ID A0A1X9RIR0_9ADEN Unreviewed; 422 AA.
AC A0A1X9RIR0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
OS Bat mastadenovirus WIV17.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Bat mastadenovirus F.
OX NCBI_TaxID=1986505 {ECO:0000313|EMBL:ARQ79746.1, ECO:0000313|Proteomes:UP000201453};
RN [1] {ECO:0000313|EMBL:ARQ79746.1, ECO:0000313|Proteomes:UP000201453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WIV17 {ECO:0000313|EMBL:ARQ79746.1};
RX PubMed=28475035; DOI=10.1099/jgv.0.000739;
RA Tan B., Yang X.L., Ge X.Y., Peng C., Liu H.Z., Zhang Y.Z., Zhang L.B.,
RA Shi Z.L.;
RT "Novel bat adenoviruses with low G+C content shed new light on the
RT evolution of adenoviruses.";
RL J. Gen. Virol. 98:739-748(2017).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KX961095; ARQ79746.1; -; Genomic_DNA.
DR OrthoDB; 5048at10239; -.
DR Proteomes; UP000201453; 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:UP000201453};
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..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..422
FT /note="DNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
FT COMPBIAS 19..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
SQ SEQUENCE 422 AA; 47904 MW; E74E141A8413162D CRC64;
MSNQCATVHS DGINPNKKIK TMEGQNNGTS GSTQISTLQQ KQSKSKKQRS LLDGITLGHV
TELWEKLNVL QNALKSMPWS EGLKPLKNFS SLQELLSLGG DKLINDLVNE NNQISEAMNS
VLPYLNPNKT CKSINFNMQP VIGVIYGPTG SGKSQLLRNL LSCHLINPPP ETIFFIVPQI
EMIPPQELAA WEIQICEGNY MPGEDNTIIP RSGSLLPQFI KMSYDEFTAQ QNYDIGDPNN
VFAKAAANGP IAIIMDECME NLGSHKGISQ FFHAFPSKLH NRFPKCTGYT VLVVLHNMNP
RKDHSGNIAT LKIQSKLHIL SPKMQPSQLN RFINTYTKGL PLAISLLLKD IFNYHNLHSN
FDWIIYNTCP ENEALQWMYL HPKEGLMPMY LNVQCMLYEI LLKIHRVISD RERWNKYYHK
HK
//
