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
//