locus-tag	class	description
Izhevsk_103	COG0322	excinuclease ABC activity
Izhevsk_124	COG0187	DNA topoisomerase II activity
Izhevsk_125	COG0188	A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner
Izhevsk_130	COG0209	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Izhevsk_131	COG0208	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Izhevsk_139	COG0194	GDP metabolic process
Izhevsk_153	COG1404	Belongs to the peptidase S8 family
Izhevsk_157	COG0740	serine-type endopeptidase activity
Izhevsk_158	COG1793	dna ligase
Izhevsk_168	COG0462	Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P)
Izhevsk_178	COG0207	Catalyzes the reductive methylation of 2'-deoxyuridine- 5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis
Izhevsk_181	COG0740	serine-type endopeptidase activity
Izhevsk_183	COG1435	thymidine kinase activity
Izhevsk_185	COG0587	DNA-directed DNA polymerase activity
Izhevsk_187	COG0817	Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group
Izhevsk_197	COG5632	N-Acetylmuramoyl-L-alanine amidase
Izhevsk_197	COG3409	Peptidoglycan-binding domain 1 protein
Izhevsk_197	COG1388	LysM domain
Izhevsk_204	COG2433	Pfam Transposase IS66
Izhevsk_207	COG0739	heme binding
Izhevsk_207	COG1196	nuclear chromosome segregation
Izhevsk_207	COG0741	lytic transglycosylase activity
Izhevsk_208	COG0582	viral genome integration into host DNA
Izhevsk_22	COG2195	Cleaves the N-terminal amino acid of tripeptides
Izhevsk_230	COG1875	ATPase related to phosphate starvation-inducible protein PhoH
Izhevsk_242	COG0739	heme binding
Izhevsk_248	COG0507	A helicase nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD
Izhevsk_75	COG3091	SprT-like family
Izhevsk_85	COG3584	3D domain protein
Izhevsk_85	COG1388	LysM domain
Izhevsk_86	COG0125	Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis
Izhevsk_93	COG0608	single-stranded DNA 5'-3' exodeoxyribonuclease activity
Izhevsk_95	COG0317	In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance