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Preterminal protein (pTP) (Bellett protein) (Precursor terminal protein) [Cleaved into: Intermediate terminal protein (iTP); Terminal protein (TP)]

 TERM_ADE05              Reviewed;         671 AA.
P04499;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
29-OCT-2014, sequence version 2.
23-MAY-2018, entry version 69.
RecName: Full=Preterminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
Short=pTP {ECO:0000255|HAMAP-Rule:MF_04061};
AltName: Full=Bellett protein {ECO:0000255|HAMAP-Rule:MF_04061};
AltName: Full=Precursor terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
Contains:
RecName: Full=Intermediate terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
Short=iTP {ECO:0000255|HAMAP-Rule:MF_04061};
Contains:
RecName: Full=Terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
Short=TP {ECO:0000255|HAMAP-Rule:MF_04061};
Name=PTP {ECO:0000255|HAMAP-Rule:MF_04061};
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
NCBI_TaxID=28285;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6325298; DOI=10.1016/0378-1119(84)90244-0;
Dekker B.M.M., van Ormondt H.;
"The nucleotide sequence of fragment HindIII-C of human adenovirus
type 5 DNA (map positions 17.1-31.7).";
Gene 27:115-120(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=1727603; DOI=10.1016/0042-6822(92)90082-Z;
Chroboczek J., Bieber F., Jacrot B.;
"The sequence of the genome of adenovirus type 5 and its comparison
with the genome of adenovirus type 2.";
Virology 186:280-285(1992).
[3]
COVALENT DNA LINKAGE AT SER-580.
PubMed=7265205; DOI=10.1016/0022-2836(81)90208-4;
Desiderio S.V., Kelly T.J. Jr.;
"Structure of the linkage between adenovirus DNA and the 55,000
molecular weight terminal protein.";
J. Mol. Biol. 145:319-337(1981).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8497057;
Fredman J.N., Engler J.A.;
"Adenovirus precursor to terminal protein interacts with the nuclear
matrix in vivo and in vitro.";
J. Virol. 67:3384-3395(1993).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8416372;
Roovers D.J., van der Lee F.M., van der Wees J., Sussenbach J.S.;
"Analysis of the adenovirus type 5 terminal protein precursor and DNA
polymerase by linker insertion mutagenesis.";
J. Virol. 67:265-276(1993).
[6]
INTERACTION WITH HOST POU2F1.
PubMed=9013582; DOI=10.1074/jbc.272.6.3398;
van Leeuwen H.C., Rensen M., van der Vliet P.C.;
"The Oct-1 POU homeodomain stabilizes the adenovirus preinitiation
complex via a direct interaction with the priming protein and is
displaced when the replication fork passes.";
J. Biol. Chem. 272:3398-3405(1997).
[7]
INTERACTION WITH HOST POU2F1.
PubMed=10373599; DOI=10.1093/nar/27.13.2799;
Botting C.H., Hay R.T.;
"Characterisation of the adenovirus preterminal protein and its
interaction with the POU homeodomain of NFIII (Oct-1).";
Nucleic Acids Res. 27:2799-2805(1999).
[8]
FUNCTION, AND INTERACTION WITH HOST POU2F1.
PubMed=11847120; DOI=10.1093/emboj/21.4.725;
de Jong R.N., Mysiak M.E., Meijer L.A., van der Linden M.,
van der Vliet P.C.;
"Recruitment of the priming protein pTP and DNA binding occur by
overlapping Oct-1 POU homeodomain surfaces.";
EMBO J. 21:725-735(2002).
[9]
INTERACTION WITH THE POLYMERASE.
PubMed=12134025; DOI=10.1128/JVI.76.16.8200-8207.2002;
Brenkman A.B., Breure E.C., van der Vliet P.C.;
"Molecular architecture of adenovirus DNA polymerase and location of
the protein primer.";
J. Virol. 76:8200-8207(2002).
[10]
FUNCTION, AND IDENTIFICATION IN THE INITIATION COMPLEX.
