|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-557 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1082.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 1 MKEAPESLNFIEQIIEEDLANGLPQeQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVD 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 81 AIKNDIEWLGFQWATE-CYSSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTASPFRDTPVEENLAIFEK 159
Cdd:PRK05347 83 SIKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 160 MKNGEYEAGTYVLRAKIDMASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHREL 239
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 240 YDWFLDQIydKSKLRPKQREFARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISK 319
Cdd:PRK05347 243 YDWVLDNL--PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 320 RDGVTDVSLLEFCIREDLNKTATRVMGVIDPVKLVITNYPEGKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKEDA 399
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 400 GNKFFRLTIGNEVRLKNAYIIKGETVVKDADGNITEIHCTADLDSKSGSGTEAsmRKVKGTLHWVSIKHAIKAEVREYDR 479
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADG--RKVKGTIHWVSAAHAVPAEVRLYDR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995471327 480 LFLDEAPDshEEKGFMEFVNPNSLnIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDKDSSPSHLIFNKTVGLKDTWAK 557
Cdd:PRK05347 479 LFTVPNPA--AGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 686.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 28 LRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATEC-YSSDYFQQL 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 107 YDWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTASPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 187 DPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYdkSKLRPKQREFARRNLS 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH--IFPRPAQYEFSRLNLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 267 YTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATRVMG 346
Cdd:TIGR00440 239 GTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 347 VIDPVKLVITNYpEGKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKEDAGNKFFRLTIGNEVRLKNAYIIKGETVV 426
Cdd:TIGR00440 319 VIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 427 KDADGNITEIHCTADLDSKSGSGTEAsmRKVKGTLHWVSIKHAIKAEVREYDRLFLDEAPdSHEEkGFMEFVNPNSLnIV 506
Cdd:TIGR00440 398 KDAAGKITTIFCTYDNKTLGKEPADG--RKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPD-DFLSVINPESL-VI 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1995471327 507 KEAYLEPYLMNAQLDDKYQFQRLGYFTLD-KDSSPSHLIFNKTVGLKDTW 555
Cdd:TIGR00440 473 KQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
31-343 |
2.48e-132 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 389.30 E-value: 2.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWA 110
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 111 IELIKQGKAYVdgqsseaiaeqkgtpttpgtaspfrdtpveenlaifekmkngeyeagtyvlrakidmaspnmlmrdpll 190
Cdd:cd00807 85 EQLIKKGKAYV--------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 191 yriinkaHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydkSKLRPKQREFARRNLSYTVM 270
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL---RLYRPHQWEFSRLNLTYTVM 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1995471327 271 SKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATR 343
Cdd:cd00807 166 SKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-338 |
8.32e-119 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 357.40 E-value: 8.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 27 QLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATE-CYSSDYFQQ 105
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 106 LYDWAIELIKQGKAYVDGQSSEAIAEQKGtpTTPGTASPFRDTPVEENLAIF-EKMKNGEYEAGTYVLRAKIDMASPnML 184
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 185 MRDPLLYRIIN---KAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydKSKLRPKQREFA 261
Cdd:pfam00749 158 FRDPVRGRIKFtpqEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDAL--GWEPPPFIHEYL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995471327 262 RRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVS-LLEFCIREDLN 338
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSkSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-532 |
