|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
18-575 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1085.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 18 MTTPQSERRDFIREMIANDLASGNCKTPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQE 97
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDY---GGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 98 YVDSIQSDIKWLGFDWGNNLYFASNIFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPYRDRSIEENIAR 177
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 178 FTAMKNGEIPEGKAVLRAKIDMASSNMNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENH 257
Cdd:PRK05347 160 FERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 258 RPLYDWVIDNCPVPSRPRQTEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGIT 337
Cdd:PRK05347 240 RPLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 338 KFNGITDVALLEHSVRGELNATAPRRMAVLRPLKLVLTNLPANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMID 417
Cdd:PRK05347 320 KQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 418 PPKKYFRLGVGRTVRLRGGYCVTCTGYCTDEAGNVTEVQAEIIPGTIGNNPPEGIKCKTAIHWVAVPHAVDAEVRLYDRL 497
Cdd:PRK05347 400 PPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRL 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 498 FSCENPDAhEEGFLAALNPDSLdIIAHAKIEPALAAAEPEFVCQFERLGYFVADrRDHAPEHPVYNRAVALKDSWAKA 575
Cdd:PRK05347 480 FTVPNPAA-GKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
47-572 |
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: 667.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 47 TRFPPEPNGYLHIGHAKAICLNFGLALEYAsvgARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNIFDF 126
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYN---GTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 127 FYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPYRDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSNMNM 206
Cdd:TIGR00440 80 LYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 207 RDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSRLNITY 286
Cdd:TIGR00440 160 RDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 287 TVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGELNATAPRRMAV 366
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 367 LRPLKLVLTNLpANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMIDPPKKYFRLGVGRTVRLRGGYCVTCTGYCT 446
Cdd:TIGR00440 320 IDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 447 DEAGNVTEVQAEIIPGTIGNNPPEGIKCKTAIHWVAVPHAVDAEVRLYDRLFSCENPdAHEEGFLAALNPDSLdIIAHAK 526
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPDDFLSVINPESL-VIKQGF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1093279645 527 IEPALAAAEPEFVCQFERLGYFVADRRDHAPEHPVYNRAVALKDSW 572
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
46-362 |
1.97e-138 |
|
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: 401.24 E-value: 1.97e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNnLYFASNIFD 125
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKY---GGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK-VTYASDYFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVdeqdvetiraqrgnlvtpgthspyrdrsieeniarftamkngeipegkavlrakidmassnmn 205
Cdd:cd00807 79 QLYEYAEQLIKKGKAYV--------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 206 mrdpilyrivfaeHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPsRPRQTEFSRLNIT 285
Cdd:cd00807 96 -------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLT 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093279645 286 YTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGELNATAPR 362
Cdd:cd00807 162 YTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
46-338 |
4.31e-126 |
|
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: 372.81 E-value: 4.31e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNIFD 125
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNH---NGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGthSPYRDRSIEENIARFT-AMKNGEIPEGKAVLRAKIDMASSnM 204
Cdd:pfam00749 80 IYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-Y 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 205 NMRDPILYRIVFAE---HHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSR 281
Cdd:pfam00749 157 VFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093279645 282 LNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITK 338
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIK 293
