|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1247.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 1 MTQASSPTNFIRQIIDEDLASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 81 IKRDVQWLGFQWNGEVCYSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKNSPFRDRSVDENLALFDKM 160
Cdd:PRK05347 84 IKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 161 KNGEFAEGTACLRAKIDMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLY 240
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 241 DWVLDNISIECHPRQYEFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDN 320
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 321 IVEMGMLEACIRDDLNENAPRAMAVLNPVKVVIENL--DHDETLTAPAHPNKPEMGSRELHFGREIFIDQADFREEANKQ 398
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYpeGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 399 FKRLVLGKEVRLRNAYVIKAERVEKDAEGKVTCIYCSYDADTLGKDPADGRKVKGVIHWVSAPTSLPAEIRLYDRLFKVP 478
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759052087 479 NPGAEEDFEAALNPESLVIIEGaRVEASLKDAKPEFAYQFEREGYFCADnKLSSAEHLVFNRTVALRDSWGKV 551
Cdd:PRK05347 484 NPAAGKDFLDFLNPDSLVIKQG-FVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-548 |
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: 954.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDKL 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKNSPFRDRSVDENLALFDKMKNGEFAEGTACLRAKIDMASPFMVMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 187 DPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIECHPRQYEFSRLNLEYT 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 267 VMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNENAPRAMAVL 346
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 347 NPVKVVIENLDHD-ETLTAPAHPNKPEMGSRELHFGREIFIDQADFREEANKQFKRLVLGKEVRLRNAYVIKAERVEKDA 425
Cdd:TIGR00440 321 DPVEVVIENLSDEyELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 426 EGKVTCIYCSYDADTLGKDPADGRKVKGVIHWVSAPTSLPAEIRLYDRLFKVPNPGAEEDFEAALNPESLVIIEGArVEA 505
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGF-MEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1759052087 506 SLKDAKPEFAYQFEREGYFCADNKLSSAEHLVFNRTVALRDSW 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-337 |
1.03e-164 |
|
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: 470.26 E-value: 1.03e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDKL 106
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVDELTPEQMREYRGTLtePGKNSPFRDRSVDENLALF-DKMKNGEFAEGTACLRAKIDMASPfMVM 185
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 186 RDPVIYRIKFA---HHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIECHPRQYEFSRLN 262
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759052087 263 LEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNI-VEMGMLEACIRDDLNE 337
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-341 |
9.30e-155 |
|
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: 442.08 E-value: 9.30e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWnGEVCYSSDYFDKL 106
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVdeltpeqmreyrgtltepgknspfrdrsvdenlalfdkmkngefaegtaclrakidmaspfmvmr 186
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 187 dpviyrikfahHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEChPRQYEFSRLNLEYT 266
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1759052087 267 VMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNENAPR 341
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-524 |
9.41e-139 |
|
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: 409.95 E-value: 9.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 25 SSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFD 104
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 105 KLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKN----SPFRDRSVDENlalfDKMKngefAEG-TACLRAKI--- 176
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 177 -----DMAS-----PFMVMRDPVIYRikfahhhqtGDKwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 246
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 247 ISIEcHPrqyEFSRLNLEY----TVMSKRKlnqlvteKHVegwddprmlTVSGLRRRGYTPAAIREFCLRIGVTKQDN-- 320
