位置:首页 > 蛋白库 > ENDA_ARCFU
ENDA_ARCFU
ID   ENDA_ARCFU              Reviewed;         305 AA.
AC   O29362;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=AF_0900;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=10986124; DOI=10.1006/jmbi.2000.3941;
RA   Li H., Abelson J.;
RT   "Crystal structure of a dimeric archaeal splicing endonuclease.";
RL   J. Mol. Biol. 302:639-648(2000).
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.
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.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC       long subfamily. {ECO:0000255|HAMAP-Rule:MF_01834}.
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; AE000782; AAB90338.1; -; Genomic_DNA.
DR   PIR; D69362; D69362.
DR   PDB; 1R0V; X-ray; 2.00 A; A/B/C/D=1-305.
DR   PDB; 1R11; X-ray; 2.70 A; A/B=1-305.
DR   PDB; 1RLV; X-ray; 3.00 A; A/B=1-305.
DR   PDB; 2GJW; X-ray; 2.85 A; A/B/C/D=2-305.
DR   PDB; 3P1Y; X-ray; 2.05 A; A/B/C/D=1-305.
DR   PDBsum; 1R0V; -.
DR   PDBsum; 1R11; -.
DR   PDBsum; 1RLV; -.
DR   PDBsum; 2GJW; -.
DR   PDBsum; 3P1Y; -.
DR   AlphaFoldDB; O29362; -.
DR   SMR; O29362; -.
DR   STRING; 224325.AF_0900; -.
DR   EnsemblBacteria; AAB90338; AAB90338; AF_0900.
DR   KEGG; afu:AF_0900; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_791347_0_0_2; -.
DR   OMA; GADFRTY; -.
DR   PhylomeDB; O29362; -.
DR   BRENDA; 4.6.1.16; 414.
DR   EvolutionaryTrace; O29362; -.
DR   Proteomes; UP000002199; 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_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; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   Pfam; PF02778; tRNA_int_endo_N; 1.
DR   SUPFAM; SSF53032; SSF53032; 2.
DR   SUPFAM; SSF55267; SSF55267; 2.
DR   TIGRFAMs; TIGR00324; endA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..305
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000109484"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   HELIX           13..18
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   HELIX           32..40
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   HELIX           49..59
FT                   /evidence="ECO:0007829|PDB:3P1Y"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:2GJW"
FT   HELIX           63..75
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          86..97
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           104..110
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           183..191
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           216..228
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          241..247
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           252..257
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          259..264
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   HELIX           272..284
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          288..293
FT                   /evidence="ECO:0007829|PDB:1R0V"
FT   STRAND          296..303
FT                   /evidence="ECO:0007829|PDB:1R0V"
SQ   SEQUENCE   305 AA;  35959 MW;  DC0B5A5DEBD99E35 CRC64;
     MIGGDFAVVK AKKSLERRGF GVKRGDKIYL HPLEVVYLQI KGIESFGELE DVLSWAESRM
     EDFSTYYFVY EDLRDRGNKV KIQGEFLLTK KPYLPISERK TIRMEEIAEK ARNFDELRLA
     VVDEESEITY FRVYEPDMMG EQKEELPEIA GILSDEYVIT KQTEIFSRYF YGSEKGDLVT
     LSLIESLYLL DLGKLNLLNA DREELVKRAR EVERNFDRRY EVYRNLKERG FVVKTGFKFG
     SEFRVYRKVE SVDDLPHSEY LVDIADSREI RLIDLARAVR LAQNVRKRMV FAYGKNYLCF
     ERVKV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025