[GTOP] [HELP] [ORGANISMS] [SEARCH] [SUMMARY]
Ralstonia metallidurans CH34 (rmet0)
Gene : ABF09019.1
DDBJ      :             glutamyl-tRNA synthetase
Swiss-Prot:SYE_RALME    RecName: Full=Glutamyl-tRNA synthetase;         EC=6.1.1.17;AltName: Full=Glutamate--tRNA ligase;         Short=GluRS;

Homologs  Archaea  56/68 : Bacteria  908/915 : Eukaryota  186/199 : Viruses  0/175   --->[See Alignment]
a.97.1c.26.1
:465 amino acids
:SECSTR
:PSIPRED
:DISOPRED
:BLT:PDB   5->370 2cfoB PDBj 2e-78 42.6 %
:RPS:PDB   5->465 2cfoB PDBj 6e-67 35.6 %
:RPS:SCOP  5->304 1g59A2  c.26.1.1 * 2e-96 38.1 %
:RPS:SCOP  305->462 1g59A1  a.97.1.1 * 1e-28 30.8 %
:HMM:SCOP  4->304 1j09A2 c.26.1.1 * 2.1e-103 48.1 %
:HMM:SCOP  305->467 1j09A1 a.97.1.1 * 1.9e-38 39.8 %
:RPS:PFM   5->310 PF00749 * tRNA-synt_1c 3e-80 50.8 %
:HMM:PFM   5->311 PF00749 * tRNA-synt_1c 1.6e-100 42.0 307/314  
:BLT:SWISS 1->465 SYE_RALME 0.0 100.0 %
:PROS 11->22|PS00178|AA_TRNA_LIGASE_I
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID ABF09019.1 GT:GENE ABF09019.1 GT:PRODUCT glutamyl-tRNA synthetase GT:DATABASE GIB00349CH01 GT:ORG rmet0 GB:ACCESSION GIB00349CH01 GB:LOCATION complement(2330543..2331940) GB:FROM 2330543 GB:TO 2331940 GB:DIRECTION - GB:PRODUCT glutamyl-tRNA synthetase GB:PROTEIN_ID ABF09019.1 GB:DB_XREF GI:93354930 InterPro:IPR000924 InterPro:IPR001412 InterPro:IPR004527 LENGTH 465 SQ:AASEQ MTQRVRTRFAPSPTGFIHLGNIRSAFYPWAFARRMKGDFILRIEDTDVERSTDVAVDVILESMAWLDLDIDEGPFYQMQRMDRYREVVQQMLDNELAYHCYMSTEELDALREAQRAAGEKPRYNGFWRPEPGKVLPEPPAGVQPVVRFKNPIGGSVVWDDAVKGRIEISNDELDDLVIARPDGTPTYNFCVVVDDLDMKITHVIRGDDHVNNTPRQINIIRALGGEVPVYAHLPTVLNEQGEKMSKRHGALPVTGYRDEGYLPEAVLNYLARLGWAHGDAEIFSREQFVEWFDLEHLGKSPAQYNPEKLAWLNNHYIKVGDNTRLADLTRPFIEALGGKVEGANLVDVIALVKDRANTLKEVAQTAMLFYRGEPQADAALKAEHLTDEIRPALQALATQLAALPEWKREAISAAFKAVLAEFGLKMPKLAMPVRLLVAGQLQTPSIDAVLELFGRDTVLRRLAAA GT:EXON 1|1-465:0| SW:ID SYE_RALME SW:DE RecName: Full=Glutamyl-tRNA synthetase; EC=6.1.1.17;AltName: Full=Glutamate--tRNA ligase; Short=GluRS; SW:GN Name=gltX; OrderedLocusNames=Rmet_2140; SW:KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;Ligase; Nucleotide-binding; Protein biosynthesis. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->465|SYE_RALME|0.0|100.0|465/465| GO:SWS:NREP 6 GO:SWS GO:0004812|"GO:aminoacyl-tRNA ligase activity"|Aminoacyl-tRNA synthetase| GO:SWS GO:0005524|"GO:ATP binding"|ATP-binding| GO:SWS GO:0005737|"GO:cytoplasm"|Cytoplasm| GO:SWS GO:0016874|"GO:ligase activity"|Ligase| GO:SWS GO:0000166|"GO:nucleotide binding"|Nucleotide-binding| GO:SWS GO:0006412|"GO:translation"|Protein biosynthesis| PROS 11->22|PS00178|AA_TRNA_LIGASE_I|PDOC00161| SEG 392->403|alqalatqlaal| BL:PDB:NREP 1 BL:PDB:REP 5->370|2cfoB|2e-78|42.6|366/487| RP:PDB:NREP 1 RP:PDB:REP 5->465|2cfoB|6e-67|35.6|461/487| RP:PFM:NREP 1 RP:PFM:REP 5->310|PF00749|3e-80|50.8|305/309|tRNA-synt_1c| HM:PFM:NREP 1 HM:PFM:REP 5->311|PF00749|1.6e-100|42.0|307/314|tRNA-synt_1c| GO:PFM:NREP 6 GO:PFM GO:0000166|"GO:nucleotide