AC   MF_03144;
DC   Protein; auto
TR   HAMAP; MF_03144; -; 1; level=0
XX
Names: RtcB_euk
XX
ID   RTCB
DE   RecName: Full=RNA-splicing ligase RtcB homolog;
DE            EC=6.5.1.8;
DE   AltName: Full=3'-phosphate/5'-hydroxy nucleic acid ligase;
case <OC:Vertebrata>
GN   Name=RTCB;
end case
XX
CC   -!- FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that
CC       acts by directly joining spliced tRNA halves to mature-sized tRNAs by
CC       incorporating the precursor-derived splice junction phosphate into the
CC       mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA
CC       ligase with broad substrate specificity, and may function toward other
CC       RNAs.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-
CC         ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA +
CC         diphosphate + GMP; Xref=Rhea:RHEA:68076, Rhea:RHEA-COMP:10463,
CC         Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83062,
CC         ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end
CC         dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-
CC         ribonucleotide-RNA + diphosphate + GMP + H(+); Xref=Rhea:RHEA:68080,
CC         Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83064,
CC         ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 manganese ions per subunit
CC   -!- SUBUNIT: Catalytic component of the tRNA-splicing ligase complex.
case <OC:Vertebrata>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- MISCELLANEOUS: Ligation probably proceeds through 3 nucleotidyl
CC       transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to
CC       3'-P termini in a step that precedes 3'-P activation with GMP. In the
CC       first nucleotidyl transfer step, RTCB reacts with GTP to form a
CC       covalent RTCB-histidine-GMP intermediate with release of PPi; in the
CC       second step, the GMP moiety is transferred to the RNA 3'-P; in the
CC       third step, the 5'-OH from the opposite RNA strand attacks the
CC       activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.
CC   -!- SIMILARITY: Belongs to the RtcB family.
XX
DR   PROSITE; PS01288; UPF0027; 1; trigger=no
DR   Pfam; PF01139; RtcB; 1; trigger=no
XX
case <OC:Vertebrata>
KW   Cytoplasm
end case
KW   GTP-binding
KW   Ligase
KW   Manganese
KW   Metal-binding
KW   Nucleotide-binding
KW   tRNA processing
XX
GO   GO:0072669; C:tRNA-splicing ligase complex
GO   GO:0016886; F:ligase activity, forming phosphoric ester bonds
GO   GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation
XX
FT   From: RTCB_HUMAN (Q9Y3I0)
FT   BINDING         226..230
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: N-H-Y-x-E
FT   BINDING         353..354
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: H-N
FT   BINDING         402..405
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: G-G-[TS]-M
FT   BINDING         428..431
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: H-G-[AS]-G
FT   ACT_SITE        428
FT                   /note="GMP-histidine intermediate"
FT   Condition: H
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: C
FT   BINDING         227
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         353
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         409
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: S
FT   BINDING         504
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: K
XX
XX
Size: 457-535;
Related: None;
Template: Q9Y3I0;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in CULQU, ENTDI, ENTHI
Plasmid: None
Comments: None
XX
# Revision 1.11 2022/11/19
//