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 321 IVEMGMLEACIrdDLNENaPRAMAVLNPVKVVIENLDH-----DETLTAPAHPNKPEMG-----SRELHFGRE------- 383
Cdd:COG0008 283 IFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYiraldDEELAELLAPELPEAGiredlERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 384 -------IFIDQADfrEEANKqfKRLVLgKEVRlrnAYVIKAERVEKDAEgkvtciycSYDADTlgkdpadgrkVKGVIH 456
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVR---KVLKAALEVLEAVE--------TWDPET----------VKGTIH 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1759052087 457 WVSAptslPAEIRlyDRLFKVPnpgaeedfeaalnpesL-VIIEGARVEASLKDA-----KPEFayqFEREGYF 524
Cdd:COG0008 414 WVSA----EAGVK--DGLLFMP----------------LrVALTGRTVEPSLFDVlellgKERV---FERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1247.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 1 MTQASSPTNFIRQIIDEDLASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 81 IKRDVQWLGFQWNGEVCYSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKNSPFRDRSVDENLALFDKM 160
Cdd:PRK05347 84 IKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 161 KNGEFAEGTACLRAKIDMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLY 240
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 241 DWVLDNISIECHPRQYEFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDN 320
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 321 IVEMGMLEACIRDDLNENAPRAMAVLNPVKVVIENL--DHDETLTAPAHPNKPEMGSRELHFGREIFIDQADFREEANKQ 398
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYpeGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 399 FKRLVLGKEVRLRNAYVIKAERVEKDAEGKVTCIYCSYDADTLGKDPADGRKVKGVIHWVSAPTSLPAEIRLYDRLFKVP 478
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759052087 479 NPGAEEDFEAALNPESLVIIEGaRVEASLKDAKPEFAYQFEREGYFCADnKLSSAEHLVFNRTVALRDSWGKV 551
Cdd:PRK05347 484 NPAAGKDFLDFLNPDSLVIKQG-FVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-548 |
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: 954.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDKL 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKNSPFRDRSVDENLALFDKMKNGEFAEGTACLRAKIDMASPFMVMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 187 DPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIECHPRQYEFSRLNLEYT 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 267 VMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNENAPRAMAVL 346
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 347 NPVKVVIENLDHD-ETLTAPAHPNKPEMGSRELHFGREIFIDQADFREEANKQFKRLVLGKEVRLRNAYVIKAERVEKDA 425
Cdd:TIGR00440 321 DPVEVVIENLSDEyELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 426 EGKVTCIYCSYDADTLGKDPADGRKVKGVIHWVSAPTSLPAEIRLYDRLFKVPNPGAEEDFEAALNPESLVIIEGArVEA 505
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGF-MEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1759052087 506 SLKDAKPEFAYQFEREGYFCADNKLSSAEHLVFNRTVALRDSW 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-553 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 868.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 1 MTQASSPT-----NFIRQIIDEDLASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDI 75
Cdd:PRK14703 1 MSDAPRPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 76 EYVESIKRDVQWLGFQWNGEVCYSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKNSPFRDRSVDENLA 155
Cdd:PRK14703 81 EYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 156 LFDKMKNGEFAEGTACLRAKIDMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQD 235
Cdd:PRK14703 161 LFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 236 NRRLYDWVLDNIS-IECHPRQYEFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIG 314
Cdd:PRK14703 241 NRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 315 VTKQDNIVEMGMLEACIRDDLNENAPRAMAVLNPVKVVIENL--DHDETLTAPAHPNK-PEMGSRELHFGREIFIDQADF 391
Cdd:PRK14703 321 VAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLpaGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 392 REEANKQFKRLVLGKEVRLRNAYVIKAERVEKDAEGKVTCIYCSYDADTLGKDPAdGRKVKGVIHWVSAPTSLPAEIRLY 471
Cdd:PRK14703 401 SEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 472 DRLFKVPNP-GAEEDFEAALNPESLVIIEGaRVEASLKDAKPEFAYQFEREGYFCADNKLSSAEHLVFNRTVALRDSWGK 550
Cdd:PRK14703 480 DRLFKVPQPeAADEDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
...