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
43-550 |
1.11e-116 |
|
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: 354.10 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 43 KTPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASN 122
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKY---GGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 123 IFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPY----RDRSIEEnIARFTAmkNGEipegKAVLRAKI- 197
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE-LERMLA--AGE----PPVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 198 -------DMAS-----SNMNMRDPILYRivfaehhntGDKwciYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVI 265
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 266 DNCPVPsRPrqtEFSRLNITY----TVMSKRKllqlvqeKRVsgwddprmpTISGMRRRGYPAAAIRNFCETVGITKFNG 341
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 342 --ITDVALLEHSVrgELNATaPRRMAVLRPLKLVLTNLPANHSETVTVVNN---PEKPEEG-----TRELTLTRE----- 406
Cdd:COG0008 281 qeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 407 ---------VWIEQDDfmIDPPKKYFRLGVGRTVrlrggycVTCTgycTDEAGNVTEVQAEIIpgtignnppegikcKTA 477
Cdd:COG0008 358 selaelarfFFIERED--EKAAKKRLAPEEVRKV-------LKAA---LEVLEAVETWDPETV--------------KGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 478 IHWVavphAVDAEVRlyDRLFScenpdahEEGFLAalnpdsldiIAHAKIEPALAAAEP-----EFvcqFERLGYFVA 550
Cdd:COG0008 412 IHWV----SAEAGVK--DGLLF-------MPLRVA---------LTGRTVEPSLFDVLEllgkeRV---FERLGYAID 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
18-575 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1085.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 18 MTTPQSERRDFIREMIANDLASGNCKTPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQE 97
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDY---GGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 98 YVDSIQSDIKWLGFDWGNNLYFASNIFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPYRDRSIEENIAR 177
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 178 FTAMKNGEIPEGKAVLRAKIDMASSNMNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENH 257
Cdd:PRK05347 160 FERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 258 RPLYDWVIDNCPVPSRPRQTEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGIT 337
Cdd:PRK05347 240 RPLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 338 KFNGITDVALLEHSVRGELNATAPRRMAVLRPLKLVLTNLPANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMID 417
Cdd:PRK05347 320 KQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 418 PPKKYFRLGVGRTVRLRGGYCVTCTGYCTDEAGNVTEVQAEIIPGTIGNNPPEGIKCKTAIHWVAVPHAVDAEVRLYDRL 497
Cdd:PRK05347 400 PPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRL 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 498 FSCENPDAhEEGFLAALNPDSLdIIAHAKIEPALAAAEPEFVCQFERLGYFVADrRDHAPEHPVYNRAVALKDSWAKA 575
Cdd:PRK05347 480 FTVPNPAA-GKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
18-574 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 841.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 18 MTTPQSERR----DFIREMIANDLASGNCKTPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSK 93
Cdd:PRK14703 1 MSDAPRPRMlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDY---GGRCHLRMDDTNPET 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 94 EDQEYVDSIQSDIKWLGFDWGNNLYFASNIFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPYRDRSIEE 173
Cdd:PRK14703 78 EDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 174 NIARFTAMKNGEIPEGKAVLRAKIDMASSNMNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLE 253
Cdd:PRK14703 158 NLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 254 FENHRPLYDWVIDNC-PVPSRPRQTEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCE 332
Cdd:PRK14703 238 FENNRAIYDWVLDHLgPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 333 TVGITKFNGITDVALLEHSVRGELNATAPRRMAVLRPLKLVLTNLPANHSETVTVVNNP-EKPEEGTRELTLTREVWIEQ 411
Cdd:PRK14703 318 QIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPhDVPKEGSRKVPFTRELYIER 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 412 DDFMIDPPKKYFRLGVGRTVRLRGGYCVTCTGYCTDEAGNVTEVQAEIIPGTIGNNPPeGIKCKTAIHWVAVPHAVDAEV 491
Cdd:PRK14703 398 DDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 492 RLYDRLFSCENPDAHEEGFLAALNPDSLDIIAHaKIEPALAAAEPEFVCQFERLGYFVADRRDHAPEHPVYNRAVALKDS 571
Cdd:PRK14703 477 RLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDT 555
|
...
