ENDA_METBF
ID ENDA_METBF Reviewed; 350 AA.
AC Q46FK9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=tRNA-splicing endonuclease {ECO:0000255|HAMAP-Rule:MF_01834};
DE EC=4.6.1.16 {ECO:0000255|HAMAP-Rule:MF_01834};
DE AltName: Full=tRNA-intron endonuclease {ECO:0000255|HAMAP-Rule:MF_01834};
GN Name=endA {ECO:0000255|HAMAP-Rule:MF_01834}; OrderedLocusNames=Mbar_A0349;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
CC -!- FUNCTION: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at
CC the 5'- and 3'-splice sites to release the intron. The products are an
CC intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and
CC 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged
CC loops of 3 bases are separated by a stem of 4 bp (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01834};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01834}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC long subfamily. {ECO:0000255|HAMAP-Rule:MF_01834}.
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DR EMBL; CP000099; AAZ69333.1; -; Genomic_DNA.
DR RefSeq; WP_011305386.1; NC_007355.1.
DR AlphaFoldDB; Q46FK9; -.
DR SMR; Q46FK9; -.
DR STRING; 269797.Mbar_A0349; -.
DR EnsemblBacteria; AAZ69333; AAZ69333; Mbar_A0349.
DR GeneID; 3626593; -.
DR KEGG; mba:Mbar_A0349; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_791347_0_0_2; -.
DR OMA; GADFRTY; -.
DR OrthoDB; 110254at2157; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1350.10; -; 1.
DR HAMAP; MF_01834; EndA_long; 1.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR InterPro; IPR006678; tRNA_intron_Endonuc_N.
DR InterPro; IPR036740; tRNA_intron_Endonuc_N_sf.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR023516; tRNA_splic_arch_long.
DR PANTHER; PTHR21227; PTHR21227; 2.
DR Pfam; PF01974; tRNA_int_endo; 2.
DR Pfam; PF02778; tRNA_int_endo_N; 2.
DR SUPFAM; SSF53032; SSF53032; 2.
DR SUPFAM; SSF55267; SSF55267; 2.
DR TIGRFAMs; TIGR00324; endA; 2.
PE 3: Inferred from homology;
KW Lyase; tRNA processing.
FT CHAIN 1..350
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000309819"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 297
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 328
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ SEQUENCE 350 AA; 40401 MW; BC26ABA079BA2549 CRC64;
MKTQLKGDRV LAEKEAVAEF YKTGYFGRPK GEGLELSLVE AAFLLSRGKL EIELEGTMLD
FRYFFEQASL RQPNFELKYI VYKDLKERGY YVQPSAADFR VYPRGSHPGK SAARIFVHVQ
SERQLLPVKL LQDSVISAEN VHKQFILAVV DEESDLTFYE VKTAVPKGEM TEPYPAIKTD
ATFLEDRVIA WDAQASETLY KRGFYGKMLD SERLQLSLVE SLYLFSRGII TVRDRKGKVF
SFDEFIEKAS EIESFFLRKY SAYKNLRDSG HVVKTGFKFG TNFRVYRKVE SIEKIPHSEY
LVNAIPADFE FRLSVMSGAV RLANSVRKKM LFAVEKDEEI EYLDISRTKM