|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
9-562 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1088.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 9 ESPVSEPSRPMHFLETLVAKDLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEF 88
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 89 IQAIQADIRWLGFDWAGDVRYASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPYRERSVEENRTLF 168
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 169 AAMRAGEFDDGAKVLRAKIDMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHR 248
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 249 PLYDWFIKNLPVPSEPHQYEFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTR 328
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 329 SDGTVDVAMLEHAVRDDLNNNAPRAMAVLNPLTVTLTNLSEDHREIVISPNHPQNEALGERELAFTRQVVIDADDFREEA 408
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 409 NKKFKRLVLGKRVRLRNAYVIEAYDVVKDAQGQIVEVLAKVIENTVGNDPEDGIKPKGVIQWVSKSEGGRATIRLYDRLF 488
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799124277 489 TQAEPEAGGDFMAVVNPNSLVVIeNAYVEPSLLAATPEQAFQFEREGYFVADRfDHSAEAPVFNRTIGLRDTWQ 562
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSLVIK-QGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSWA 552
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
38-561 |
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: 717.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 38 VVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFHQL 117
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 118 YDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKIDMASPNMNLR 197
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 198 DPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSEPHQYEFGRLNLNYT 277
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 278 VTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNAPRAMAVL 357
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 358 NPLTVTLTNLSEDHrEIVISPNHPQNEALGERELAFTRQVVIDADDFREEANKKFKRLVLGKRVRLRNAYVIEAYDVVKD 437
Cdd:TIGR00440 321 DPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 438 AQGQIVEVLAKVIENTVGNDPEDGIKPKGVIQWVSKSEGGRATIRLYDRLFTQAEPEAGGDFMAVVNPNSLvVIENAYVE 517
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFME 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1799124277 518 PSLLAATPEQAFQFEREGYFVADRFDHSAEAPVFNRTIGLRDTW 561
Cdd:TIGR00440 479 HSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
37-352 |
5.55e-143 |
|
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: 412.42 E-value: 5.55e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWaGDVRYASSYFHQ 116
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 LYDWACDLIDQGLAYVcdlsadearlyrgtltepgrnspyrersveenrtlfaamragefddgakvlrakidmaspnmnl 196
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 197 rdpilyrirrvvHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSePHQYEFGRLNLNY 276
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799124277 277 TVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNAPR 352
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-347 |
4.71e-133 |
|
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: 390.14 E-value: 4.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFHQ 116
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 LYDWACDLIDQGLAYVCDLSADEARLYRGTLtePGRNSPYRERSVEENRTLFA-AMRAGEFDDGAKVLRAKIDMASPnMN 195
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 196 LRDPILYRIR---RVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSEPHQYEFGRL 272
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799124277 273 NLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDG-TVDVAMLEHAVRDDLN 347
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
36-539 |
3.95e-129 |
|
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: 385.69 E-value: 3.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 36 KKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFH 115
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 116 QLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPY----RERSVEENrtlfAAMRA-GEfddgAKVLRAKI--- 187
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAaGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 188 -----DMAS-----PNMNLRDPILYRirrvvhhQTGsewviYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKN 257
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 258 L--PVPsephqyEFGRLNLNY----TVTSKRKlkqlvdDAVvagwddprmpTIAGMRRRGYSPAAIRTFCDMIGVTRSDG 331
Cdd:COG0008 223 LgwEPP------EFAHLPLILgpdgTKLSKRK------GAV----------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 332 TV--DVAMLEHAVrdDLNNNaPRAMAVLNPLTVTLTN------LSEDHREIVISPNHPQN--EALGERELAFTRQ----- 396
Cdd:COG0008 281 QEifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 397 ---------VVIDADDfrEEANKKfkrlvlgkrvRLRNAYVIEaydvvkdaqgqIVEVLAKVIENTVGNDPEDgikPKGV 467
Cdd:COG0008 358 selaelarfFFIERED--EKAAKK----------RLAPEEVRK-----------VLKAALEVLEAVETWDPET---VKGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799124277 468 IQWVSKSEGgratirLYDRLFtqaepeaggdFMAVVnpnslVVIENAYVEPSL---LAATPEQAFqFEREGYFVA 539