gi 1093279645 572 WAK 574
Cdd:PRK14703 556 WGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
47-572 |
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: 667.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 47 TRFPPEPNGYLHIGHAKAICLNFGLALEYAsvgARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNIFDF 126
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYN---GTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 127 FYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPYRDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSNMNM 206
Cdd:TIGR00440 80 LYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 207 RDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSRLNITY 286
Cdd:TIGR00440 160 RDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 287 TVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGELNATAPRRMAV 366
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 367 LRPLKLVLTNLpANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMIDPPKKYFRLGVGRTVRLRGGYCVTCTGYCT 446
Cdd:TIGR00440 320 IDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 447 DEAGNVTEVQAEIIPGTIGNNPPEGIKCKTAIHWVAVPHAVDAEVRLYDRLFSCENPdAHEEGFLAALNPDSLdIIAHAK 526
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPDDFLSVINPESL-VIKQGF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1093279645 527 IEPALAAAEPEFVCQFERLGYFVADRRDHAPEHPVYNRAVALKDSW 572
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
30-576 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 552.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 30 REMIANDLASGNCKTpVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWL 109
Cdd:PLN02859 251 KEILEKHLKATGGKV-YTRFPPEPNGYLHIGHAKAMFVDFGLAKER---GGCCYLRFDDTNPEAEKKEYIDHIEEIVEWM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 110 GFDWGNNLYfASNIFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVtpgtHSPYRDRSIEENIARFTAMKNGEIPEG 189
Cdd:PLN02859 327 GWEPFKITY-TSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKM----NSPWRDRPIEESLKLFEDMRRGLIEEG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 190 KAVLRAKIDMASSNMNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCP 269
Cdd:PLN02859 402 KATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 270 VpSRPRQTEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKF-NGITDVALL 348
Cdd:PLN02859 482 L-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 349 EHSVRGELNATAPRRMAVLRPLKLVLTNLPANHSETVTVVNNPEKPEE---GTRELTLTREVWIEQDDFMIDPPKKYFRL 425
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDdpsAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 426 GVGRTVRLRGGYCVTCTGY-CTDEAGNVTEVQAEIipgtignNPPEGIKCKTAIHWVAVP----HAVDAEVRLYDRLFSC 500
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVvLADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAEPspgvEPLKVEVRLFDKLFLS 713
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093279645 501 ENPDAHEEgFLAALNPDSLDIIAHAKIEPALAAAEPEFVCQFERLGYFVADrRDHAPEHPVYNRAVALKDSWAKAK 576
Cdd:PLN02859 714 ENPAELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
9-575 |
1.51e-153 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 452.51 E-value: 1.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 9 QAAQGVEKCMTTPqserrdfirEMIANDLASGNCKtPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDD 88
Cdd:PTZ00437 26 QTGRPVPGCRNTP---------ELLEKHEAVTGGK-PYFRFPPEPNGFLHIGHAKSMNLNFGSARAH---GGKCYLRYDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 89 TNPSKEDQEYVDSIQSDIKWLGF--DWgnnLYFASNIFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLvtpgTHSPY 166
Cdd:PTZ00437 93 TNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQR----EDSPW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 167 RDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSNMNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHIT 246
Cdd:PTZ00437 166 RNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDID 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 247 HSLCTLEFENHRPLYDWVIDNCPVpSRPRQTEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAA 326
Cdd:PTZ00437 246 YSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 327 IRNFCETVGITKFNGITDVALLEHSVRGELNATAPRRMAVLRPLKLVLTNLPAnhSETVTVVNNPEKPEEGTRELTLTRE 406
Cdd:PTZ00437 325 INRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIKVVVDNWKG--EREFECPNHPRKPELGSRKVMFTDT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 407 VWIEQDDFMI-DPPKKYFRLGVG-RTVRLRGGYCVTCTGYCTDEAGNVTEVQAEIipgtignNPPEGIKCKTAIHWVAVP 484
Cdd:PTZ00437 403 FYVDRSDFRTeDNNSKFYGLAPGpRVVGLKYSGNVVCKGFEVDAAGQPSVIHVDI-------DFERKDKPKTNISWVSAT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 485 HAVDAEVRLYDRLFScENPDAHEEGFLAALNPDSlDIIAHAKIEPALAAAEPEFVCQFERLGYFVADrRDHAPEHPVYNR 564
Cdd:PTZ00437 476 ACTPVEVRLYNALLK-DDRAAIDPEFLKFIDEDS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVD-PDTRPDHLVMNR 552
|
570
....*....|.
