404:284-292(2010).
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:0000256|HAMAP-
CC Rule:MF_04057}.
CC -!- SUBUNIT: Homodimer. Part of a genome packaging complex composed of
CC packaging proteins 1, 2 and 3; this complex specifically binds to the
CC packaging sequence on the left end of viral genomic DNA and performs
CC packaging of the viral genome. Interacts with protein 33K.
CC {ECO:0000256|HAMAP-Rule:MF_04057}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04057}. Host
CC nucleus, host nucleoplasm {ECO:0000256|HAMAP-Rule:MF_04057}. Host
CC nucleus, host nucleolus {ECO:0000256|HAMAP-Rule:MF_04057}. Note=Located
CC at a unique vertex of the capsid. Present in about 6-8 copies per
CC virion. {ECO:0000256|HAMAP-Rule:MF_04057}.
CC -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000256|HAMAP-Rule:MF_04057}.
CC -!- SIMILARITY: Belongs to the adenoviridae packaging protein 1 family.
CC {ECO:0000256|HAMAP-Rule:MF_04057}.
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DR EMBL; GU191019; ACZ92147.1; -; Genomic_DNA.
DR Proteomes; UP000139114; Genome.
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:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0039708; P:nuclear capsid assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Activator {ECO:0000256|HAMAP-Rule:MF_04057};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04057};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04057};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04057};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04057};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04057};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_04057};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_04057};
KW Viral genome packaging {ECO:0000256|ARBA:ARBA00023219, ECO:0000256|HAMAP-
KW Rule:MF_04057};
KW Viral release from host cell {ECO:0000256|ARBA:ARBA00022612,
KW ECO:0000256|HAMAP-Rule:MF_04057}; Virion {ECO:0000256|HAMAP-Rule:MF_04057}.
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..448
FT /note="DNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
FT COMPBIAS 18..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
SQ SEQUENCE 448 AA; 51077 MW; C9957A32FE77E735 CRC64;
MESQGRRRPV QYQPSEFEAH IGQRTTRSAS IYSDGNNSQA HLATLERQNS RPPRRSSSHP
LQQQPTQPPQ RGNLLDRDAI ENITELWDRL QLLKQTLDHM PMADGLKPLK NFKSLQELLS
LGGERLLGEL AKQNTCVRQM MNEVAPLLRE DGSCTSLNYH LQPVIGVIYG PTGCGKSQLL
RNLLSAQLVT PAPETVFFIA PQVDMIPPSE IKAWEMQICE GNYAPGPQGT LIPQSGTLRP
KFVKLSYDDL TLDHNYDVSD PKNIFAQAAA VGPIAIIMDE CMENLGSHKA VSKFFHAFPS
KLHDKFPKCT GYTVLVVLHN MNPRRDLAGN IANLKIQSKM HIMSPRMHPT QLNRFINTYT
KGLPLAISLL LKDIFHHHAQ RSCYDWIIYN TTPEHEALQW CYLHPKDGLM PMYLNIQSHL
YSILEHIHRV ISDRERWTRA YHVRKNKH
//