A0A182F4X4 · A0A182F4X4_ANOAL

Function

function

Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.

Miscellaneous

Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site120Mn2+ 1 (UniProtKB | ChEBI)
Binding site123Mn2+ 1 (UniProtKB | ChEBI)
Binding site123Mn2+ 2 (UniProtKB | ChEBI)
Binding site227-231GMP (UniProtKB | ChEBI)
Binding site228Mn2+ 1 (UniProtKB | ChEBI)
Binding site260Mn2+ 2 (UniProtKB | ChEBI)
Binding site354Mn2+ 2 (UniProtKB | ChEBI)
Binding site354-355GMP (UniProtKB | ChEBI)
Binding site403-406GMP (UniProtKB | ChEBI)
Binding site410GMP (UniProtKB | ChEBI)
Active site429GMP-histidine intermediate
Binding site429-432GMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmembrane
Cellular ComponenttRNA-splicing ligase complex
Molecular FunctionGTP binding
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionphosphoprotein phosphatase activity
Molecular FunctionRNA ligase (GTP) activity
Biological ProcesstRNA splicing, via endonucleolytic cleavage and ligation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RNA-splicing ligase RtcB homolog
  • EC number
  • Alternative names
    • 3'-phosphate/5'-hydroxy nucleic acid ligase

Organism names

  • Taxonomic identifier
  • Strain
    • ALBI9_A
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Nematocera > Culicoidea > Culicidae > Anophelinae > Anopheles

Accessions

  • Primary accession
    A0A182F4X4

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Membrane
; Lipid-anchor

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Catalytic component of the tRNA-splicing ligase complex.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the PP2C family.
Belongs to the RtcB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,358
  • Mass (Da)
    149,930
  • Last updated
    2016-09-07 v1
  • Checksum
    8591D43D09FAA5CA
MVVREYNEEMKYIERLSPNSFLIKKGFQPNMNVDGVFYANSRLEKLMFEELRNACRPGMSGGFLPGVKQIANVAALPGIVGRSVGLPDIHSGYGFAIGNMAAFDMNDPTSIVSPGGVGFDINCGVRLLRTNLFEKDVTPVKEQLAQSLFDHIPVGVGSKGIIPMNAHDLEEALEMGMDWSLREGYVWAEDKEHCEEYGRMLNADPSKVSLRAKKRGLPQLGTLGAGNHYAEIQVVEEIYDKYAASKMGIEELGQICVMIHSGSRGFGHQVATDALVEMEKAMKRDKIETNDRQLACARINSPEGQNYLKAMSAAANFAWVNRSSMTFLTRQAFAKQFNTTPDDLDMHVIYDVSHNVAKMEEHMVDGRPKQLLVHRKGSTRAFPPHHPLIPVDYQLTGQPVLVGGSMGTCSFVLTGTEKGMVETFGSTCHGAGRSLSRAKSRRQLDYKDVLRDLEEKGISIRVASPKLVQEEAPDSYKDVRDVVQTCHDVGISNKAIKLRPIAPLLAVSALVPAYHLSRHFTMGVCLCKDKVEEGFVNDSSRDSYVGSGSDTGRLAGGGAGPGSNGNHVRNCSRSDRQASLADTVDALVKETLDIIGSIVDNEPETPNSMILLHDITDKPSGWIQLVKSLIRVVPLDNPMGPSVITLLLDDSPLPSKDSVLEVADMITRSIRRTPKRERNMCVILGFLAERLAGPCSISVLSDVTLGYLLGNLDEGIHPDVMLFSLIALEKFAQTSENKSTIRRKLALFPDNPLTRLERHTSSNDYTLRQVGFCAQWCLDNYFLIEGRQYSYEVADVSKVNVMLNTRDVSEYLKISADGLEARCDAYSFESVRCTYQVSSGCWYYEVLIITPGVMQIGWATKDSNFLSHEGYGIGDDAYSIAFDGCRKLIWHKAKSMQHTLHVWTGGSILGCLLDLDAREVLFSLDGVDGEVQTQLFGSGARDGFFAAASFMSFQQCRFNFGSEPFVYPPKNRPYKSFNDHAVLSEQDKAAQQYHPARYGDTMGAFLEKPITVKHNERGEGNGLRFGVGSMQGWRCEMEDAYHAKTGLGEKLEDWNYFAMFDGHAGDNVAKHCAENLLQRIVNTTEFSNNDITRAIHSGFLQQDEAMRGIPELASGADKSGTTAVCAFISREHLYIANCGDSRAVLCRNAQPVFTTQDHKPILPGEKERIQNAGGSVMVQRVNGSLAVSRALGDYDYKQGTALGQCEQLVSPEPEIFCQDREPSDEFLVLACDGVWDVMSNLEVCQFVHNRLQLSDDLVEVANQVIDTCLHKGSRDNMSIIIIAFPGAPVPSEEAQKREQALEATLRQRIEAILQQMSDVNFGDLLKELASEDIPDLPPGGGIYAKSTFVSDVFKELHP

Genome annotation databases

Similar Proteins

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