gi 1093279645 565 AVALKDSWAKA 575
Cdd:PTZ00437 553 VLGLREDKEKA 563
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
46-362 |
1.97e-138 |
|
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: 401.24 E-value: 1.97e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNnLYFASNIFD 125
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKY---GGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK-VTYASDYFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVdeqdvetiraqrgnlvtpgthspyrdrsieeniarftamkngeipegkavlrakidmassnmn 205
Cdd:cd00807 79 QLYEYAEQLIKKGKAYV--------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 206 mrdpilyrivfaeHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPsRPRQTEFSRLNIT 285
Cdd:cd00807 96 -------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLT 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093279645 286 YTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGELNATAPR 362
Cdd:cd00807 162 YTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
46-338 |
4.31e-126 |
|
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: 372.81 E-value: 4.31e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNIFD 125
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNH---NGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGthSPYRDRSIEENIARFT-AMKNGEIPEGKAVLRAKIDMASSnM 204
Cdd:pfam00749 80 IYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-Y 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 205 NMRDPILYRIVFAE---HHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSR 281
Cdd:pfam00749 157 VFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093279645 282 LNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITK 338
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIK 293
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
43-550 |
1.11e-116 |
|
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: 354.10 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 43 KTPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASN 122
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKY---GGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 123 IFDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNLVTPGTHSPY----RDRSIEEnIARFTAmkNGEipegKAVLRAKI- 197
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE-LERMLA--AGE----PPVLRFKIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 198 -------DMAS-----SNMNMRDPILYRivfaehhntGDKwciYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVI 265
Cdd:COG0008 153 eegvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 266 DNCPVPsRPrqtEFSRLNITY----TVMSKRKllqlvqeKRVsgwddprmpTISGMRRRGYPAAAIRNFCETVGITKFNG 341
Cdd:COG0008 221 EALGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 342 --ITDVALLEHSVrgELNATaPRRMAVLRPLKLVLTNLPANHSETVTVVNN---PEKPEEG-----TRELTLTRE----- 406
Cdd:COG0008 281 qeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 407 ---------VWIEQDDfmIDPPKKYFRLGVGRTVrlrggycVTCTgycTDEAGNVTEVQAEIIpgtignnppegikcKTA 477
Cdd:COG0008 358 selaelarfFFIERED--EKAAKKRLAPEEVRKV-------LKAA---LEVLEAVETWDPETV--------------KGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 478 IHWVavphAVDAEVRlyDRLFScenpdahEEGFLAalnpdsldiIAHAKIEPALAAAEP-----EFvcqFERLGYFVA 550
Cdd:COG0008 412 IHWV----SAEAGVK--DGLLF-------MPLRVA---------LTGRTVEPSLFDVLEllgkeRV---FERLGYAID 464
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
46-552 |
1.02e-98 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 315.51 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDwGNNLYFASNIFD 125
Cdd:PLN02907 215 CTRFPPEPSGYLHIGHAKAALLNQYFARRY---KGKLIVRFDDTNPSKESDEFVENILKDIETLGIK-YDAVTYTSDYFP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNlvtpGTHSPYRDRSIEENIARFTAMKNGEiPEGKA-VLRAKIDMASSNM 204
Cdd:PLN02907 291 QLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGS-ERGLQcCVRGKLDMQDPNK 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 205 NMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPsRPRQTEFSRLNI 284
Cdd:PLN02907 366 SLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIWEFSRLNF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 285 TYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKfngitDVALLEHSVRGELNA-----T 359
Cdd:PLN02907 445 VYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLMEWDKLWTINKkiidpV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 360 APRRMAVLRPLK--LVLTNLPANhSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMIdppkkyfrLGVGRTVRLRG-G 436
Cdd:PLN02907 520 CPRHTAVLKEGRvlLTLTDGPET-PFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMDwG 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 437 YCVTcTGYCTDEAGNVTEVQAEIipgtignNPPEGIK-CKTAIHWVA-VPHAVDAEVRLYDRLFSCENPDaHEEGFLAAL 514
Cdd:PLN02907 591 NAII-KEITKDEGGAVTALSGEL-------HLEGSVKtTKLKLTWLPdTNELVPLSLVEFDYLITKKKLE-EDDNFLDVL 661
|
490 500 510
....*....|....*....|....*....|....*...
gi 1093279645 515 NPDSLDIIAhAKIEPALAAAEPEFVCQFERLGYFVADR 552
Cdd:PLN02907 662 NPCTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCDA 698
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
46-558 |
1.89e-92 |
|
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: 294.42 E-value: 1.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYfASNIFD 125
Cdd:TIGR00463 95 VMRFAPNPSGPLHIGHARAAILNHEYAKKY---DGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY-QSDRIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNlvtpGTHSPYRDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSNMN 205
Cdd:TIGR00463 171 TYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 206 MRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEF--ENHRPLYDWVIDNCpvpsRPRQT---EFS 280
Cdd:TIGR00463 247 IRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGW----EPPEFihwGRL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 281 RLNITYTVMSKRKlLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGItkfnGITDVALLEHSVRGE----L 356
Cdd:TIGR00463 323 KIDDVRALSTSSA-RKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGV----KINDVTMSWKNIYALnrkiI 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 357 NATAPRRMAVLRPLKLVLTNLPanhsETVTVVN--NPEKPEEGTRELTLTREVWIEQDDFmidppkkyfrlGVGRT-VRL 433
Cdd:TIGR00463 398 DEEARRYFFIWNPVKIEIVGLP----EPKRVERplHPDHPEIGERVLILRGEIYVPKDDL-----------EEGVEpVRL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 434 RggycvtctgyctdEAGNV--TEVQAEIIPGTIgnnppEGIKCKTA--IHWVAVPHAVDAEVrlydrlfscenpdaheeg 509
Cdd:TIGR00463 463 M-------------DAVNViySKKELRYHSEGL-----EGARKLGKsiIHWLPAKDAVKVKV------------------ 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1093279645 510 flaaLNPDSLdiIAHAKIEPALAAAEPEFVCQFERLGYFvadRRDHAPE 558
Cdd:TIGR00463 507 ----IMPDAS--IVEGVIEADASELEVGDVVQFERFGFA---RLDSADK 546
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
46-561 |
4.30e-90 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 287.29 E-value: 4.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYAsvgARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDwGNNLYFASNIFD 125
Cdd:PLN03233 13 VTRFPPEPSGYLHIGHAKAALLNDYYARRYK---GRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNLvtpgTHSPYRDRSIEENIARFTAMKNGEiPEGKA-VLRAKIDMASSNM 204
Cdd:PLN03233 89 PIRCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGK-EEGGAwCLRAKIDMQSDNG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 205 NMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVpSRPRQTEFSRLNI 284
Cdd:PLN03233 164 TLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL-RRPRIHAFARMNF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 285 TYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGELNATAPRRM 364
Cdd:PLN03233 243 MNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 365 AVLRP--LKLVLTNLP-ANHSETVTVVNNPEKPEEGTRELTLTREVWIEQ---DDFMIDPPKKYFRLGVGRTVRLRGGyc 438
Cdd:PLN03233 323 AIDKAdhTALTVTNADeEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKadtEDIQLGEDIVLLRWGVIEISKIDGD-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 439 vtctgyctdeagnvteVQAEIIPgtigNNPPEGIKCKtaIHWVA-VPHAVDAEVRLYDRLFSCENPDaHEEGFLAALNPD 517
Cdd:PLN03233 401 ----------------LEGHFIP----DGDFKAAKKK--ISWIAdVSDNIPVVLSEFDNLIIKEKLE-EDDKFEDFINPD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1093279645 518 SL---DIIAHAkiepALAAAEPEFVCQFERLGYFVADRRDHAPEHPV 561
Cdd:PLN03233 458 TLaetDVIGDA----GLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
46-551 |
1.51e-88 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 285.70 E-value: 1.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYAsvgARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNIFD 125
Cdd:PTZ00402 54 VTRFPPEASGFLHIGHAKAALINSMLADKYK---GKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 126 FFYDCAVHLINNGLAYVDEQDVETIRAQRGNlvtpGTHSPYRDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSNMN 205
Cdd:PTZ00402 131 LMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 206 MRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVpSRPRQTEFSRLNIT 285
Cdd:PTZ00402 207 MRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI-RKPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 286 YTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKfngitDVALLEHSVRGELNA-----TA 360
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSK-----TVNFMEWSKLWYFNTqildpSV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 361 PRRMAVLRPLKLVLTNLPANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMIdppkkyfrlgvgrtvrLRGGYCVT 440
Cdd:PTZ00402 361 PRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVAL----------------LKEGDEVT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 441 CTGYCTDEAGNVTEVQAEIIP--GTIGNNPPEGI-KCKTAIHWVA-VPHAVDAEVRLYDRLFSCENPDAHE--EGFLAAL 514
Cdd:PTZ00402 425 LMDWGNAYIKNIRRSGEDALItdADIVLHLEGDVkKTKFKLTWVPeSPKAEVMELNEYDHLLTKKKPDPEEsiDDIIAPV 504
|
490 500 510
....*....|....*....|....*....|....*..