Cdd:COG0008 412 IHWVSAEAG------VKDGLL----------FMPLR-----VALTGRTVEPSLfdvLELLGKERV-FERLGYAID 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
9-562 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1088.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 9 ESPVSEPSRPMHFLETLVAKDLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEF 88
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 89 IQAIQADIRWLGFDWAGDVRYASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPYRERSVEENRTLF 168
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 169 AAMRAGEFDDGAKVLRAKIDMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHR 248
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 249 PLYDWFIKNLPVPSEPHQYEFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTR 328
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 329 SDGTVDVAMLEHAVRDDLNNNAPRAMAVLNPLTVTLTNLSEDHREIVISPNHPQNEALGERELAFTRQVVIDADDFREEA 408
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 409 NKKFKRLVLGKRVRLRNAYVIEAYDVVKDAQGQIVEVLAKVIENTVGNDPEDGIKPKGVIQWVSKSEGGRATIRLYDRLF 488
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799124277 489 TQAEPEAGGDFMAVVNPNSLVVIeNAYVEPSLLAATPEQAFQFEREGYFVADRfDHSAEAPVFNRTIGLRDTWQ 562
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSLVIK-QGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSWA 552
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
21-565 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 783.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 21 FLETLVAKDLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLG 100
Cdd:PRK14703 15 FITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 101 FDWAGDVRYASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPYRERSVEENRTLFAAMRAGEFDDGA 180
Cdd:PRK14703 95 FDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 181 KVLRAKIDMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNL-P 259
Cdd:PRK14703 175 HVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLgP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 260 VPSEPHQYEFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLE 339
Cdd:PRK14703 255 WPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 340 HAVRDDLNNNAPRAMAVLNPLTVTLTNLSEDHREIVISPNHPQN-EALGERELAFTRQVVIDADDFREEANKKFKRLVLG 418
Cdd:PRK14703 335 FAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 419 KRVRLRNAYVIEAYDVVKDAQGQIVEVLAKVIENTVGNDPEdGIKPKGVIQWVSKSEGGRATIRLYDRLFTQAEPEAG-G 497
Cdd:PRK14703 415 REVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAAdE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799124277 498 DFMAVVNPNSLVVIENaYVEPSLLAATPEQAFQFEREGYFVADRFDHSAEAPVFNRTIGLRDTWQEGA 565
Cdd:PRK14703 494 DFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
38-561 |
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: 717.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 38 VVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFHQL 117
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 118 YDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKIDMASPNMNLR 197
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 198 DPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSEPHQYEFGRLNLNYT 277
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 278 VTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNAPRAMAVL 357
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 358 NPLTVTLTNLSEDHrEIVISPNHPQNEALGERELAFTRQVVIDADDFREEANKKFKRLVLGKRVRLRNAYVIEAYDVVKD 437
Cdd:TIGR00440 321 DPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 438 AQGQIVEVLAKVIENTVGNDPEDGIKPKGVIQWVSKSEGGRATIRLYDRLFTQAEPEAGGDFMAVVNPNSLvVIENAYVE 517
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFME 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1799124277 518 PSLLAATPEQAFQFEREGYFVADRFDHSAEAPVFNRTIGLRDTW 561
Cdd:TIGR00440 479 HSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
37-564 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 557.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGfdWAG-DVRYASSYFH 115
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPfKITYTSDYFQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 116 QLYDWACDLIDQGLAYVCDLSADEARLYRgtltEPGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKIDMASPNMN 195
Cdd:PLN02859 342 ELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 196 LRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVpSEPHQYEFGRLNLN 275
Cdd:PLN02859 418 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 276 YTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGT-VDVAMLEHAVRDDLNNNAPRAM 354
Cdd:PLN02859 497 NTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSlIRMDRLEHHIREELNKTAPRTM 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 355 AVLNPLTVTLTNLSEDHREIV---ISPNHPQNEALGERELAFTRQVVIDADDFREEANKKFKRLVLGKRVRLRNAYVIEA 431
Cdd:PLN02859 577 VVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKC 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 432 YDVV-KDAQGQIVEVLAKVientvgnDPEDGIKPKGVIQWVSKSEGG----RATIRLYDRLFTQAEPEAGGDFMAVVNPN 506
Cdd:PLN02859 657 TDVVlADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAEPSPGveplKVEVRLFDKLFLSENPAELEDWLEDLNPQ 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799124277 507 SLVVIENAYVEPSLLAATPEQAFQFEREGYFVADRfDHSAEAPVFNRTIGLRDTWQEG 564