gi 1759052087 551 VEG 553
Cdd:PRK14703 559 RAR 561
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
12-550 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 608.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 12 RQIIDEDL--ASGKhssVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLG 89
Cdd:PLN02859 251 KEILEKHLkaTGGK---VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 90 fqWNG-EVCYSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRgtltEPGKNSPFRDRSVDENLALFDKMKNGEFAEG 168
Cdd:PLN02859 328 --WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 169 TACLRAKIDMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNIS 248
Cdd:PLN02859 402 KATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 249 IEcHPRQYEFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDN-IVEMGML 327
Cdd:PLN02859 482 LY-QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 328 EACIRDDLNENAPRAMAVLNPVKVVIENLDHDET--LTAPAHPNKPEMGSRELH---FGREIFIDQADFREEANKQFKRL 402
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVieLDAKRWPDAQNDDPSAFYkvpFSRVVYIERSDFRLKDSKDYYGL 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 403 VLGKEVRLRNAYVIK-AERVEKDAEGKVTCIYCSYdadtlgkDPADGRKVKGVIHWVSAPT----SLPAEIRLYDRLFKV 477
Cdd:PLN02859 641 APGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAEPSpgvePLKVEVRLFDKLFLS 713
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759052087 478 PNPGAEEDFEAALNPESLVIIEGARVEASLKDAKPEFAYQFEREGYFCADnKLSSAEHLVFNRTVALRDSWGK 550
Cdd:PLN02859 714 ENPAELEDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
23-546 |
5.85e-174 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 503.75 E-value: 5.85e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 23 KHSSV-----HTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQ--Wnge 95
Cdd:PTZ00437 43 KHEAVtggkpYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdW--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 96 VCYSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRgtltEPGKNSPFRDRSVDENLALFDKMKNGEFAEGTACLRAK 175
Cdd:PTZ00437 120 VTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 176 IDMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIeCHPRQ 255
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 256 YEFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDL 335
Cdd:PTZ00437 275 WEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 336 NENAPRAMAVLNPVKVVIENLDHDETLTAPAHPNKPEMGSRELHFGREIFIDQADFR-EEANKQFKRLVLG-KEVRLRNA 413
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 414 YVIKAERVEKDAEGKVTCIYCsyDADTLGKDpadgrKVKGVIHWVSAPTSLPAEIRLYDRLFKVPNPGAEEDFEAALNPE 493
Cdd:PTZ00437 435 GNVVCKGFEVDAAGQPSVIHV--DIDFERKD-----KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDED 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1759052087 494 SLVIIEGaRVEASLKDAKPEFAYQFEREGYFCADNKlSSAEHLVFNRTVALRD 546
Cdd:PTZ00437 508 SEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-337 |
1.03e-164 |
|
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: 470.26 E-value: 1.03e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDKL 106
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVDELTPEQMREYRGTLtePGKNSPFRDRSVDENLALF-DKMKNGEFAEGTACLRAKIDMASPfMVM 185
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 186 RDPVIYRIKFA---HHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIECHPRQYEFSRLN 262
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759052087 263 LEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNI-VEMGMLEACIRDDLNE 337
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-341 |
9.30e-155 |
|
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: 442.08 E-value: 9.30e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWnGEVCYSSDYFDKL 106
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGLAYVdeltpeqmreyrgtltepgknspfrdrsvdenlalfdkmkngefaegtaclrakidmaspfmvmr 186
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 187 dpviyrikfahHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEChPRQYEFSRLNLEYT 266
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1759052087 267 VMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNENAPR 341
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-524 |
9.41e-139 |
|
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: 409.95 E-value: 9.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 25 SSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFD 104
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 105 KLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEPGKN----SPFRDRSVDENlalfDKMKngefAEG-TACLRAKI--- 176
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 177 -----DMAS-----PFMVMRDPVIYRikfahhhqtGDKwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 246
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 247 ISIEcHPrqyEFSRLNLEY----TVMSKRKlnqlvteKHVegwddprmlTVSGLRRRGYTPAAIREFCLRIGVTKQDN-- 320
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 321 IVEMGMLEACIrdDLNENaPRAMAVLNPVKVVIENLDH-----DETLTAPAHPNKPEMG-----SRELHFGRE------- 383