gi 1093279645 515 NPDSLDIIAhakiEPALAAAEPEFVCQFERLGYFVAD 551
Cdd:PTZ00402 505 TKYTQEVYG----EEALSVLKKGDIIQLERRGYYIVD 537
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
46-547 |
8.17e-85 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 274.81 E-value: 8.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPS--KEDQEYVDSIQSDIKWLGFDWgNNLYFASNI 123
Cdd:PRK04156 103 VMRFAPNPSGPLHLGHARAAILNDEYAKMY---GGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKW-DEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 124 FDFFYDCAVHLINNGLAYVDEQDVETIRAQRGNlvtpGTHSPYRDRSIEENIARFTAMKNGEIPEGKAVLRAKIDMASSN 203
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 204 MNMRDPILYRIVFAEHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEF----ENHRPLYD---WVIdncpvpsrPRQ 276
Cdd:PRK04156 255 PSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYDyfgWEY--------PET 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 277 TEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGItkfnGITDVALLEHSV---- 352
Cdd:PRK04156 327 IHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGV----KETDATISWENLyain 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 353 RGELNATAPRRMAVLRPLKLVLTNLPanhSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFMidppkkyfrlGVGRTVR 432
Cdd:PRK04156 403 RKLIDPIANRYFFVRDPVELEIEGAE---PLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMVR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 433 LRGGYCVTCTG-------YCTDEAGNVTEVQAEIipgtignnppegikcktaIHWVAVPHAVDAEVRlydrlfsceNPDA 505
Cdd:PRK04156 470 LMDLFNVEITGvsvdkarYHSDDLEEARKNKAPI------------------IQWVPEDESVPVRVL---------KPDG 522
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1093279645 506 -HEEGFlaalnpdsldiiahakIEPALAAAEPEFVCQFERLGY 547
Cdd:PRK04156 523 gDIEGL----------------AEPDVADLEVDDIVQFERFGF 549
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
360-551 |
6.18e-66 |
|
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: 212.52 E-value: 6.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 360 APRRMAVLRPLKLVLTNLPANHSETVTVVNNPEKPEEGTRELTLTREVWIEQDDFmidppkkyFRLGVGRTVRLRGGYCV 439
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 440 TCTGYCTDEAGNVTEVQAEIIPGTIGNNppegIKCKTA-IHWVAVPHAVDAEVRLYDRLFSCENpdahEEGFLaaLNPDS 518
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGKiIHWVSASDAVPAEVRLYDRLFKDED----DADFL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 1093279645 519 LDIIAHAKIEPALAAAEPEFVCQFERLGYFVAD 551
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
44-349 |
5.74e-55 |
|
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: 185.75 E-value: 5.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 44 TPVTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNI 123
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKY---GGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 124 FDFFYDCAVHLINNGlayvdeqdvetiraqrgnlvtpgthspyrdrsieeniarftamkngeipegkavlrakidmassn 203
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 204 mnmrdpilyrivfaehhntgdkwcIYPMYDFAHPLEDAYEHITHSLCTLEFENHRPLYDWVIDNCPVPsRPRQTEFSRLN 283
Cdd:cd00418 93 ------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLL 147
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093279645 284 ITY-TVMSKRKLlqlvqekrvsgwddprMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLE 349
Cdd:cd00418 148 LEDgTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEE 198
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
46-362 |
1.82e-38 |
|
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: 141.72 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNP--SKEDQEYVDSIQSDIKWLGFDWgNNLYFASNI 123
Cdd:cd09287 3 VMRFAPNPNGPLHLGHARAAILNGEYAKMY---GGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKW-DEVVIASDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 124 FDFFYDCAVHLINNGLAYVdeqdvetiraqrgnlvtpgthspyrdrsieeniarftamkngeipegkavlrakidmassn 203