Cdd:PLN02859 730 SKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDK-DSTPEKLVFNRTVTLKDSYGKG 786
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
41-565 |
2.34e-150 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 444.04 E-value: 2.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 41 RFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGF--DWagdVRYASSYFHQLY 118
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 119 DWACDLIDQGLAYVCDLSADEARLYRgtltEPGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKIDMASPNMNLRD 198
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 199 PILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVpSEPHQYEFGRLNLNYTV 278
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 279 TSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNAPRAMAVLN 358
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 359 PLTVTLTNLseDHREIVISPNHPQNEALGERELAFTRQVVIDADDFR-EEANKKFKRLVLGKRV---RLRNAYVIEAYDV 434
Cdd:PTZ00437 367 PIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRVvglKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 435 vkDAQGQIVEVLAKVientvgnDPEDGIKPKGVIQWVSKSEGGRATIRLYDRLFTQAEPEAGGDFMAVVNPNSLVViENA 514
Cdd:PTZ00437 445 --DAAGQPSVIHVDI-------DFERKDKPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVV-SHG 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1799124277 515 YVEPSLLAATPEQAFQFEREGYFVADRfDHSAEAPVFNRTIGLRDTWQEGA 565
Cdd:PTZ00437 515 YAEKGIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLREDKEKAT 564
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
37-352 |
5.55e-143 |
|
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: 412.42 E-value: 5.55e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWaGDVRYASSYFHQ 116
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 LYDWACDLIDQGLAYVcdlsadearlyrgtltepgrnspyrersveenrtlfaamragefddgakvlrakidmaspnmnl 196
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 197 rdpilyrirrvvHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSePHQYEFGRLNLNY 276
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799124277 277 TVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNAPR 352
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-347 |
4.71e-133 |
|
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: 390.14 E-value: 4.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFHQ 116
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 LYDWACDLIDQGLAYVCDLSADEARLYRGTLtePGRNSPYRERSVEENRTLFA-AMRAGEFDDGAKVLRAKIDMASPnMN 195
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 196 LRDPILYRIR---RVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSEPHQYEFGRL 272
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799124277 273 NLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDG-TVDVAMLEHAVRDDLN 347
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
36-539 |
3.95e-129 |
|
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: 385.69 E-value: 3.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 36 KKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFH 115
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 116 QLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEPGRNSPY----RERSVEENrtlfAAMRA-GEfddgAKVLRAKI--- 187
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAaGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 188 -----DMAS-----PNMNLRDPILYRirrvvhhQTGsewviYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKN 257
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 258 L--PVPsephqyEFGRLNLNY----TVTSKRKlkqlvdDAVvagwddprmpTIAGMRRRGYSPAAIRTFCDMIGVTRSDG 331
Cdd:COG0008 223 LgwEPP------EFAHLPLILgpdgTKLSKRK------GAV----------TVSGLRRRGYLPEAIRNYLALLGWSKSDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 332 TV--DVAMLEHAVrdDLNNNaPRAMAVLNPLTVTLTN------LSEDHREIVISPNHPQN--EALGERELAFTRQ----- 396
Cdd:COG0008 281 QEifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 397 ---------VVIDADDfrEEANKKfkrlvlgkrvRLRNAYVIEaydvvkdaqgqIVEVLAKVIENTVGNDPEDgikPKGV 467
Cdd:COG0008 358 selaelarfFFIERED--EKAAKK----------RLAPEEVRK-----------VLKAALEVLEAVETWDPET---VKGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799124277 468 IQWVSKSEGgratirLYDRLFtqaepeaggdFMAVVnpnslVVIENAYVEPSL---LAATPEQAFqFEREGYFVA 539
Cdd:COG0008 412 IHWVSAEAG------VKDGLL----------FMPLR-----VALTGRTVEPSLfdvLELLGKERV-FERLGYAID 464
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
29-541 |
5.28e-107 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 336.70 E-value: 5.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 29 DLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDwaGD-V 107
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIK--YDaV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 108 RYASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEpgrnSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKI 187
Cdd:PLN02907 283 TYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 188 DMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPsEPHQY 267
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 268 EFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRsdgtvDVAMLEHAVRDDLN 347
