REP_HCYV5
ID REP_HCYV5 Reviewed; 280 AA.
AC D4N3P2;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE EC=3.6.1.-;
DE AltName: Full=ATP-dependent helicase Rep;
DE AltName: Full=RepP;
GN Name=Rep; ORFNames=ORF1;
OS Human associated cyclovirus 1 (isolate Homo sapiens/Pakistan/PK5510/2007)
OS (HuCyV-1) (Cyclovirus PK5510).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Cyclovirus.
OX NCBI_TaxID=742918;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20007276; DOI=10.1128/jvi.02109-09;
RA Li L., Kapoor A., Slikas B., Bamidele O.S., Wang C., Shaukat S.,
RA Masroor M.A., Wilson M.L., Ndjango J.B., Peeters M., Gross-Camp N.D.,
RA Muller M.N., Hahn B.H., Wolfe N.D., Triki H., Bartkus J., Zaidi S.Z.,
RA Delwart E.;
RT "Multiple diverse circoviruses infect farm animals and are commonly found
RT in human and chimpanzee feces.";
RL J. Virol. 84:1674-1682(2010).
CC -!- FUNCTION: Essential for the replication of viral ssDNA. The closed
CC circular ssDNA genome is first converted to a superhelical dsDNA. Rep
CC and/or Rep' binds a specific hairpin at the genome origin of
CC replication. Introduces an endonucleolytic nick within the conserved
CC sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby
CC initiating the rolling circle replication (RCR). Following cleavage,
CC binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The
CC cleavage gives rise to a free 3'-OH that serves as a primer for the
CC cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA
CC by rolling circle mechanism. After one round of replication, a Rep-
CC catalyzed nucleotidyl transfer reaction releases a circular single-
CC stranded virus genome, thereby terminating the replication. Displays
CC origin-specific DNA cleavage, and nucleotidyl transferase.
CC {ECO:0000250|UniProtKB:Q805H4}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q805H4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q805H4};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC {ECO:0000250|UniProtKB:Q805H4};
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:Q805H4}.
CC -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 is
CC probably involved in metal coordination. RCR-3 is required for
CC phosphodiester bond cleavage for initiation of RCR.
CC {ECO:0000250|UniProtKB:Q805H4}.
CC -!- SIMILARITY: Belongs to the nanoviruses/circoviruses replication-
CC associated protein family. {ECO:0000305}.
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DR EMBL; GQ404847; ADD62457.1; -; Genomic_DNA.
DR SMR; D4N3P2; -.
DR Proteomes; UP000146794; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003365; Viral_rep_N.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF02407; Viral_Rep; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..280
FT /note="Replication-associated protein"
FT /id="PRO_0000445708"
FT MOTIF 11..15
FT /note="RCR-1"
FT /evidence="ECO:0000250|UniProtKB:P27260"
FT MOTIF 47..53
FT /note="RCR-2"
FT /evidence="ECO:0000250|UniProtKB:P27260"
FT MOTIF 88..91
FT /note="RCR-3"
FT /evidence="ECO:0000250|UniProtKB:P27260"
FT ACT_SITE 88
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:P27260"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P27260"
SQ SEQUENCE 280 AA; 32665 MW; 59F5DA1CDFC787DA CRC64;
MSNSTVRRFC FTWNNYTELN YALCQEFIKK YCKYGIVGKE LAPTTNTPHL QGFCNLQKPM
RFSTIKKRLD NGIHIEKSMG SDTQNQTYCS KSGEFFEAGD PQCQGKRNDL QSVVDTIQAG
NGSLSSIANE HPTAYIRYFR GIQEYIKTVR PIPPRYHKTE VRYYHGPPGS GKSRRALEEA
TALASDLNDI YYKPRGTWWD GYKQQSCVII DDFYGWIKYD EMLKICDRYP YKVQIKGGFE
EFTSKYIWIT SNIDTNLLYK FNDYNDTAFV RRIEIKLLIE
