TERM_ADE12
ID TERM_ADE12 Reviewed; 606 AA.
AC P12541;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 02-JUN-2021, entry version 73.
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 Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803925; DOI=10.1016/0378-1119(86)90403-8;
RA Shu L., Hong J.S., Wei Y.-F., Engler J.A.;
RT "Nucleotide sequence of the genes encoded in early region 2b of human
RT adenovirus type 12.";
RL Gene 46:187-195(1986).
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, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73487; CAA51884.1; -; Genomic_DNA.
DR EMBL; M14785; AAA42480.1; ALT_INIT; Genomic_DNA.
DR PIR; B25770; UZAD12.
DR Proteomes; UP000004993; 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; Viral DNA replication.
FT CHAIN 1..606
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221896"
FT CHAIN 141..606
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433936"
FT CHAIN 290..606
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433937"
FT REGION 573..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 320..329
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT COMPBIAS 580..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 140..141
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 289..290
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 515
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 515
FT /note="O-(5'-phospho-DNA)-serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT CONFLICT 248
FT /note="L -> F (in Ref. 2; AAA42480)"
FT /evidence="ECO:0000305"
FT CONFLICT 405..406
FT /note="EL -> DV (in Ref. 2; AAA42480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 69447 MW; A62C0E78DFD11A1C CRC64;
MRATTTAAGI TWMSRYIYEY HRLMLEDLAP GAAATLGWPL YREPPPHFLV GYQYLVRTCN
DYVFDSRAYS RLRYTETVQP GTQTVNWSVM TNCSYTINAG AYHRFVDVDD FATTLTQIQQ
AVLAERVVAD LALLQPLQGY GSTHMADRGN REVEVERLMQ DYYKDLGRCQ SDVWGMADRL
RIQQAGPKDV VLLKTIRGLK TAYFNYIISS IAQLPGTLEE TKLSLPCDCD WLDAFLERFS
DPVDMQTLSS LRGVPTQQII KCIISAVSLP NAPRNASFPI LHETELRGGV FELRPRENGR
AVTETMRRRR GEMIERFVDR LPVRRRRRRQ PPPPVVEEEI MEVEEEEQEI VPGAFQQEVR
ETVAELIRLL EEELTVAARN SQFFNFAVDF YEAMERLEAL GDINELTLRR WILYFFVSEH
VATTLNYLFQ RLRNYGVFAR LVELNLAQVV MRARDSEGGV VYSRVWNEIG LNAFSQLMSR
ISNDLAATIE RAGHGDLQEE EIDQLMAEIA YQDNSGDVQE ILRQAAVNDT EIDSVELSFR
FKTTGPVVFT QRRQIQDINR RVVAHASQLR AQHLPLPERQ ADIPLPPLPA GPEPPLPPGA
RPRRRF