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLMEWDKLWTIN 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 348 NN-----APRAMAVLNP--LTVTLTNLSEDhREIVISPNHPQNEALGERELAFTRQVVIDADDfrEEANKKfkrlvlGKR 420
Cdd:PLN02907 513 KKiidpvCPRHTAVLKEgrVLLTLTDGPET-PFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEAISE------GEE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 421 VRLR---NAYVIEaydVVKDAQGQIVEVLAKVientvgnDPEDGIK-PKGVIQWVSK-SEGGRATIRLYDRLFTQAEPEA 495
Cdd:PLN02907 584 VTLMdwgNAIIKE---ITKDEGGAVTALSGEL-------HLEGSVKtTKLKLTWLPDtNELVPLSLVEFDYLITKKKLEE 653
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1799124277 496 GGDFMAVVNPNSLVVIEnAYVEPSLLAATPEQAFQFEREGYFVADR 541
Cdd:PLN02907 654 DDNFLDVLNPCTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCDA 698
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
29-406 |
5.00e-96 |
|
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: 303.28 E-value: 5.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 29 DLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWaGDVR 108
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW-DEVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 109 YASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTltepGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKID 188
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 189 MASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDH--RPLYDWFIKNLPVPsEPHQ 266
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrrKQEYIYRYFGWEPP-EFIH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 267 YEFGRLNLNYTVTSKRKLKQLVDDAVVaGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDL 346
Cdd:TIGR00463 319 WGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKII 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 347 NNNAPRAMAVLNPLTVTLTNLSEdhREIVISPNHPQNEALGERELAFTRQVVIDADDFRE 406
Cdd:TIGR00463 398 DEEARRYFFIWNPVKIEIVGLPE--PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEE 455
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
15-540 |
8.59e-96 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 304.19 E-value: 8.59e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 15 PSRPMHflETLVAKDLEEGKikkVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQA 94
Cdd:PTZ00402 35 NANEEN--DKLQLTNAEEGK---VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 95 DIRWLGFDWAGDVRYASSYFHQLYDWACDLIDQGLAYvCDLSADEARL---YRGTLTEpgrnspYRERSVEENRTLFAAM 171
Cdd:PTZ00402 110 DLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAY-CDKTPREEMQkcrFDGVPTK------YRDISVEETKRLWNEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 172 RAGEFDDGAKVLRAKIDMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLY 251
Cdd:PTZ00402 183 KKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 252 DWFIKNLPVpSEPHQYEFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDG 331
Cdd:PTZ00402 263 YWFCDALGI-RKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 332 TVDVAMLEHAVRDDLNNNAPRAMAVLNPLTVTLTNLSEDHREIVISPNHPQNEALGERELAFTRQVVIDADDfreeankk 411
Cdd:PTZ00402 342 FMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAED-------- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 412 FKRLVLGKRVRLR---NAYvieaydvVKDAQGQIVEVLakVIENTVGNDPE-DGIKPKGVIQWVSKSEGGRA-TIRLYDR 486
Cdd:PTZ00402 414 VALLKEGDEVTLMdwgNAY-------IKNIRRSGEDAL--ITDADIVLHLEgDVKKTKFKLTWVPESPKAEVmELNEYDH 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1799124277 487 LFTQAEPEAGGDFMAVVNPNSLVVIEnAYVEPSLLAATPEQAFQFEREGYFVAD 540
Cdd:PTZ00402 485 LLTKKKPDPEESIDDIIAPVTKYTQE-VYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
28-536 |
1.12e-92 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 294.84 E-value: 1.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 28 KDLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPE-KESD-EFIQAIQADIRWLGFDWAg 105
Cdd:PRK04156 92 PPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtKRPDpEAYDMILEDLKWLGVKWD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 106 DVRYASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRgtltEPGRNSPYRERSVEENRTLFAAMRAGEFDDGAKVLRA 185
Cdd:PRK04156 171 EVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 186 KIDMASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFED----HRPLYDWFIKNLPVp 261
Cdd:PRK04156 247 KTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDYFGWEYPE- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 262 sephQYEFGRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHA 341
Cdd:PRK04156 326 ----TIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAI 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 342 VRDDLNNNAPRAMAVLNPLTVTLtnlsEDHREIVIS-PNHPQNEALGERELAFTRQVVIDADDFREeankkfkrlvLGKR 420
Cdd:PRK04156 402 NRKLIDPIANRYFFVRDPVELEI----EGAEPLEAKiPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKM 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 421 VRLRNAYVIEAYDVVKDAqgqivevlAKVIentvGNDPEDGIKPKG-VIQWVSKSEGGRATIRlydrlftqaEPEAGgdf 499
Cdd:PRK04156 468 VRLMDLFNVEITGVSVDK--------ARYH----SDDLEEARKNKApIIQWVPEDESVPVRVL---------KPDGG--- 523
|
490 500 510
....*....|....*....|....*....|....*..
