TERM_ADEB2
ID TERM_ADEB2 Reviewed; 620 AA.
AC O55438;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 12-AUG-2020, entry version 59.
DE RecName: Full=Preterminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=pTP {ECO:0000255|HAMAP-Rule:MF_04061};
DE AltName: Full=Bellett protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE AltName: Full=Precursor terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Contains:
DE RecName: Full=Intermediate terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=iTP {ECO:0000255|HAMAP-Rule:MF_04061};
DE Contains:
DE RecName: Full=Terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=TP {ECO:0000255|HAMAP-Rule:MF_04061};
GN Name=PTP {ECO:0000255|HAMAP-Rule:MF_04061};
OS Bovine adenovirus 2 (BAdV-2) (Mastadenovirus bos2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Ovine mastadenovirus A.
OX NCBI_TaxID=114429;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=19;
RX PubMed=9612727; DOI=10.1159/000150555;
RA Ojkic D., Yagubi A., Bautista D., Haj-Ahmad Y.;
RT "Sequence analysis of the terminal protein precursor coding regions from
RT bovine adenovirus serotypes 2 and 3.";
RL Intervirology 40:253-262(1997).
CC -!- FUNCTION: Protein covalently bound to the viral DNA that acts as a
CC primer for viral genomic replication by DNA strand displacement.
CC Assembles on the viral origin of replication in an initiation complex
CC with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During
CC initiation, the polymerase covalently couples the first dCTP with Ser-
CC 580 of pTP. The terminal protein stimulates the template activity over
CC 20 fold compared to protein-free templates. Neo-synthesized viral
CC genomes are linked to two preterminal proteins, one for each 5' end.
CC These new genomes are encapsidated in the nucleus, and during capsid
CC maturation by viral protease, preterminal protein is first cleaved into
CC intermediary (iTP), then into mature TP. May play a role in host
CC nuclear matrix localization of genomic DNA. {ECO:0000255|HAMAP-
CC Rule:MF_04061}.
CC -!- SUBUNIT: Heterodimer with the polymerase; this heterodimer binds to bp
CC 9 to 18 of the genome. Interacts with host POU2F1; POU2F1 binds to the
CC auxiliary sequences in the inverted terminal repeats and tethers the
CC pTP-POL heterodimer to the origin DNA thereby participating in the
CC assembly of the pre-initiation complex (POL-TP-DBP-NFIA-POU2F1).
CC {ECO:0000255|HAMAP-Rule:MF_04061}.
CC -!- SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-
CC Rule:MF_04061}.
CC -!- PTM: Preterminal protein is used to replicate viral genome, upon
CC genomic encapsidation it is processed first into iTP and finally into
CC TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061}.
CC -!- SIMILARITY: Belongs to the adenoviridae terminal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04061}.
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DR EMBL; AF252854; AAB88488.1; -; Genomic_DNA.
DR RefSeq; NP_064287.1; NC_002513.1.
DR GeneID; 1732717; -.
DR KEGG; vg:1732717; -.
DR Proteomes; UP000154597; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039687; P:viral DNA strand displacement replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04061; ADV_TERM; 1.
DR InterPro; IPR003391; Adeno_preterminal.
DR Pfam; PF02459; Adeno_terminal; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage; DNA replication; DNA-binding; Host nucleus;
KW Phosphoprotein; Reference proteome; Viral DNA replication.
FT CHAIN 1..620
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221898"
FT CHAIN 188..620
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433940"
FT CHAIN 326..620
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433941"
FT MOTIF 356..365
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 187..188
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 325..326
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 545
FT /note="Priming of strand displacement replication by
FT covalently linking the first nucleotide of the new DNA
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT MOD_RES 545
FT /note="O-(5'-phospho-DNA)-serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
SQ SEQUENCE 620 AA; 71441 MW; 08AB33B5953F3124 CRC64;
MHLHYKPNGC LFILQNAIDC ARLTGQSIYT IEVFRPVRNI WNRAQEWARA AITPAGLGWM
SKYIYQYHRL MLMNLSPREP ATHNWPLYNY PPPHILVGYQ KLLQICNDYI FDVRAYSRLK
YSEQINFGSQ LMNWSVMANC SYTINTGAYH RFIDMDNFSD TLTSIQQAIL AEKIVADLAL
IRPMRGFGRT NLDADHDVPV EYLLQEQSKD IGACQERAWG LADRIRVQNA GRKDLVILTT
IRKLKTAYFN FFLVKHLPLA PEQELSLPCD CFWLDAFIQK FAESDQAAEI DEALRLQQVP
TQTLTKCIIS ALSLPNCAGT ALRGGAFTLR PREGNRAVTE SMRRARGEMI EQFVDRLPMR
RRRRREVPQP QVAAEEYPSE PEELSFESEV RTAVAETIRL LEEELTVSAR NQQFFNFAVN
FYEVIQRLEA LGDINETTLQ RWVMYFFVAE HIATTLNYLN HQIRVSSPFG RYVMLNLAQV
VMRARNEDGQ IVYSRARNEN GNTVLVTSCL ALALTWLPQL REQGEEIRAG RDEQFMAEIA
YHDNSGDVSE ILKQVAVNDA DIDSMEISFR FRVTGPVVFS GLREIQNINR RVIRAATLFR
QERRPLPALN ERVQLPPAQE
