RNA 3'-phosphate cyclase; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.

TIGRFAM: RNA methylase, NOL1/NOP2/sun family; PFAM: Fmu (Sun) domain protein; KEGG: hypothetical protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.

Thiamine-monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.

KEGG: hch:HCH_02741 hypothetical protein.

eRF1 domain 2 protein; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.

KEGG: abu:Abu_2180 hypothetical protein.

PFAM: class II aldolase/adducin family protein; KEGG: hsm:HSM_1905 putative aldolase.

DNA primase, small subunit; Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. [...]