PubMed=12747549;
Liu H., Naismith J.H., Hay R.T.;
"Adenovirus DNA replication.";
Curr. Top. Microbiol. Immunol. 272:131-164(2003).
[11]
FUNCTION, INTERACTION WITH THE POLYMERASE, AND MUTAGENESIS OF ASP-578
AND ASP-582.
PubMed=15273278; DOI=10.1093/nar/gkh726;
Mysiak M.E., Holthuizen P.E., van der Vliet P.C.;
"The adenovirus priming protein pTP contributes to the kinetics of
initiation of DNA replication.";
Nucleic Acids Res. 32:3913-3920(2004).
-!- FUNCTION: Protein covalently bound to the viral DNA that acts as a
primer for viral genomic replication by DNA strand displacement.
Assembles on the viral origin of replication in an initiation
complex with viral polymerase, DBP, host NFIA and host
POU2F1/OCT1. During initiation, the polymerase covalently couples
the first dCTP with Ser-580 of pTP. The terminal protein
stimulates the template activity over 20 fold compared to protein-
free templates. Neo-synthesized viral genomes are linked to two
preterminal proteins, one for each 5' end. These new genomes are
encapsidated in the nucleus, and during capsid maturation by viral
protease, preterminal protein is first cleaved into intermediary
(iTP), then into mature TP. May play a role in host nuclear matrix
localization of genomic DNA. {ECO:0000255|HAMAP-Rule:MF_04061,
ECO:0000269|PubMed:11847120, ECO:0000269|PubMed:12747549,
ECO:0000269|PubMed:15273278, ECO:0000269|PubMed:8416372,
ECO:0000269|PubMed:8497057}.
-!- SUBUNIT: Heterodimer with the polymerase; this heterodimer binds
to bp 9 to 18 of the genome (PubMed:12134025, PubMed:15273278).
Interacts with host POU2F1; POU2F1 binds to the auxiliary
sequences in the inverted terminal repeats and tethers the pTP-POL
heterodimer to the origin DNA thereby participating in the
assembly of the pre-initiation complex (POL-TP-DBP-NFIA-POU2F1)
(PubMed:9013582, PubMed:10373599, PubMed:11847120,
PubMed:12747549). {ECO:0000255|HAMAP-Rule:MF_04061,
ECO:0000269|PubMed:10373599, ECO:0000269|PubMed:11847120,
ECO:0000269|PubMed:12134025, ECO:0000269|PubMed:15273278,
ECO:0000269|PubMed:9013582, ECO:0000305|PubMed:12747549}.
-!- SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-
Rule:MF_04061, ECO:0000269|PubMed:8416372,
ECO:0000269|PubMed:8497057}.
-!- PTM: Preterminal protein is used to replicate viral genome, upon
genomic encapsidation it is processed first into iTP and finally
into TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061}.
-!- SIMILARITY: Belongs to the adenoviridae terminal protein family.
{ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X02996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A03840; UZADP5.
RefSeq; AP_000203.1; AC_000008.1.
SMR; P04499; -.
DIP; DIP-44807N; -.
IntAct; P04499; 1.
PRIDE; P04499; -.
OrthoDB; VOG0900004X; -.
Proteomes; UP000004992; Genome.
GO; GO:0044204; C:host cell nuclear matrix; IDA:UniProtKB.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
GO; GO:0039687; P:viral DNA strand displacement replication; IDA:UniProtKB.
HAMAP; MF_04061; ADV_TERM; 1.
InterPro; IPR003391; Adeno_preterminal.
Pfam; PF02459; Adeno_terminal; 1.
1: Evidence at protein level;
Complete proteome; Covalent protein-DNA linkage; DNA replication;
DNA-binding; Host nucleus; Phosphoprotein; Reference proteome;
Viral DNA replication.
CHAIN 1 671 Preterminal protein. {ECO:0000255|HAMAP-
Rule:MF_04061}.
/FTId=PRO_0000221894.
CHAIN 176 671 Intermediate terminal protein.
{ECO:0000255|HAMAP-Rule:MF_04061}.
/FTId=PRO_0000433932.
CHAIN 350 671 Terminal protein. {ECO:0000255|HAMAP-
Rule:MF_04061}.
/FTId=PRO_0000433933.
MOTIF 380 389 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04061}.
SITE 175 176 Cleavage; by adenovirus protease.
{ECO:0000255|HAMAP-Rule:MF_04061}.
SITE 349 350 Cleavage; by adenovirus protease.
{ECO:0000255|HAMAP-Rule:MF_04061}.
SITE 580 580 Priming of strand displacement
replication by covalently linking the
first nucleotide of the new DNA chain.
{ECO:0000255|HAMAP-Rule:MF_04061}.
MOD_RES 580 580 O-(5'-phospho-DNA)-serine.
{ECO:0000255|HAMAP-Rule:MF_04061,
ECO:0000269|PubMed:7265205}.
MUTAGEN 578 578 D->E: No effect on pTP initiation
activity. No effect on DNA binding.
{ECO:0000269|PubMed:15273278}.
MUTAGEN 578 578 D->N: Decreased pTP initiation activity
to 29% of wild-type activity. No effect
on DNA binding.
{ECO:0000269|PubMed:15273278}.
MUTAGEN 578 578 D->R: Decreased pTP initiation activity
to 7% of wild-type activity. No effect on
DNA binding.
{ECO:0000269|PubMed:15273278}.
MUTAGEN 582 582 D->E,N,R: Decreased pTP initiation
activity to 65% of wild-type activity. No
effect on DNA binding.
{ECO:0000269|PubMed:15273278}.
MUTAGEN 582 582 D->N: Decreased pTP initiation activity
to 85% of wild-type activity. No effect
on DNA binding.
{ECO:0000269|PubMed:15273278}.
MUTAGEN 582 582 D->R: Complete loss of pTP initiation
activity. No effect on DNA binding.
{ECO:0000269|PubMed:15273278}.
SEQUENCE 671 AA; 76500 MW; 075A579546FA3F91 CRC64;
MALSVNDCAR LTGQSVPTME HFLPLRNIWN RVRDFPRAST TAAGITWMSR YIYGYHRLML
EDLAPGAPAT LRWPLYRQPP PHFLVGYQYL VRTCNDYVFD SRAYSRLRYT ELSQPGHQTV
NWSVMANCTY TINTGAYHRF VDMDDFQSTL TQVQQAILAE RVVADLALLQ PMRGFGVTRM
GGRGRHLRPN SAAAAAIDAR DAGQEEGEEE VPVERLMQDY YKDLRRCQNE AWGMADRLRI
QQAGPKDMVL LSTIRRLKTA YFNYIISSTS ARNNPDRRPL PPATVLSLPC DCDWLDAFLE
RFSDPVDADS LRSLGGGVPT QQLLRCIVSA VSLPHGSPPP THNRDMTGGV FQLRPRENGR
AVTETMRRRR GEMIERFVDR LPVRRRRRRV PPPPPPPEEE EGEALMEEEI EEEEEAPVAF
EREVRDTVAE LIRLLEEELT VSARNSQFFN FAVDFYEAME RLEALGDINE STLRRWVMYF
FVAEHTATTL NYLFQRLRNY AVFARHVELN LAQVVMRARD AEGGVVYSRV WNEGGLNAFS
QLMARISNDL AATVERAGRG DLQEEEIEQF MAEIAYQDNS GDVQEILRQA AVNDTEIDSV
ELSFRLKLTG PVVFTQRRQI QEINRRVVAF ASNLRAQHQL LPARGADVPL PPLPAGPEPP
LPPGARPRHR F


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