4.09e-110 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 340.62 E-value: 4.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 29 RFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATE-CYSSDYFQQLY 107
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 108 DWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTA----SPFRDTPVEENlaifEKMK-NGEyeagTYVLRAKI------ 176
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERMLaAGE----PPVLRFKIpeegvv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 177 --DMAS-----PNMLMRDPLLYRiinkahhRTGnewciYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYD 249
Cdd:COG0008 158 fdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 250 KsklRPkqrEFARRNLSY----TVMSKRKllelvqtKTVsgwddprmpTISGLRRRGYTPASIRKFSEVSGISKRDGVT- 324
Cdd:COG0008 226 E---PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEi 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 325 -DVSLLEFCIreDLNKTaTRVMGVIDPVKLVITNYPEGKE---ELLIAENNPEDADSGTHE-----VPFSRE-------- 387
Cdd:COG0008 284 fSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 388 ------LYIEREDfkEDAGNKffRLTIgNEVRlknayiikgeTVVKDADGNITEIhctADLDSKSgsgteasmrkVKGTL 461
Cdd:COG0008 361 aelarfFFIERED--EKAAKK--RLAP-EEVR----------KVLKAALEVLEAV---ETWDPET----------VKGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1995471327 462 HWVSIKHAIKaevreyDRLFldeapdsheekgFMEFVnpnslNIVKEAYLEPYL---MNAQLDDKYqFQRLGYF 532
Cdd:COG0008 413 HWVSAEAGVK------DGLL------------FMPLR-----VALTGRTVEPSLfdvLELLGKERV-FERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-557 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1082.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 1 MKEAPESLNFIEQIIEEDLANGLPQeQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVD 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHT-RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 81 AIKNDIEWLGFQWATE-CYSSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTASPFRDTPVEENLAIFEK 159
Cdd:PRK05347 83 SIKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 160 MKNGEYEAGTYVLRAKIDMASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHREL 239
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 240 YDWFLDQIydKSKLRPKQREFARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISK 319
Cdd:PRK05347 243 YDWVLDNL--PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 320 RDGVTDVSLLEFCIREDLNKTATRVMGVIDPVKLVITNYPEGKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKEDA 399
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 400 GNKFFRLTIGNEVRLKNAYIIKGETVVKDADGNITEIHCTADLDSKSGSGTEAsmRKVKGTLHWVSIKHAIKAEVREYDR 479
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADG--RKVKGTIHWVSAAHAVPAEVRLYDR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995471327 480 LFLDEAPDshEEKGFMEFVNPNSLnIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDKDSSPSHLIFNKTVGLKDTWAK 557
Cdd:PRK05347 479 LFTVPNPA--AGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-588 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 809.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 1 MKEAP-----ESLNFIEQIIEEDLANGlPQEQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEE 75
Cdd:PRK14703 1 MSDAPrprmlVSPNFITEIIEEDLEAG-RYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 76 QEYVDAIKNDIEWLGFQW-ATECYSSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTASPFRDTPVEENL 154
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWgEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 155 AIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFK 234
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 235 SHRELYDWFLDQIYDKSKlRPKQREFARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEV 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGPWPP-RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 315 SGISKRDGVTDVSLLEFCIREDLNKTATRVMGVIDPVKLVITNYPEGKEELLIAENNPEDADS-GTHEVPFSRELYIERE 393
Cdd:PRK14703 319 IGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 394 DFKEDAGNKFFRLTIGNEVRLKNAYIIKGETVVKDADGNITEIHCTADLDSKSGSGTEasmRKVKGTLHWVSIKHAIKAE 473
Cdd:PRK14703 399 DFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTG---RKAAGVIHWVSAKHALPAE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 474 VREYDRLFLDEAPDShEEKGFMEFVNPNSLNiVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDK-DSSPSHLIFNKTVGLK 552
Cdd:PRK14703 476 VRLYDRLFKVPQPEA-ADEDFLEFLNPDSLR-VAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLK 553
|
570 580 590
....*....|....*....|....*....|....*.
