ENDA_METKA
ID ENDA_METKA Reviewed; 179 AA.
AC Q8TGZ7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=tRNA-splicing endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
DE EC=4.6.1.16 {ECO:0000255|HAMAP-Rule:MF_01833};
DE AltName: Full=tRNA-intron endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
GN Name=endA {ECO:0000255|HAMAP-Rule:MF_01833}; OrderedLocusNames=MK0341;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01833}.
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_01833};
CC -!- SUBUNIT: Homotetramer; although the tetramer contains four active
CC sites, only two participate in the cleavage. Therefore, it should be
CC considered as a dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_01833}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC short subfamily. {ECO:0000255|HAMAP-Rule:MF_01833}.
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DR EMBL; AE009439; AAM01556.1; -; Genomic_DNA.
DR PDB; 5X89; X-ray; 1.53 A; A=2-179.
DR PDBsum; 5X89; -.
DR AlphaFoldDB; Q8TGZ7; -.
DR SMR; Q8TGZ7; -.
DR STRING; 190192.MK0341; -.
DR EnsemblBacteria; AAM01556; AAM01556; MK0341.
DR KEGG; mka:MK0341; -.
DR HOGENOM; CLU_114393_0_0_2; -.
DR OMA; KGPGIDH; -.
DR Proteomes; UP000001826; Chromosome.
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_01833; EndA_short; 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; IPR016442; tRNA_splic_arch_short.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR Pfam; PF02778; tRNA_int_endo_N; 1.
DR PIRSF; PIRSF005285; tRNA_splic_archaea; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR SUPFAM; SSF55267; SSF55267; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..179
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109471"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:5X89"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5X89"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:5X89"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:5X89"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:5X89"
SQ SEQUENCE 179 AA; 20939 MW; AC84893E8167E5D5 CRC64;
MLCAGNGGKE LPRAKVFEGG SLVSKDYEDL KRRYFGTEHG NVLFLDPFET VYLTEKGEID
PETPEGEPMS VEELLSFFER RRPGFRAGYV VYRDLTERGY VVKSGFKYGG RFRVYEEDPD
REHSKYVVRV VEPDTELSTR DVLRATRLAH SVRKDFVLAV VEDVEEPRIE YVMWRWKRL
