TERM_ADES1
ID TERM_ADES1 Reviewed; 610 AA.
AC A9CB87;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 02-JUN-2021, entry version 41.
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 Snake adenovirus serotype 1 (SnAdV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Atadenovirus.
OX NCBI_TaxID=189830;
OH NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT guttata) implies common origin with the members of the proposed new genus
RT Atadenovirus.";
RL J. Gen. Virol. 83:2403-2410(2002).
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; DQ106414; ABA47237.1; -; Genomic_DNA.
DR RefSeq; YP_001552248.1; NC_009989.1.
DR PRIDE; A9CB87; -.
DR GeneID; 10973890; -.
DR KEGG; vg:10973890; -.
DR Proteomes; UP000136605; 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..610
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000425916"
FT CHAIN 178..610
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000425917"
FT CHAIN 286..610
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000425918"
FT REGION 288..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 328..337
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 177..178
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 285..286
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 549
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 549
FT /note="O-(5'-phospho-DNA)-serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
SQ SEQUENCE 610 AA; 70028 MW; 97C2D6BE41197FF4 CRC64;
MATRQIEAWH RLTGQRPQTL RYFMMTTDLN NRRILRQRTA SEAGIRWASR YFEYPVTQLL
DLRPFGPVTR NPPFEGEPPP NLLVGYYYVM KAINAYLFDQ RTVSNISYNL QLALATNERA
MVWQVLTDSS YSIDTGAFSR ALDGNTEDLG GTVVQIQNAV MMDRVLTSLT VTPVRGLGAV
VREQNNNGIA AFTVRPNFPQ ARVSKRDATL LRNICECKKA LINYITWSPC PPLPCQLDLP
FNDGWVEDFV RHFSSASPME NNSQNLVGDF AAVMTMGKQA GMRGGALTLR SGTQTGLPMR
LRQREGRRAV TATMRRRRGQ AVQSFIDSLP IRRRRRRGTR RQVEREDSVR EPPSPGEGPS
GIRAPEEEEE SFSDDVGLSR EDDRADFNQE VVDTIGQLIE ELERELNPAA EESGFFNFSQ
RMYGLLLQLQ RENRLTFQMI LTWLSNFFVL EHLASTLFYL NEQFVRNGLA RRNIGLQFAQ
VILRGRSDTG RELYTRVWYN REREAFHTLY DRIVTDFIAV TEMADTETMF QAPEEREQLL
ADMQYVENSG SVDEVIAQLQ TRAQQTDSVE LSFRIKFSGL VGYSQNPVIQ RSFERTREAA
IGRWRRQQQQ