Cdd:COG0008 283 IFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYiraldDEELAELLAPELPEAGiredlERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 384 -------IFIDQADfrEEANKqfKRLVLgKEVRlrnAYVIKAERVEKDAEgkvtciycSYDADTlgkdpadgrkVKGVIH 456
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVR---KVLKAALEVLEAVE--------TWDPET----------VKGTIH 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1759052087 457 WVSAptslPAEIRlyDRLFKVPnpgaeedfeaalnpesL-VIIEGARVEASLKDA-----KPEFayqFEREGYF 524
Cdd:COG0008 414 WVSA----EAGVK--DGLLFMP----------------LrVALTGRTVEPSLFDVlellgKERV---FERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
18-527 |
1.33e-117 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 364.05 E-value: 1.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 18 DLASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNgEVC 97
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 98 YSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEpgknSPFRDRSVDENLALFDKMKNGEfAEGTAC-LRAKI 176
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGS-ERGLQCcVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 177 DMASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEcHPRQY 256
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 257 EFSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLN 336
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIID 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 337 ENAPRAMAVLNPVKVVIENLDHDET---LTAPAHPNKPEMGSRELHFGREIFIDQADFREeankqfkrLVLGKEVRLR-- 411
Cdd:PLN02907 518 PVCPRHTAVLKEGRVLLTLTDGPETpfvRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMdw 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 412 -NAYVikaERVEKDAEGKVTCIYCSYDADtlgkdpADGRKVKGVIHWVSAPTSL-PAEIRLYDRLFKVPNPGAEEDFEAA 489
Cdd:PLN02907 590 gNAII---KEITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNFLDV 660
|
490 500 510
....*....|....*....|....*....|....*...
gi 1759052087 490 LNPESLVIIeGARVEASLKDAKPEFAYQFEREGYFCAD 527
Cdd:PLN02907 661 LNPCTKKET-AALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
18-529 |
6.08e-115 |
|
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: 351.82 E-value: 6.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 18 DLASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNgEVC 97
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 98 YSSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTltepGKNSPFRDRSVDENLALFDKMKNGEFAEGTACLRAKID 177
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 178 MASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR--LYDWVLDNISI-ECHpr 254
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYIYRYFGWEPpEFI-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 255 QYEFSRLNLEYTVMSKRKLnQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDD 334
Cdd:TIGR00463 318 HWGRLKIDDVRALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 335 LNENAPRAMAVLNPVKVVIENLDHDETLTAPAHPNKPEMGSRELHFGREIFIDQADFREeankqfkrlvLGKEVRLRNAY 414
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLPEPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEE----------GVEPVRLMDAV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 415 VIKAErvEKDAEgkvtciYCSYDADtlgkdpADGRKVKGVIHWVSAPTSLPAEIRLYDRLfkvpnpgaeedfeaalnpes 494
Cdd:TIGR00463 467 NVIYS--KKELR------YHSEGLE------GARKLGKSIIHWLPAKDAVKVKVIMPDAS-------------------- 512
|
490 500 510
....*....|....*....|....*....|....*
gi 1759052087 495 lvIIEGaRVEASLKDAKPEFAYQFEREGYFCADNK 529
Cdd:TIGR00463 513 --IVEG-VIEADASELEVGDVVQFERFGFARLDSA 544
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
19-528 |
2.48e-109 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 338.86 E-value: 2.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 19 LASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCY 98
Cdd:PTZ00402 45 LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 99 SSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTltepGKNSPFRDRSVDENLALFDKMKNGEfAEGT-ACLRAKID 177
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQeTCLRAKIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 178 MASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEcHPRQYE 257
Cdd:PTZ00402 200 VDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR-KPIVED 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 258 FSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNE 337
Cdd:PTZ00402 279 FSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 338 NAPRAMAVLNPVKV--VIENLDHDETLTAPAHPNKPEMGSRELHFGREIFIDQADfreeankqFKRLVLGKEVRLR---N 412
Cdd:PTZ00402 359 SVPRYTVVSNTLKVrcTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAED--------VALLKEGDEVTLMdwgN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 413 AYVIKAERVEKDAegkvtciyCSYDADTLGKDPADGRKVKGVIHWV-SAPTSLPAEIRLYDRLFKVPNPGAEEDFEAALN 491
Cdd:PTZ00402 431 AYIKNIRRSGEDA--------LITDADIVLHLEGDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPDPEESIDDIIA 502
|
490 500 510
....*....|....*....|....*....|....*..
