ID A0A497PNX8_THOAR Unreviewed; 144 AA. AC A0A497PNX8; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 07-OCT-2020, entry version 8. DE RecName: Full=3'-phosphate/5'-hydroxy nucleic acid ligase {ECO:0000256|ARBA:ARBA00017066}; DE EC=6.5.1.8 {ECO:0000256|ARBA:ARBA00012726}; DE AltName: Full=RNA-splicing ligase RtcB {ECO:0000256|ARBA:ARBA00015720}; DE Flags: Fragment; GN ORFNames=DRP09_17745 {ECO:0000313|EMBL:RLI52518.1}; OS Thorarchaeota archaeon (strain OWC). OC Archaea; Asgard group; Candidatus Thorarchaeota. OX NCBI_TaxID=2053491 {ECO:0000313|EMBL:RLI52518.1, ECO:0000313|Proteomes:UP000273160}; RN [1] {ECO:0000313|EMBL:RLI52518.1, ECO:0000313|Proteomes:UP000273160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B59_G1 {ECO:0000313|EMBL:RLI52518.1}; RA Dombrowski N., Teske A., Baker B.J.; RT "Extensive metabolic versatility and redundancy in microbially diverse, RT dynamic hydrothermal sediments."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(Ribonucleotide)(n)-2',3'-cyclophosphate + 5'-hydroxy- CC (ribonucleotide)(m) + GTP + H(2)O = (ribonucleotide)(n+m) + GMP + CC diphosphate (overall reaction).; EC=6.5.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00000761}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(Ribonucleotide)(n)-3'-phosphate + 5'-hydroxy- CC (ribonucleotide)(m) + GTP = (ribonucleotide)(n+m) + GMP + CC diphosphate.; EC=6.5.1.8; Evidence={ECO:0000256|ARBA:ARBA00001461}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR601233-3}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR601233-3}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SIMILARITY: Belongs to the RtcB family. CC {ECO:0000256|ARBA:ARBA00008071}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RLI52518.1}. 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; QMYS01000206; RLI52518.1; -; Genomic_DNA. DR Proteomes; UP000273160; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008452; F:RNA ligase activity; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.90.1860.10; -; 1. DR InterPro; IPR001233; RtcB. DR InterPro; IPR036025; RtcB-like_sf. DR Pfam; PF01139; RtcB; 2. DR SUPFAM; SSF103365; SSF103365; 1. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601233-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601233-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}. FT METAL 62 FT /note="Manganese 1" FT /evidence="ECO:0000256|PIRSR:PIRSR601233-3" FT NON_TER 144 FT /evidence="ECO:0000313|EMBL:RLI52518.1" SQ SEQUENCE 144 AA; 15473 MW; F52EB4BC344AE923 CRC64; MKTKIYAEVL EQQALDQFNA AMSLPCAVQG ALMPDAHTGY SLPIGAVVKT DGEIFPSFVG FDIGCGVACL ELAINYKSVN LELLKSHILN TIPIGFNKHS EPQDTSSLDF TGTSVKLQDI FSQKGKHQLG TLGGGNHFIE VGYL //