binding"|PF00749|IPR020058| GO:PFM GO:0005524|"GO:ATP binding"|PF00749|IPR020058| GO:PFM GO:0005737|"GO:cytoplasm"|PF00749|IPR020058| GO:PFM GO:0006412|"GO:translation"|PF00749|IPR020058| GO:PFM GO:0016876|"GO:ligase activity, forming aminoacyl-tRNA and related compounds"|PF00749|IPR020058| GO:PFM GO:0043039|"GO:tRNA aminoacylation"|PF00749|IPR020058| RP:SCP:NREP 2 RP:SCP:REP 5->304|1g59A2|2e-96|38.1|294/305|c.26.1.1| RP:SCP:REP 305->462|1g59A1|1e-28|30.8|156/163|a.97.1.1| HM:SCP:REP 4->304|1j09A2|2.1e-103|48.1|295/0|c.26.1.1|1/1|Nucleotidylyl transferase| HM:SCP:REP 305->467|1j09A1|1.9e-38|39.8|161/0|a.97.1.1|1/1|An anticodon-binding domain of class I aminoacyl-tRNA synthetases| OP:NHOMO 1968 OP:NHOMOORG 1150 OP:PATTERN 11-1111-111111111-111111-11-1-1-1111111111111--1-111111111111111-1-1 332122222222222-111-12111211111122223222111111211111222222111112111111112222112222211111111111111-11111111111111111111111111111111111111111111111111111111122222222111111111221111211213331111131111111111111111121111111111111111111111111111111111111111111112111111111111111111111111111111111111111111111111111212111111111111142112111111111112221112212112122122222321112225111212222222222332332223223333333333333122322423333122222221221223223332333333333333333333332332222222232222222222222222222213333233323322223222222232222222233222222222222223222222323333222222222323332112122433323332223222222333332322222222222222222222222222332222323223233333333333332333331-1233311111122222222222222222-22222222222222222222222222122222222222222223222222231222222222222111222222222232323222222222222221222322222323222222222222222222222222222222222222332332222222222111122211111111111111111111111-111-1111111111111112222222222123 1111221-3-1---111211122111122111111111111112221111221122122-11232112121222321-1123331233-14113221112131111-1322131111111111111-313A111121111111-1-111111121111211211111111211-12111T2321212222112111114 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 465 STR:RPRED 100.0 SQ:SECSTR cccccEEEEcccccccccHHHHHHHHHHHHHHHHTTcEEEEEEccccTTTccHHHHHHHHHHHHHHTccccEEEEEGGGcHHHHHHHHHHHHHHTcEEEEcccHHHHHHHHHHHHHTTcccccccTTTTccHHHHHHHHTTcccEEEEcccTTcEEEEEETTTEEEEEEGGGGcccEEEEccccccHHHHHHHHHHHTTccEEEEEGGGTTHHHHHHHHHHHTTccccEEEEEccEEcTTcccccTTcccccHHHHHHTTccHHHHHHHHHHTTccccTTccccHHHHHHHccGGGcccccEEccHHHHHHHHHHHHTTccHHHHHHHHHHHHHHTTccccHHHHHHHHHHHGGGcccTTHHHHHHHHHHcccccccHHHHHHHTcTTHHHHHHHHHHHccccccccHHHHHHHHHHHHHHHTccHHHHHHHHHHHHHcccccccHHHHHHHHHHTcHHHHHHHH DISOP:02AL 1-2,108-125,464-466| PSIPRED cccccEEEccccccccccHHHHHHHHHHHHHHHHHccEEEEEEcccccccccHHHHHHHHHHHHHccccccccEEEcccHHHHHHHHHHHHHHccccccccccHHHHHHHHHHHHHcccccccccccccccHHHHHHHHcccccEEEEEccccccEEEcccccccEEcccccccccEEEEccccHHHHcHHHHHHHHccccEEEEcccccccHHHHHHHHHHcccccccEEEEEEEEcccccccccccccccHHHHHHccccHHHHHHHHHHccccccccccccHHHHHHHccHHHcccccccccHHHHHHHHHHHHHHccHHHHHHHHHHHHHHHcccccHHHHHHHHHHHHcccccHHHHHHHHHHHccccccccHHHHHHHccHHHHHHHHHHHHHHHccccccHHHHHHHHHHHHHHHcccHHHHHHHHHHHHHcccccccHHHHHHHHcHHHHHHHHHcc //