gi 1759052087 492 PESLVIIEgARVEASLKDAKPEFAYQFEREGYFCADN 528
Cdd:PTZ00402 503 PVTKYTQE-VYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
27-523 |
1.12e-106 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 331.05 E-value: 1.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPV--KEDIEYVESIKRDVQWLGFQWNgEVCYSSDYFD 104
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 105 KLHGYAIELIEKGLAYVDELTPEQMREYRgtltEPGKNSPFRDRSVDENLALFDKMKNGEFAEGTACLRAKIDMASPFMV 184
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 185 MRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDN----RRLYD---WVLdnisiechPRQYE 257
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY--------PETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 258 FSRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNE 337
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 338 NAPRAMAVLNPVKVVIENLDhDETLTAPAHPNKPEMGSRELHFGREIFIDQADFREeankqfkrlvLGKEVRLRNAYVIK 417
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAE-PLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFNVE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 418 AERVEKDaegkvtciYCSYDADTLgkdpADGRKVKG-VIHWVSAPTSLPAEIRlydrlfkVPNPGaeedfeaalnpeslv 496
Cdd:PRK04156 478 ITGVSVD--------KARYHSDDL----EEARKNKApIIQWVPEDESVPVRVL-------KPDGG--------------- 523
|
490 500
....*....|....*....|....*..
gi 1759052087 497 IIEGaRVEASLKDAKPEFAYQFEREGY 523
Cdd:PRK04156 524 DIEG-LAEPDVADLEVDDIVQFERFGF 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-527 |
4.28e-103 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 320.42 E-value: 4.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 19 LASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNgEVCY 98
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 99 SSDYFDKLHGYAIELIEKGLAYVDELTPEQMREYRGTLTEpgknSPFRDRSVDENLALFDKMKNGEFAEGTACLRAKIDM 178
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 179 ASPFMVMRDPVIYRIKFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEcHPRQYEF 258
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 259 SRLNLEYTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNEN 338
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 339 APRAMAV--LNPVKVVIENLD---HDETLTAPAHPNKPEMGSRELHFGREIFIDQADfreeankqFKRLVLGKEVRLRNA 413
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADeeaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 414 YVIKAERVEKDAEGKVTciycsydadtlgkDPADGRKVKGVIHWVS-APTSLPAEIRLYDRLFKVPNPGAEEDFEAALNP 492
Cdd:PLN03233 390 GVIEISKIDGDLEGHFI-------------PDGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINP 456
|
490 500 510
....*....|....*....|....*....|....*
gi 1759052087 493 ESLVIIEgARVEASLKDAKPEFAYQFEREGYFCAD 527
Cdd:PLN03233 457 DTLAETD-VIGDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
339-527 |
9.84e-79 |
|
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: 245.26 E-value: 9.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 339 APRAMAVLNPVKVVIENLDHD--ETLTAPAHPNKPEMGSRELHFGREIFIDQADFreeankqfKRLVLGKEVRLRNAYVI 416
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGqeETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 417 KAERVEKDAEGKVTCIYCSYDADTLGKDpadgRKVKG-VIHWVSAPTSLPAEIRLYDRLFKVPNpgaEEDFEaaLNPESL 495
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---DADFL--LNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1759052087 496 VIIEGARVEASLKDAKPEFAYQFEREGYFCAD 527
Cdd:pfam03950 144 KVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-337 |
4.19e-78 |
|
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: 245.46 E-value: 4.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDKL 106
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 107 HGYAIELIEKGlayvdeltpeqmreyrgtltepgknspfrdrsvdenlalfdkmkngefaegtaclrakidmaspfmvmr 186
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 187 dpviyrikfahhhqtgdkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEcHPRQYEFSRLNLEY- 265
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 266 TVMSKRKLNQlvtekhvegwddprmlTVSGLRRRGYTPAAIREFCLRIGVTK-----------------------QDNIV 322