gi 1995471327 553 DTWAKQQpdNKPQQQKTAKNPNQGQGQRSAINEIQK 588
Cdd:PRK14703 554 DTWGARA--REAAREKRAAAPKKTAKPRRSKAEARA 587
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 686.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 28 LRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATEC-YSSDYFQQL 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 107 YDWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTASPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 187 DPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYdkSKLRPKQREFARRNLS 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH--IFPRPAQYEFSRLNLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 267 YTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATRVMG 346
Cdd:TIGR00440 239 GTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 347 VIDPVKLVITNYpEGKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKEDAGNKFFRLTIGNEVRLKNAYIIKGETVV 426
Cdd:TIGR00440 319 VIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 427 KDADGNITEIHCTADLDSKSGSGTEAsmRKVKGTLHWVSIKHAIKAEVREYDRLFLDEAPdSHEEkGFMEFVNPNSLnIV 506
Cdd:TIGR00440 398 KDAAGKITTIFCTYDNKTLGKEPADG--RKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPD-DFLSVINPESL-VI 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1995471327 507 KEAYLEPYLMNAQLDDKYQFQRLGYFTLD-KDSSPSHLIFNKTVGLKDTW 555
Cdd:TIGR00440 473 KQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
31-560 |
8.70e-177 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 523.17 E-value: 8.70e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWA 110
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 111 IELIKQGKAYVDGQSSEAIAE--QKGTPttpgtaSPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRDP 188
Cdd:PLN02859 348 VELIRRGHAYVDHQTPEEIKEyrEKKMN------SPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 189 LLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydkSKLRPKQREFARRNLSYT 268
Cdd:PLN02859 422 IAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL---GLYQPYVWEYSRLNVTNT 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 269 VMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDG-VTDVSLLEFCIREDLNKTATRVMGV 347
Cdd:PLN02859 499 VMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAPRTMVV 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 348 IDPVKLVITNYPEGKEELLIAE---NNPEDADSGTHEVPFSRELYIEREDFKEDAGNKFFRLTIGNEVRLKNAYIIK-GE 423
Cdd:PLN02859 579 LHPLKVVITNLESGEVIELDAKrwpDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKcTD 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 424 TVVKDADGNITEIHCTADLDSKSgsgteasmrKVKGTLHWVSI----KHAIKAEVREYDRLFLDEAPDSHEEkgFMEFVN 499
Cdd:PLN02859 659 VVLADDNETVVEIRAEYDPEKKT---------KPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENPAELED--WLEDLN 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1995471327 500 PNSLNIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDKDSSPSHLIFNKTVGLKDTWAKQQP 560
Cdd:PLN02859 728 PQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
30-553 |
8.03e-150 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 446.74 E-value: 8.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 30 FRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQ--WATecYSSDYFQQLY 107
Cdd:PTZ00437 54 FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdWVT--FSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 108 DWAIELIKQGKAYVDGQSSEAIAEQKGTPTTpgtaSPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRD 187
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQREQRED----SPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 188 PLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydkSKLRPKQREFARRNLSY 267
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEEL---NLWRPHVWEFSRLNVTG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 268 TVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATRVMGV 347
Cdd:PTZ00437 285 SLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 348 IDPVKLVITNYpEGKEELLiAENNPEDADSGTHEVPFSRELYIEREDFK-EDAGNKFFRLTIGNE-VRLKNAYIIKGETV 425
Cdd:PTZ00437 365 IDPIKVVVDNW-KGEREFE-CPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRvVGLKYSGNVVCKGF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 426 VKDADGNITEIHCTADLDSKSgsgteasmrKVKGTLHWVSIKHAIKAEVREYDRLFLDE--APDSHeekgFMEFVNPNSl 503
