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RTCB_BRUMA
ID   RTCB_BRUMA              Reviewed;         505 AA.
AC   A8QC60;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=RNA-splicing ligase RtcB homolog {ECO:0000255|HAMAP-Rule:MF_03144};
DE            EC=6.5.1.8 {ECO:0000255|HAMAP-Rule:MF_03144};
DE   AltName: Full=3'-phosphate/5'-hydroxy nucleic acid ligase {ECO:0000255|HAMAP-Rule:MF_03144};
GN   ORFNames=Bm1_49220;
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17885136; DOI=10.1126/science.1145406;
RA   Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA   Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA   Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA   Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA   Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA   Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA   Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA   Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA   McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA   Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA   Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA   Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA   Blaxter M.L., Scott A.L.;
RT   "Draft genome of the filarial nematode parasite Brugia malayi.";
RL   Science 317:1756-1760(2007).
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. {ECO:0000255|HAMAP-Rule:MF_03144}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_03144};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_03144};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03144};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03144};
CC   -!- SUBUNIT: Catalytic component of the tRNA-splicing ligase complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03144}.
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       {ECO:0000255|HAMAP-Rule:MF_03144}.
CC   -!- SIMILARITY: Belongs to the RtcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_03144}.
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DR   EMBL; DS239429; EDP29990.1; -; Genomic_DNA.
DR   RefSeq; XP_001901310.1; XM_001901275.1.
DR   AlphaFoldDB; A8QC60; -.
DR   SMR; A8QC60; -.
DR   STRING; 6279.A8QC60; -.
DR   EnsemblMetazoa; Bm3402.1; Bm3402.1; WBGene00223663.
DR   GeneID; 6104729; -.
DR   KEGG; bmy:BM_BM3402; -.
DR   WBParaSite; Bm3402.1; Bm3402.1; WBGene00223663.
DR   CTD; 6104729; -.
DR   WormBase; Bm3402; BM21216; WBGene00223663; -.
DR   HOGENOM; CLU_022279_0_0_1; -.
DR   InParanoid; A8QC60; -.
DR   OrthoDB; 394775at2759; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:0072669; C:tRNA-splicing ligase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1860.10; -; 1.
DR   HAMAP; MF_03144; RtcB_euk; 1.
DR   InterPro; IPR001233; RtcB.
DR   InterPro; IPR036025; RtcB-like_sf.
DR   InterPro; IPR027513; RtcB_euk.
DR   PANTHER; PTHR11118; PTHR11118; 1.
DR   Pfam; PF01139; RtcB; 1.
DR   SUPFAM; SSF103365; SSF103365; 1.
DR   PROSITE; PS01288; UPF0027; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Ligase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome; tRNA processing.
FT   CHAIN           1..505
FT                   /note="RNA-splicing ligase RtcB homolog"
FT                   /id="PRO_0000407228"
FT   ACT_SITE        428
FT                   /note="GMP-histidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         226..230
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         227
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         353..354
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         353
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         402..405
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         409
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         428..431
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
FT   BINDING         504
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03144"
SQ   SEQUENCE   505 AA;  55470 MW;  59137D092BA28819 CRC64;
     MPRTYDEECS YIERITDVVY RIKKGFVPNM NVEGRFYVNT ALEKLMFEEL RNACRLDGIG
     GFLPAVRQIG NVAALPAIVN ASIGLPDIHS GYGFAIGNIA AFDVSDPDAV VSPGGVGFDI
     NCGVRLIRTN LSEKDVQPVK EQLAQSLFDH IPVGVGSKGI IPIGAQQFEE CLEMGMDWTL
     REGYSWAEDK EHCEEYGRML QADAAKVSPR AKKRGLPQLG TLGAGNHYGE VQVIDEIYDE
     YAASRMGIDR LGQVCIMIHC GSRGLGHQVA TDSLVVMEKA MKRDNIIVND RQLACARINS
     MEGQDYLKGM AAAANFAWVN RSCMTFCARQ AFAKVFNTSP DDLDMHVIYD VSHNIAKIEE
     HLINGRPKQL CVHRKGSTRA FPPHHPLIPV DYQLTGQPVL IGGTMGTCSY VLTGTEQGMN
     ETFATTCHGA GRALSRAKSR RNIDFQEVLN KMQAMGISIR VASPKLVMEE APESYKNVTD
     VVNTCHEAGI SKKSVKLRPI AVIKG
 
 
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