Cdd:cd09287 79 IELYYEYARKLIEMGGAYV------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 204 mnmrdpilyrivfaeHHNTGDKWCIYPMYDFAHPLEDAYEHITHSLCTLEF----ENHRPLYD---WvidncpvpSRPRQ 276
Cdd:cd09287 98 ---------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYEyfgW--------EYPET 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 277 TEFSRLNITYTVMSKRKLLQLVQEKRVSGWDDPRMPTISGMRRRGYPAAAIRNFCETVGITKFNGITDVALLEHSVRGEL 356
Cdd:cd09287 155 IHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLI 234
|
....*.
gi 1093279645 357 NATAPR 362
Cdd:cd09287 235 DPRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
44-141 |
9.67e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 69.11 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 44 TPVTRFPPEPNGYLHIGHAKAICLNFGLAleyASVGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDWGNNLYFASNI 123
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDA---RAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR 81
|
90
....*....|....*....
gi 1093279645 124 FDfFYDCAV-HLINNGLAY 141
Cdd:PRK05710 82 HD-AYRAALdRLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
46-113 |
4.57e-11 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates 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.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 62.99 E-value: 4.57e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYasvGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDW 113
Cdd:cd00808 3 RTRFAPSPTGFLHIGGARTALFNYLFARKH---GGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW 67
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
46-293 |
6.68e-11 |
|
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: 60.57 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 46 VTRFPPEPNGYLHIGHAKAICLNFGLALEYASVGA--RCHLRFDDTNPSKEDQEYVdsiqsdikwlgfdwgnnlyfasni 123
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYkvRCIALIDDAGGLIGDPANK------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 124 fdfFYDCAVHlinnglayvdeqdvetiraqrgnlvtpgthspYRDRSIEEniarftamkngeipegkavlrakidmassn 203
Cdd:cd00802 57 ---KGENAKA--------------------------------FVERWIER------------------------------ 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 204 mnMRDPILYRIvfaehhntgdKWCiypmYDFAHPLEdayEHITHSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSRLN 283
Cdd:cd00802 72 --IKEDVEYMF----------LQA----ADFLLLYE---TECDIHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGRVM 132
|
250
....*....|.
gi 1093279645 284 ITY-TVMSKRK 293
Cdd:cd00802 133 GADgTKMSKSK 143
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
46-117 |
1.10e-08 |
|
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: 52.93 E-value: 1.10e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093279645 46 VTRFPPEPnGYLHIGHAKAICLNFGLALEyasvgarCHLRFDDTNPSK------EDQEYVDSIQSDIKWLGFDWGNNL 117
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIADQ-------CVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNR 70
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
247-293 |
9.70e-08 |
|
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: 50.23 E-value: 9.70e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1093279645 247 HSLCTLEFENHRPLYDWVIDNCPVPSRPRQTEFSRLNITYTVMSKRK 293
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
44-113 |
2.06e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 53.59 E-value: 2.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093279645 44 TPVTRFPPEPNGYLHIGHAKAICLNFGLAleyASVGARCHLRFDDTNPSKEDQEYVDSIQSDIKWLGFDW 113
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFA---RSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDW 111
|
|
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