ID 6.5.1.8 DE 3'-phosphate/5'-hydroxy nucleic acid ligase. CA (1) a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho- CA ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + CA diphosphate + GMP. CA (2) a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho- CA ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + CA diphosphate + GMP + H(+). CC -!- The enzyme is a 3'-5' nucleic acid ligase with the ability to join CC RNA with 3'-phosphate or 2',3'-cyclic-phosphate ends to RNA with CC 5'-hydroxy ends. CC -!- It can also join DNA with 3'-phosphate ends to DNA with 5'-hydroxy CC ends, provided the DNA termini are unpaired. CC -!- The enzyme is found in members of all three kingdoms of life, and is CC essential in metazoa for the splicing of intron-containing tRNAs. CC -!- The reaction follows a three-step mechanism with initial activation CC of the enzyme by GTP hydrolysis, forming a phosphoramide bond between CC the guanylate and a histidine residue. CC -!- The guanylate group is transferred to the 3'-phosphate terminus of CC the substrate, forming the capped structure [DNA/RNA]- CC 3'-(5'-diphosphoguanosine). CC -!- When a suitable 5'-OH end is available, the enzyme catalyzes an CC attack of the 5'-OH on the capped end to form a 3'-5' phosphodiester CC splice junction, releasing the guanylate. CC -!- When acting on an RNA 2',3'-cyclic-phosphate, the enzyme catalyzes an CC additional reaction, hydrolyzing the cyclic phosphate to a CC 3'-phosphate. CC -!- The metazoan enzyme requires activating cofactors in order to achieve CC multiple turnover catalysis. DR B0WCT9, RTCB1_CULQU; P0DX92, RTCB1_ECOS1; B0EAV2, RTCB1_ENTDS; DR C4M244, RTCB1_ENTH1; B0XKF3, RTCB2_CULQU; P0DX91, RTCB2_ECOS1; DR B0EIW5, RTCB2_ENTDS; C4M6T2, RTCB2_ENTH1; Q17FP1, RTCB_AEDAE ; DR Q9YB37, RTCB_AERPE ; Q7Q412, RTCB_ANOGA ; O29399, RTCB_ARCFU ; DR Q5E9T9, RTCB_BOVIN ; C3YN79, RTCB_BRAFL ; A8QC60, RTCB_BRUMA ; DR P90838, RTCB_CAEEL ; A8JC00, RTCB_CHLRE ; Q6NZS4, RTCB_DANRE ; DR Q54Y09, RTCB_DICDI ; Q9VIW7, RTCB_DROME ; P46850, RTCB_ECOLI ; DR Q9Y3I0, RTCB_HUMAN ; Q4R6X4, RTCB_MACFA ; Q58095, RTCB_METJA ; DR Q8TUS2, RTCB_METKA ; Q6LXF9, RTCB_METMP ; O27634, RTCB_METTH ; DR C1E9Y5, RTCB_MICCC ; C1MI97, RTCB_MICPC ; A9UXG6, RTCB_MONBE ; DR Q99LF4, RTCB_MOUSE ; P59975, RTCB_MYCBO ; P9WGW4, RTCB_MYCTO ; DR P9WGW5, RTCB_MYCTU ; Q74MJ0, RTCB_NANEQ ; A7RKF6, RTCB_NEMVE ; DR A4S3S3, RTCB_OSTLU ; Q00ZY2, RTCB_OSTTA ; A9CB42, RTCB_PAPAN ; DR Q19PY3, RTCB_PIG ; Q4YUZ9, RTCB_PLABA ; Q8IIU6, RTCB_PLAF7 ; DR B3L4K9, RTCB_PLAKH ; Q7RI54, RTCB_PLAYO ; Q9V168, RTCB_PYRAB ; DR Q8ZY09, RTCB_PYRAE ; Q8U0H4, RTCB_PYRFU ; O59245, RTCB_PYRHO ; DR Q6AYT3, RTCB_RAT ; B8LBM8, RTCB_THAPS ; Q4U923, RTCB_THEAN ; DR Q5JCZ1, RTCB_THEKO ; Q4N1R8, RTCB_THEPA ; B3RID0, RTCB_TRIAD ; DR Q561P3, RTCB_XENTR ; //