ID A0A126HGN1_9CAUD Unreviewed; 316 AA. AC A0A126HGN1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 29-MAY-2024, entry version 26. DE RecName: Full=Sliding-clamp-loader large subunit {ECO:0000256|HAMAP-Rule:MF_04162}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04162}; DE AltName: Full=Clamp loader gp44 subunit {ECO:0000256|HAMAP-Rule:MF_04162}; GN ORFNames=phiGrn1_0193 {ECO:0000313|EMBL:ALP47015.1}; OS Vibrio phage phi-Grn1. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Straboviridae; Schizotequatrovirus; Schizotequatrovirus valkk3. OX NCBI_TaxID=1747713 {ECO:0000313|EMBL:ALP47015.1, ECO:0000313|Proteomes:UP000230575}; RN [1] {ECO:0000313|EMBL:ALP47015.1, ECO:0000313|Proteomes:UP000230575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27895630; RA Skliros D., Kalatzis P.G., Katharios P., Flemetakis E.; RT "Comparative Functional Genomic Analysis of Two Vibrio Phages Reveals RT Complex Metabolic Interactions with the Host Cell."; RL Front. Microbiol. 7:1807-1807(2016). CC -!- FUNCTION: Forms the sliding-clamp-loader together with the small CC subunit. Functions as an ATPase enzyme. The clamp loader holds the CC clamp in an open conformation and places it onto the DNA. 4 ATP CC molecules must bind to the sliding-clamp-loader before the latter can CC open the sliding clamp. ATP hydrolysis triggers the detachment of the CC sliding clamp from the sliding-clamp-loader, freeing the sliding clamp CC to track along DNA. {ECO:0000256|HAMAP-Rule:MF_04162}. CC -!- SUBUNIT: The sliding-clamp-loader consists of 4 large subunits and 1 CC small subunit. Interacts with the sliding clamp; this interaction CC allows the sliding-clamp-loader to open the sliding clamp. Part of the CC replicase complex that includes the DNA polymerase, the polymerase CC clamp, the clamp loader complex, the single-stranded DNA binding CC protein, the primase, the helicase and the helicase assembly factor. CC {ECO:0000256|HAMAP-Rule:MF_04162}. CC -!- SIMILARITY: Belongs to the Tevenvirinae sliding-clamp-loader large CC subunit family. {ECO:0000256|HAMAP-Rule:MF_04162}. 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; KT919972; ALP47015.1; -; Genomic_DNA. DR Proteomes; UP000230575; Genome. DR GO; GO:0005663; C:DNA replication factor C complex; IEA:TreeGrafter. DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:TreeGrafter. DR GO; GO:0031389; C:Rad17 RFC-like complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:TreeGrafter. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:TreeGrafter. DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule. DR CDD; cd00009; AAA; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.272.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_04162; T4_Clamp_Loader_L; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR048817; Gp44_C. DR InterPro; IPR048815; Gp44_lid. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR046388; T4_Clamp_Loader_L. DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1. DR PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF21429; Gp44_C; 1. DR Pfam; PF21328; Gp44_lid; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04162}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04162}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04162}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04162}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04162}; KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04162}. FT DOMAIN 41..161 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT BINDING 11..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04162" FT BINDING 23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04162" FT BINDING 52..57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04162" FT BINDING 203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04162" SQ SEQUENCE 316 AA; 35375 MW; DD3BD80F0DC86B3D CRC64; MNFDPKELLW EQRYRPQTIN DCVLPERVRE HFQAMIDSGE IPNMLLASSS PGTGKTTVAR AVLADMGYEV LFINASSSRG IKLVQNDLPA FCSTVSFSGK PKAIILDEAD NLTPDAQKAL RGLIEQYSKN VRFILTCNYS QKILTPIRSR LQTFEFVYDK DERLSCIKQM ILRSMSICKQ EGISVTNAAV LKELVKRNYP DNRKTVVALQ NYSRKGVIDE GILSEITAND DISEMIAALK SKDFKTIRGL IPKYSGDLAS FLHNLYKAAY TDLDGNSIPT FIQIVGEANN NATTCVDTEI LLAYTLVQIM LECTFV //