VE1_HPV33
ID VE1_HPV33 Reviewed; 644 AA.
AC P06421;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Replication protein E1 {ECO:0000255|HAMAP-Rule:MF_04000};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04000};
DE AltName: Full=ATP-dependent helicase E1 {ECO:0000255|HAMAP-Rule:MF_04000};
GN Name=E1 {ECO:0000255|HAMAP-Rule:MF_04000};
OS Human papillomavirus 33.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10586;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009902; DOI=10.1128/jvi.58.3.991-995.1986;
RA Cole S.T., Streeck R.E.;
RT "Genome organization and nucleotide sequence of human papillomavirus type
RT 33, which is associated with cervical cancer.";
RL J. Virol. 58:991-995(1986).
RN [2]
RP DOMAIN E2 PROTEIN BINDING.
RX PubMed=8623535; DOI=10.1006/viro.1996.0242;
RA Mueller F., Sapp M.;
RT "Domains of the E1 protein of human papillomavirus type 33 involved in
RT binding to the E2 protein.";
RL Virology 219:247-256(1996).
CC -!- FUNCTION: ATP-dependent DNA helicase required for initiation of viral
CC DNA replication. It forms a complex with the viral E2 protein. The E1-
CC E2 complex binds to the replication origin which contains binding sites
CC for both proteins. During the initial step, a dimer of E1 interacts
CC with a dimer of protein E2 leading to a complex that binds the viral
CC origin of replication with high specificity. Then, a second dimer of E1
CC displaces the E2 dimer in an ATP-dependent manner to form the E1
CC tetramer. Following this, two E1 monomers are added to each half of the
CC site, which results in the formation of two E1 trimers on the viral
CC ori. Subsequently, two hexamers will be created. The double hexamer
CC acts as a bi-directional helicase machinery and unwinds the viral DNA
CC and then recruits the host DNA polymerase to start replication.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04000};
CC -!- SUBUNIT: Can form hexamers. Interacts with E2 protein; this interaction
CC increases E1 DNA binding specificity. Interacts with host DNA
CC polymerase subunit POLA2. Interacts with host single stranded DNA-
CC binding protein RPA1. Interacts with host TOP1; this interaction
CC stimulates the enzymatic activity of TOP1. {ECO:0000255|HAMAP-
CC Rule:MF_04000}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
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DR EMBL; M12732; AAA46960.1; -; Genomic_DNA.
DR PIR; A03660; W1WL33.
DR SMR; P06421; -.
DR Proteomes; UP000009118; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.510; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04000; PPV_E1; 1.
DR InterPro; IPR001177; DNA_helicase_E1_C_Papillomavir.
DR InterPro; IPR014000; DNA_helicase_E1_N_Papillomavir.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016393; Rep_E1_papillomaV.
DR InterPro; IPR037102; Znf_lg_T-Ag_D1_dom_sf.
DR Pfam; PF00519; PPV_E1_C; 1.
DR Pfam; PF00524; PPV_E1_N; 1.
DR PIRSF; PIRSF003383; Rep_E1_papillomaV; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..644
FT /note="Replication protein E1"
FT /id="PRO_0000133131"
FT DOMAIN 444..594
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 179..345
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 312..644
FT /note="Required for E2 binding"
FT MOTIF 86..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT BINDING 470..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 644 AA; 72469 MW; F6F5A93C9E32D201 CRC64;
MADPEGTNGA GMGCTGWFEV EAVIERRTGD NISEDEDETA DDSGTDLLEF IDDSMENSIQ
ADTEAARALF NIQEGEDDLN AVCALKRKFA ACSQSAAEDV VDRAANPCRT SINKNKECTY
RKRKIDELED SGYGNTEVET QQMVQQVESQ NGDTNLNDLE SSGVGDDSEV SCETNVDSCE
NVTLQEISNV LHSSNTKANI LYKFKEAYGI SFMELVRPFK SDKTSCTDWC ITGYGISPSV
AESLKVLIKQ HSLYTHLQCL TCDRGIIILL LIRFRCSKNR LTVAKLMSNL LSIPETCMVI
EPPKLRSQTC ALYWFRTAMS NISDVQGTTP EWIDRLTVLQ HSFNDNIFDL SEMVQWAYDN
ELTDDSDIAY YYAQLADSNS NAAAFLKSNS QAKIVKDCGI MCRHYKKAEK RKMSIGQWIQ
SRCEKTNDGG NWRPIVQLLR YQNIEFTAFL GAFKKFLKGI PKKSCMLICG PANTGKSYFG
MSLIQFLKGC VISCVNSKSH FWLQPLSDAK IGMIDDVTPI SWTYIDDYMR NALDGNEISI
DVKHRALVQL KCPPLLLTSN TNAGTDSRWP YLHSRLTVFE FKNPFPFDEN GNPVYAINDE
NWKSFFSRTW CKLDLIEEED KENHGGNIST FKCSAGENTR SLRS