Cdd:PTZ00437 443 EVDAAGQPSVIHVDIDFERKD---------KPKTNISWVSATACTPVEVRLYNALLKDDraAIDPE----FLKFIDEDS- 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1995471327 504 NIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDKDSSPSHLIFNKTVGLKD 553
Cdd:PTZ00437 509 EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
31-343 |
2.48e-132 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 389.30 E-value: 2.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWA 110
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 111 IELIKQGKAYVdgqsseaiaeqkgtpttpgtaspfrdtpveenlaifekmkngeyeagtyvlrakidmaspnmlmrdpll 190
Cdd:cd00807 85 EQLIKKGKAYV--------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 191 yriinkaHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydkSKLRPKQREFARRNLSYTVM 270
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL---RLYRPHQWEFSRLNLTYTVM 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1995471327 271 SKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATR 343
Cdd:cd00807 166 SKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-338 |
8.32e-119 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 357.40 E-value: 8.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 27 QLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATE-CYSSDYFQQ 105
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 106 LYDWAIELIKQGKAYVDGQSSEAIAEQKGtpTTPGTASPFRDTPVEENLAIF-EKMKNGEYEAGTYVLRAKIDMASPnML 184
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 185 MRDPLLYRIIN---KAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydKSKLRPKQREFA 261
Cdd:pfam00749 158 FRDPVRGRIKFtpqEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDAL--GWEPPPFIHEYL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995471327 262 RRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVS-LLEFCIREDLN 338
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSkSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-532 |
4.09e-110 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 340.62 E-value: 4.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 29 RFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATE-CYSSDYFQQLY 107
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 108 DWAIELIKQGKAYVDGQSSEAIAEQKGTPTTPGTA----SPFRDTPVEENlaifEKMK-NGEyeagTYVLRAKI------ 176
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERMLaAGE----PPVLRFKIpeegvv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 177 --DMAS-----PNMLMRDPLLYRiinkahhRTGnewciYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYD 249
Cdd:COG0008 158 fdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 250 KsklRPkqrEFARRNLSY----TVMSKRKllelvqtKTVsgwddprmpTISGLRRRGYTPASIRKFSEVSGISKRDGVT- 324
Cdd:COG0008 226 E---PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEi 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 325 -DVSLLEFCIreDLNKTaTRVMGVIDPVKLVITNYPEGKE---ELLIAENNPEDADSGTHE-----VPFSRE-------- 387
Cdd:COG0008 284 fSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 388 ------LYIEREDfkEDAGNKffRLTIgNEVRlknayiikgeTVVKDADGNITEIhctADLDSKSgsgteasmrkVKGTL 461
Cdd:COG0008 361 aelarfFFIERED--EKAAKK--RLAP-EEVR----------KVLKAALEVLEAV---ETWDPET----------VKGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1995471327 462 HWVSIKHAIKaevreyDRLFldeapdsheekgFMEFVnpnslNIVKEAYLEPYL---MNAQLDDKYqFQRLGYF 532
Cdd:COG0008 413 HWVSAEAGVK------DGLL------------FMPLR-----VALTGRTVEPSLfdvLELLGKERV-FERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
31-535 |
7.12e-98 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 316.67 E-value: 7.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWA 110
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 111 IELIKQGKAYVDGQSSEAIAEQKGTpttpGTASPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRDPLL 190
Cdd:PLN02907 297 EKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVY 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 191 YRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydksKLRPKQ-REFARRNLSYTV 269
