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Database: UniProt
Entry: D3JIS0_ADE18
LinkDB: D3JIS0_ADE18
Original site: D3JIS0_ADE18 
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
//
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