TERM_ADE07
ID TERM_ADE07 Reviewed; 640 AA.
AC P03270;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 64.
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 B serotype 7 (HAdV-7) (Human adenovirus 7).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=10519;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Gomen;
RX PubMed=6301944; DOI=10.1016/0378-1119(83)90156-7;
RA Engler J.A., Hoppe M.S., van Bree M.P.;
RT "The nucleotide sequence of the genes encoded in early region 2b of human
RT adenovirus type 7.";
RL Gene 21:145-159(1983).
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; X03000; CAA26775.1; -; Genomic_DNA.
DR PIR; A03841; UZADP7.
DR PRIDE; P03270; -.
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..640
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221895"
FT CHAIN 158..640
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433934"
FT CHAIN 321..640
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433935"
FT REGION 232..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 351..360
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 157..158
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 320..321
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 640 AA; 73746 MW; FF9D96A336CAAC60 CRC64;
MNYFMPLRNI WNRVREFPRA STTASGITWM SRYIYGYHRL MLEDLAPGAP ATERWPLYRQ
PSPHFLIGYQ YLVRTCNDYI FDTRAYSRLK YTELVRPGHQ TVNWSVMANC SYTINTGAYH
RFVDFDDFQA TLTQVQQAIL AERVVAELAL VQPMRGFGIT RMHGRAGEEE VPVERLMQDY
YKDLARCQDD AWGMAHRLRI QQAGPKDLVL LATIRRLKTA YFNFITSSIV SPSQEGEGEE
RENPDRASSR PRPQETVLSL PCDCDWLDAF VERFSDPVDL ETIRSLRGVP TGQLIKCIIS
AVSLPNGEPP SHHFREMRGG VFTLRPRENG RAVTETMRRR RGEVIERFID RLPVRRRRRR
VPPPPAAPPE EEEMLVEEEE IEEEILGAFE REVRTTIAEL IRLLEEELTV SARNSQFFNF
AVNFYEAMER LEALGDVSEM PLRRWIMYFF VTEHIATTLN YLFQRLCNYA VFTRHVELNL
AQVVMRARDP VGAVVYSRVW NEAGMNAFSQ LIGRISNDLA ATVERAGRGD LQEEEIEQFM
AEIAYQDNSG DVQEILRQAA VNDTEIDSVE LSFRFKLTGP VAFTQRRQIQ DVNRRVVAHA
SLLRAQYQNL PARGADVPLP AMPPGPEPPL PPGARPRHRF