Cdd:PLN02907 373 YRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDM----GLRKVHiWEFSRLNFVYTL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 270 MSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKrdgvtDVSLLEFCIREDLNKTatrvmgVID 349
Cdd:PLN02907 449 LSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLMEWDKLWTINKK------IID 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 350 P-------------VKLVITNYPEgKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKEdagnkffrLTIGNEVRLK- 415
Cdd:PLN02907 518 PvcprhtavlkegrVLLTLTDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMd 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 416 --NAYIIKgetVVKDADGNITEIHCTADLdsksgsgtEASMRKVKGTLHWV-SIKHAIKAEVREYDRLFLDEAPDshEEK 492
Cdd:PLN02907 589 wgNAIIKE---ITKDEGGAVTALSGELHL--------EGSVKTTKLKLTWLpDTNELVPLSLVEFDYLITKKKLE--EDD 655
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1995471327 493 GFMEFVNPNSlNIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLD 535
Cdd:PLN02907 656 NFLDVLNPCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-536 |
1.19e-93 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 300.59 E-value: 1.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 1 MKEAPESLNfIEQIIEEDLANGLPQ------EQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKE 74
Cdd:TIGR00463 62 QKELMKRLG-LDIKKKEKKRKGLRElpgakmGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 75 EQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKGTpttpGTASPFRDTPVEENL 154
Cdd:TIGR00463 141 DPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 155 AIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFK 234
Cdd:TIGR00463 217 ERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 235 SHRE--LYDW-FLDQIYDKSklrpKQREFARRNLSYTVMSKRKLLELVQtKTVSGWDDPRMPTISGLRRRGYTPASIRKF 311
Cdd:TIGR00463 297 DNRRkqEYIYrYFGWEPPEF----IHWGRLKIDDVRALSTSSARKGILR-GEYSGWDDPRLPTLRAIRRRGIRPEAIRKF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 312 SEVSGISKRDGVTDVSLLEFCIREDLNKTATRVMGVIDPVKLVITNYPEGKEELLiaENNPEDADSGTHEVPFSRELYIE 391
Cdd:TIGR00463 372 MLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVER--PLHPDHPEIGERVLILRGEIYVP 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 392 REDFKEDAgnkffrltigNEVRLKNAyiikGETVVkdaDGNITEIHctadldsksGSGTEASMRKVKGTLHWVSIKHAIK 471
Cdd:TIGR00463 450 KDDLEEGV----------EPVRLMDA----VNVIY---SKKELRYH---------SEGLEGARKLGKSIIHWLPAKDAVK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995471327 472 AEVREydrlfldeaPDSHEEKGFMEfvnpnslniVKEAYLEpylmnaqLDDKYQFQRLGYFTLDK 536
Cdd:TIGR00463 504 VKVIM---------PDASIVEGVIE---------ADASELE-------VGDVVQFERFGFARLDS 543
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-536 |
7.97e-91 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 292.30 E-value: 7.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 19 LANGLPQeQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECY 98
Cdd:PLN03233 4 LEGAIAG-QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 99 SSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKgtptTPGTASPFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDM 178
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 179 ASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYDKsklRPKQR 258
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR---RPRIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 259 EFARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRdgVTDVSLLEFCI--RED 336
Cdd:PLN03233 236 AFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRR--VVNLDWAKFWAenKKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 337 LNKTATRVMGV--IDPVKLVITNYPEGKEELLIAEN-NPEDADSGTHEVPFSRELYIEREDFKEdagnkffrLTIGNEVR 413
Cdd:PLN03233 314 IDKRAKRFMAIdkADHTALTVTNADEEADFAFSETDcHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 414 LKNAYIIKgetvVKDADGNItEIHCTADLDSKsgsgteASMRKvkgtLHWVS-IKHAIKAEVREYDRLFLDEAPDshEEK 492
Cdd:PLN03233 386 LLRWGVIE----ISKIDGDL-EGHFIPDGDFK------AAKKK----ISWIAdVSDNIPVVLSEFDNLIIKEKLE--EDD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1995471327 493 GFMEFVNPNSLNIVkEAYLEPYLMNAQLDDKYQFQRLGYFTLDK 536
Cdd:PLN03233 449 KFEDFINPDTLAET-DVIGDAGLKTLKEHDIIQLERRGFYRVDR 491
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-536 |
