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Database: UniProt
Entry: A0MK46_9ADEN
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Original site: A0MK46_9ADEN 
ID   A0MK46_9ADEN            Unreviewed;       447 AA.
AC   A0MK46;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:ABK35034.1};
OS   Human adenovirus 52.
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus G.
OX   NCBI_TaxID=332179 {ECO:0000313|EMBL:ABK35034.1, ECO:0000313|Proteomes:UP000109192};
RN   [1] {ECO:0000313|EMBL:ABK35034.1, ECO:0000313|Proteomes:UP000109192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T03-2244 {ECO:0000313|EMBL:ABK35034.1};
RX   PubMed=17360747; DOI=10.1128/JVI.02650-06;
RA   Jones M.S., Harrach B., Ganac R.D., Gozum M.M., Dela Cruz W.P., Riedel B.,
RA   Pan C., Delwart E.L., Schnurr D.P.;
RT   "New adenovirus species found in a patient presenting with
RT   gastroenteritis.";
RL   J. Virol. 81:5978-5984(2007).
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; DQ923122; ABK35034.1; -; Genomic_DNA.
DR   Proteomes; UP000109192; 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   Reference proteome {ECO:0000313|Proteomes:UP000109192};
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..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..447
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic 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   447 AA;  50926 MW;  AFFC87A317EC3811 CRC64;
     METQGRRRPL QHQQDEPEAH PRKRPARGSS LHRHRDHPHP NTETLEGQNP RGPGRPPAGA
     LQRKSAQPPQ PRSLLDRDSI EHVTELWDRL YLLRQSLEKM PMADGLKPLK HFNSLEELLS
     LGGERLLQNL VSENKHVRSM MNDVAPLLRP DGSCSSLNYQ LQPVIGVIYG PTGCGKSQLL
     RNLLSTQLIN PPPETVFFIA PQVDMIPPSE IKAWEMQICE GNYAPGPDGT IIPQSGTLLP
     RFVKMAYDEL TLEQNYDVSN PQNVFAKAAA RGPIAIIMDE CMENLGGHKG VSKFFHAFPS
     KLHDKFPKCT GYTVLVVLHN MNPRRDLGGN IANLKIQAKM HIISPRMHPS QLNRFVNTYT
     KGLPLAISLL LKDIFQFHAQ KPCYDWVIYN TTPEHDALQW SYLHPRDGLM PMYLNIQAHL
     YRVLENIHKV LNDRDRWTRA YRAKKNK
//
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