ID F2WTN2_9ADEN Unreviewed; 450 AA.
AC F2WTN2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 08-NOV-2023, entry version 36.
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 Simian adenovirus 50.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Simian mastadenovirus B.
OX NCBI_TaxID=995023 {ECO:0000313|EMBL:ADZ39867.1, ECO:0000313|Proteomes:UP000170956};
RN [1] {ECO:0000313|EMBL:ADZ39867.1, ECO:0000313|Proteomes:UP000170956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18222 {ECO:0000313|EMBL:ADZ39867.1};
RX PubMed=19578438; DOI=10.1371/journal.ppat.1000503;
RA Roy S., Vandenberghe L.H., Kryazhimskiy S., Grant R., Calcedo R., Yuan X.,
RA Keough M., Sandhu A., Wang Q., Medina-Jaszek C.A., Plotkin J.B.,
RA Wilson J.M.;
RT "Isolation and characterization of adenoviruses persistently shed from the
RT gastrointestinal tract of non-human primates.";
RL PLoS Pathog. 5:E1000503-E1000503(2009).
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; HQ241820; ADZ39867.1; -; Genomic_DNA.
DR Proteomes; UP000170956; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR003389; Adeno_IVa2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02456; Adeno_IVa2; 1.
DR SMART; SM00382; AAA; 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 DOMAIN 164..348
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..450
FT /note="DNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04057"
SQ SEQUENCE 450 AA; 51039 MW; 9E1511C658D35776 CRC64;
METRGGRKRP LQHQSPQPQA HAGQRPTRGP SLHRHRDHPH ADPQTLAGPD PGPPRRPPPG
ALQRKPPQPP QPGDLLDRDA LVEDVSELWE RLQLLRQSLQ NMPMADGLKP LKGFDTLSEL
LSLGGQRLLT HLARENRQVR RMMDEVAPLL RPDGSCSSLN YQLQPVIGVI YGPTGCGKSQ
LLRNLLSAQL VSPAPETVFF IAPQVDMIPP SEIKAWEMQI CEGNYAPGPE GTIVPQSGTL
RPRFVKLSYD DLTLEHNYDV SDPRNIFAQA AARGPIAIIM DECMENLGGH KGVSKFFHAF
PSKLHDKFPR CTGYTVLVVL HNMNPRRDLG GNIANLKIQA KMHIISPRMH PSQLNRFVNT
YTKGLPLAIS LLLKDIFHHH AQKPAYDWII YNTTPEHEAM QWCYLHPREG LMPMYLHIQA
RLYRVLENIH RVLNDRDRWS RAYHARKNKQ
//