1.68e-89 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 289.83 E-value: 1.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 2 KEAPESLNFIEQIIEEDlaNGLPQ------EQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPA--K 73
Cdd:PRK04156 72 ELAPELLEEEEEKKEEK--KGLPPlpnaekGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 74 EEQEYVDAIKNDIEWLGFQWATECYSSDYFQQLYDWAIELIKQGKAYVDGQSSEAIAEQKGTpttpGTASPFRDTPVEEN 153
Cdd:PRK04156 150 PDPEAYDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEEN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 154 LAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRDPLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHslcTLEF 233
Cdd:PRK04156 226 LELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 234 KSHRE-------LYDWFlDQIYdksklrPKQREFARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPA 306
Cdd:PRK04156 303 KDHIDntekqryIYDYF-GWEY------PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 307 SIRKFSEVSGIskrdGVTDVSL----LEFCIREDLNKTATRVMGVIDPVKLVITNYPEGKEELLIaenNPEDADSGTHEV 382
Cdd:PRK04156 376 AIRELIIEVGV----KETDATIswenLYAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAKIPL---HPDRPERGEREI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 383 PFSRELYIEREDFKEdagnkffrltIGNEVRLKNAYIIKgetvVKDADGNITEIHcTADLDsksgsgtEASMRKVKgTLH 462
Cdd:PRK04156 449 PVGGKVYVSSDDLEA----------EGKMVRLMDLFNVE----ITGVSVDKARYH-SDDLE-------EARKNKAP-IIQ 505
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1995471327 463 WVSIKHAIKAEVREydrlfldeaPDSHEEKGfmefvnpnslnivkeaYLEPYLMNAQLDDKYQFQRLGYFTLDK 536
Cdd:PRK04156 506 WVPEDESVPVRVLK---------PDGGDIEG----------------LAEPDVADLEVDDIVQFERFGFVRIDS 554
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
31-544 |
2.32e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 283.01 E-value: 2.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWAT-ECYSSDYFQQLYDW 109
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVgPTYSSDYMDLMYEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 110 AIELIKQGKAYVDGQSSEAIAEQK--GTPTTpgtaspFRDTPVEENLAIFEKMKNGEYEAGTYVLRAKIDMASPNMLMRD 187
Cdd:PTZ00402 136 AEELIKKGLAYCDKTPREEMQKCRfdGVPTK------YRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAMRD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 188 PLLYRIINKAHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIYDKsklRPKQREFARRNLSY 267
Cdd:PTZ00402 210 PVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR---KPIVEDFSRLNMEY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 268 TVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKTATRVMGV 347
Cdd:PTZ00402 287 SVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 348 IDPVKLVITNYPEG---KEELLIAENNPedaDSGTHEVPFSRELYIEREDFKedagnkffRLTIGNEVRLK---NAYIIK 421
Cdd:PTZ00402 367 SNTLKVRCTVEGQIhleACEKLLHKKVP---DMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLMdwgNAYIKN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 422 GETvvKDADGNITEIHCTADLdsksgsgtEASMRKVKGTLHWVSIK-HAIKAEVREYDRLFLDEAPDSHEEkgFMEFVNP 500
Cdd:PTZ00402 436 IRR--SGEDALITDADIVLHL--------EGDVKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPDPEES--IDDIIAP 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1995471327 501 NSlNIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLDKDSSPSHLI 544
Cdd:PTZ00402 504 VT-KYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
341-535 |
1.87e-72 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 231.78 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 341 ATRVMGVIDPVKLVITNYPEGKEELLIAENNPEDADSGTHEVPFSRELYIEREDFKedagnkffRLTIGNEVRLKNAYII 420
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 421 KGETVVKDADGNITEIHCTADLDSKSGSgteasmRKVKG-TLHWVSIKHAIKAEVREYDRLFLDEapdshEEKGFmeFVN 499
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA------RKVKGkIIHWVSASDAVPAEVRLYDRLFKDE-----DDADF--LLN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1995471327 500 PNSLNIVKEAYLEPYLMNAQLDDKYQFQRLGYFTLD 535
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
29-353 |
2.38e-49 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 172.27 E-value: 2.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 29 RFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATECY-SSDYFQQLY 107