Cdd:cd00418 152 TKLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADATF 215
|
330
....*....|....*
gi 1759052087 323 EMGMLEACIRDDLNE 337
Cdd:cd00418 216 DWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
27-341 |
4.59e-51 |
|
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: 175.23 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 27 VHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNP--VKEDIEYVESIKRDVQWLGFQWNgEVCYSSDYFD 104
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 105 KLHGYAIELIEKGLAYVdeltpeqmreyrgtltepgknspfrdrsvdenlalfdkmkngefaegtaclrakidmaspfmv 184
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 185 mrdpviyrikfahHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIEcHPRQYEFSRLNLE 264
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIE 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1759052087 265 YTVMSKRKLNQLVTEKHVEGWDDPRMLTVSGLRRRGYTPAAIREFCLRIGVTKQDNIVEMGMLEACIRDDLNENAPR 341
Cdd:cd09287 164 GGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-272 |
4.93e-17 |
|
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: 77.91 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 28 HTRFPPEPNGYLHIGHAKSICLNFGIARD-----YQGQCNLRFDDTNPVKEDIEyvesikrdvqwlgfqwngevcyssdy 102
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPA-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 103 fdklhgyaieliekglayvdeltpeqmreyrgtlTEPGKNSP-FRDRSVDENLALFDkmkngefaegtaclrakidmasp 181
Cdd:cd00802 55 ----------------------------------NKKGENAKaFVERWIERIKEDVE----------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 182 fmvmrdpviyrikfahhhqtgdkwciypmYDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNISIECHPRQYEF 258
Cdd:cd00802 78 -----------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTF 128
|
250
....*....|....*
gi 1759052087 259 SRLNLEY-TVMSKRK 272
Cdd:cd00802 129 GRVMGADgTKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
29-120 |
6.37e-16 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 78.35 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 29 TRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVCYSSDYFDkLHG 108
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
|
90
....*....|...
gi 1759052087 109 YAIE-LIEKGLAY 120
Cdd:PRK05710 87 AALDrLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
26-117 |
1.78e-14 |
|
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: 73.00 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 26 SVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWNGEVC-------- 97
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpy 80
|
90 100
....*....|....*....|
gi 1759052087 98 YSSDYFDKLHGYAIELIEKG 117
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
28-94 |
4.96e-12 |
|
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: 62.56 E-value: 4.96e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759052087 28 HTRFPPEPnGYLHIGHAKSICLNFGIArdyqGQCNLRFDDTNPVK------EDIEYVESIKRDVQWLGFQWNG 94
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQ 68
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
226-272 |
1.76e-11 |
|
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: 61.02 E-value: 1.76e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1759052087 226 HSLCTLEFQDNRRLYDWVLDNISIECHPRQYEFSRLNLEYTVMSKRK 272
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
20-228 |
3.01e-10 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 62.84 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 20 ASGKHSSVHTRFPPEPNGYLHIGHAKSICLNFGIARDYQGQCNLRFDDTNPVKEDIEYVESIKRDVQWLGFQWN------ 93
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 94 GEVC-Y-SSDYFDKLHGYAIELIEKGLAY-----VDELtpEQMRE----------YRGTLT---------EPGKNSPF-- 145
Cdd:PLN02627 119 GEYGpYrQSERNAIYKQYAEKLLESGHVYpcfctDEEL--EAMKEeaelkklpprYTGKWAtasdeevqaELAKGTPYty 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759052087 146 RDRSVDENLALFDKMKNGEFAEGTaclrakiDMASPFMVMRdpviyrikfahhhQTGdkwciYPMYDFTHCISDALEGIT 225
Cdd:PLN02627 197 RFRVPKEGSVKIDDLIRGEVSWNT-------DTLGDFVLLR-------------SNG-----QPVYNFCVAVDDATMGIT 251
|
...
gi 1759052087 226 HSL 228
Cdd:PLN02627 252 HVI 254
|
|
| |
