TERM_ADECR
ID TERM_ADECR Reviewed; 723 AA.
AC Q96682;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 02-JUN-2021, entry version 56.
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 Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine adenovirus 1
OS (strain RI261)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69151;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9129661; DOI=10.1099/0022-1317-78-4-873;
RA Morrison M.D., Onions D.E., Nicolson L.;
RT "Complete DNA sequence of canine adenovirus type 1.";
RL J. Gen. Virol. 78:873-878(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; Y07760; CAA69058.1; -; Genomic_DNA.
DR RefSeq; NP_044190.1; NC_001734.1.
DR GeneID; 1488952; -.
DR KEGG; vg:1488952; -.
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; Viral DNA replication.
FT CHAIN 1..723
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221901"
FT CHAIN 291..723
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433946"
FT CHAIN 423..723
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433947"
FT REGION 457..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 453..462
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 290..291
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 422..423
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 651
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 651
FT /note="O-(5'-phospho-DNA)-serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
SQ SEQUENCE 723 AA; 82334 MW; CB30D8A4DF948721 CRC64;
MPFSGLFSKS RSSSTRLEGW SLRNILPDSY FKCRNPSASS PSLSLNTLLA GMYASAASCF
ICTRGCTSGA APPCNRAKPS LSASSLTTEA GRGFICRKTG CICNGANESA IDSLFVLQNA
LDCARLTGQT PYTVEVFRPI RNIFNRVREY TRASTTSVGL AWMSKYIYQY HRLMLMNLSP
REPATEGWPL FLYPPPHLLV GYQYLVRTCN DYVFDTRSYS RLKYTEIHLP LQQKLNWTVM
ANCSYTINTG AYHRFIDFEN FEETLAQVQQ AVLAERVVAD LALIRPMRGY GTTNMAGDRQ
VPVEGLLQDH YKNLSQCQNH AWGLADRMRI QNAGNKDIVI LTTIRKLKTA FFNFLVSPRN
PHTILSLPCD CLWLDAFMQK FTDPTLSQFQ TIQSLPSQSV TKSIISALSL PGPAPCTPLS
GGAFELRPRE NGRAVTEEMR RRRGEMIERF IDRLPMRRRR RRAPPPPPMS EELSEPEVEA
FPPASPPRRS FEEEVRDTIV EAIRLLQEEL TVSARNEQFF NFAINFYEVI QRLEMLGNIN
ELTIRRWVMY FFVAEHVATT LNYLHHNLRL YPPCSRWVDL ELAQVVMRAR DHEGQVVYSR
VWNEMGENAF SQLMARVSGD LAATVERAGL GELEEEEMEQ FMADIAYHEN SGDVSEILRQ
VAINDTEVDS MELSFRFKVT GPVVFSQNRQ IQSINRRVVA LASQLRMQHR PLPAQHEQVQ
LPP
