Tag | Content |
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CPLM ID | CPLM-002057 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Replication-associated protein |
Protein Synonyms/Alias | Rep; Protein AC1; Protein AL1 |
Gene Name | AC1, AL1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Tomato golden mosaic virus (strain Yellow vein) (TGMV) |
NCBI Taxa ID | 223341 |
Lysine Modification | Position | Peptide | Type | References |
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68 | VLIQFEGKYCCQNQR | sumoylation | [1] | 102 | AKSSSDVKTYIDKDG | sumoylation | [1] |
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Reference | [1] Interaction between geminivirus replication protein and the SUMO-conjugating enzyme is required for viral infection. Sánchez-Durán MA, Dallas MB, Ascencio-Ibañez JT, Reyes MI, Arroyo-Mateos M, Ruiz-Albert J, Hanley-Bowdoin L, Bejarano ER. J Virol. 2011 Oct;85(19):9789-800. [ PMID: 21775461] |
Functional Description | Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep- catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity). |
Sequence Annotation | NP_BIND 223 230 ATP (Potential). REGION 144 154 Binding to RBR1. REGION 157 177 Oligomerization. MOTIF 16 20 RCR-1. MOTIF 58 63 RCR-2. MOTIF 104 107 RCR-3. ACT_SITE 104 104 For DNA cleavage activity (By METAL 50 50 Divalent metal cation (Potential). METAL 58 58 Divalent metal cation (Potential). METAL 60 60 Divalent metal cation (Potential). METAL 108 108 Divalent metal cation (Potential). |
Keyword | ATP-binding; Complete proteome; Covalent protein-DNA linkage; DNA replication; DNA-binding; Endonuclease; Helicase; Host nucleus; Host-virus interaction; Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleotidyltransferase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 352 AA |
Protein Sequence | MPSHPKRFQI NAKNYFLTYP QCSLSKEESL SQLQALNTPI NKKFIKICRE LHEDGQPHLH 60 VLIQFEGKYC CQNQRFFDLV SPTRSAHFHP NIQRAKSSSD VKTYIDKDGD TLVWGEFQVD 120 GRSARGGCQT SNDAAAEALN ASSKEEALQI IREKIPEKYL FQFHNLNSNL DRIFDKTPEP 180 WLPPFHVSSF TNVPDEMRQW AENYFGKSSA ARPERPISII IEGDSRTGKT MWARSLGPHN 240 YLSGHLDLNS RVYSNKVEYN VIDDVTPQYL KLKHWKELIG AQRDWQTNCK YGKPVQIKGG 300 IPSIVLCNPG EGASYKVFLD KEENTPLKNW TFHNAKFVFL NSPLYQSSTQ SS 352 |
Gene Ontology | GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. GO:0019028; C:viral capsid; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. GO:0004386; F:helicase activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. GO:0005198; F:structural molecule activity; IEA:InterPro. GO:0006260; P:DNA replication; IEA:UniProtKB-KW. GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. |
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