Cdd:cd00418 3 VTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYrQSDRFDLYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 108 DWAIELIKQGkayvdgqsseaiaeqkgtpttpgtaspfrdtpveenlaifekmkngeyeagtyvlrakidmaspnmlmrd 187
Cdd:cd00418 83 AYAEELIKKG---------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 188 pllyriinkahhrtgnewcIYPMYDWAHGESDYIEQISHSLCTLEFKSHRELYDWFLDQIydkSKLRPKQREFARRNLSY 267
Cdd:cd00418 93 -------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEAL---GWEPPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 268 -TVMSKRKLlelvqtktvsgwddprMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIR---EDLNKTATR 343
Cdd:cd00418 151 gTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAfsvERVNSADAT 214
|
330
....*....|
gi 1995471327 344 vmgvIDPVKL 353
Cdd:cd00418 215 ----FDWAKL 220
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
27-343 |
5.86e-36 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 135.56 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 27 QLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNP--AKEEQEYVDAIKNDIEWLGFQWATECYSSDYFQ 104
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 105 QLYDWAIELIKQGKAYVdgqsseaiaeqkgtpttpgtaspfrdtpveenlaifekmkngeyeagtyvlrakidmaspnml 184
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 185 mrdpllyriinkaHHRTGNEWCIYPMYDWAHGESDYIEQISHSLCTLEFKSHRE----LYDWFlDQIYdksklrPKQREF 260
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEYF-GWEY------PETIHW 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 261 ARRNLSYTVMSKRKLLELVQTKTVSGWDDPRMPTISGLRRRGYTPASIRKFSEVSGISKRDGVTDVSLLEFCIREDLNKT 340
Cdd:cd09287 158 GRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPR 237
|
...
gi 1995471327 341 ATR 343
Cdd:cd09287 238 ANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
29-120 |
6.14e-11 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 64.10 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 29 RFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQWATEC-YSSDYFqQLY 107
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVlYQSQRH-DAY 85
|
90
....*....|....
gi 1995471327 108 DWAIE-LIKQGKAY 120
Cdd:PRK05710 86 RAALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
24-155 |
3.50e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 59.76 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 24 PQEQLRFRFPPEPNGYLHIGHAASICLNFGLGERYNAPVNLRFDDTNPAKEEQEYVDAIKNDIEWLGFQW------ATEC 97
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdvGGEY 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1995471327 98 --YSSDYFQQLY-DWAIELIKQGKAYVDGQSSE------AIAEQKGTPttP------GTASpfrDTPVEENLA 155
Cdd:PLN02627 122 gpYRQSERNAIYkQYAEKLLESGHVYPCFCTDEeleamkEEAELKKLP--PrytgkwATAS---DEEVQAELA 189
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
31-123 |
1.56e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 50.94 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPNGYLHIGHAASICLNFGLGERYNAPV-----NLRFDDTNPAKEEQ---------EYVDA----IKNDIEWLgfq 92
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGykvrcIALIDDAGGLIGDPankkgenakAFVERwierIKEDVEYM--- 79
|
90 100 110
....*....|....*....|....*....|.
gi 1995471327 93 watecyssdyFQQLYDWAIELIKQGKAYVDG 123
Cdd:cd00802 80 ----------FLQAADFLLLYETECDIHLGG 100
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
31-122 |
9.66e-07 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 47.53 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995471327 31 RFPPEPnGYLHIGHAASICLNFGLGERynapVNLRFDDTNPAKEEQ------EYVDAIKNDIewlgfqwatECYSSDYFQ 104
Cdd:cd02156 3 RFPGEP-GYLHIGHAKLICRAKGIADQ----CVVRIDDNPPVKVWQdpheleERKESIEEDI---------SVCGEDFQQ 68
|
90
....*....|....*...
gi 1995471327 105 QlydwaIELIKQGKAYVD 122
Cdd:cd02156 69 N-----RELYRWVKDNIT 81
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
226-274 |
1.49e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 44.45 E-value: 1.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1995471327 226 HSLCTLEFKSHRELYDWFLDqiYDKSKLRPKQREFARRNLSYTVMSKRK 274
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKD--NITLPVDPEQVELPRLNLETTVMSKRK 105
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