gi 1799124277 500 mavvnpnslvvIENAYVEPSLLAATPEQAFQFEREGY 536
Cdd:PRK04156 524 -----------DIEGLAEPDVADLEVDDIVQFERFGF 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
30-555 |
1.53e-92 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 293.45 E-value: 1.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 30 LEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDwAGDVRY 109
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 110 ASSYFHQLYDWACDLIDQGLAYVCDLSADEARLYRGTLTEpgrnSPYRERSVEENRTLFAAMRAGEFDDGAKVLRAKIDM 189
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 190 ASPNMNLRDPILYRIRRVVHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVpSEPHQYEF 269
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL-RRPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 270 GRLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNN 349
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 350 APRAMAV--LNPLTVTLTNLSEDHREIVISPN-HPQNEALGERELAFTRQVVIDADDfreeankkFKRLVLGKRVRLRNA 426
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEEADFAFSETDcHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 427 YVIEAYDVVKDAQGQIVevlakvientvgndPEDGIK-PKGVIQWVSK-SEGGRATIRLYDRLFTQAEPEAGGDFMAVVN 504
Cdd:PLN03233 390 GVIEISKIDGDLEGHFI--------------PDGDFKaAKKKISWIADvSDNIPVVLSEFDNLIIKEKLEEDDKFEDFIN 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1799124277 505 PNSLVVIEnAYVEPSLLAATPEQAFQFEREGYFVADRFDHSAEAPVFNRTI 555
Cdd:PLN03233 456 PDTLAETD-VIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPLILFMI 505
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
350-540 |
1.03e-64 |
|
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: 209.05 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 350 APRAMAVLNPLTVTLTNLSEDHREIVISPNHPQNEALGERELAFTRQVVIDADDfreeankkFKRLVLGKRVRLRNAYVI 429
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 430 EAYDVVKDAQGQIVEVLAKVIENTVGNDpedgIKPKG-VIQWVSKSEGGRATIRLYDRLFTqaePEAGGDFmaVVNPNSL 508
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFK---DEDDADF--LLNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1799124277 509 VVIENAYVEPSLLAATPEQAFQFEREGYFVAD 540
Cdd:pfam03950 144 KVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
37-348 |
2.14e-58 |
|
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: 194.61 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYFHQ 116
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 LYDWACDLIDQGlayvcdlsadearlyrgtltepgrnspyrersveenrtlfaamragefddgakvlrakidmaspnmnl 196
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 197 rdpilyrirrvvhhqtgsewvIYPTYDFAHGQGDAIEGITHSICSLEFEDHRPLYDWFIKNLPVPSePHQYEFGRLNLNY 276
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEP-PRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 277 -TVTSKRKLKqlvddavvagwddprmPTIAGMRRRGYSPAAIRTFCDMIGVTRSDG-----------------------T 332
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGhelftleemiaafsvervnsadaT 214
|
330
....*....|....*.
gi 1799124277 333 VDVAMLEHAVRDDLNN 348
Cdd:cd00418 215 FDWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
37-352 |
3.55e-42 |
|
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: 151.35 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPE-KESD-EFIQAIQADIRWLGFDWAgDVRYASSYF 114
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtKRPDpEAYDMIPEDLEWLGVKWD-EVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 115 HQLYDWACDLIDQGLAYVcdlsadearlyrgtltepgrnspyrersveenrtlfaamragefddgakvlrakidmaspnm 194
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 195 nlrdpilyrirrvvHHQTGSEWVIYPTYDFAHGQGDAIEGITHSICSLEFED----HRPLYDWFIKNLPVpsephQYEFG 270
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYFGWEYPE-----TIHWG 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 271 RLNLNYTVTSKRKLKQLVDDAVVAGWDDPRMPTIAGMRRRGYSPAAIRTFCDMIGVTRSDGTVDVAMLEHAVRDDLNNNA 350
Cdd:cd09287 159 RLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRA 238
|
..
gi 1799124277 351 PR 352
Cdd:cd09287 239 NR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
39-155 |
1.56e-20 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 92.22 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 39 VTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWAGDVRYASSYfHQLY 118
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR-HDAY 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1799124277 119 DWACD-LIDQGLAYVCDLS-----------ADEARLYRGT---LTEPGRNSP 155
Cdd:PRK05710 86 RAALDrLRAQGLVYPCFCSrkeiaaaapapPDGGGIYPGTcrdLLHGPRNPP 137
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
37-325 |
1.27e-16 |
|
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: 79.55 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 37 KVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFIQAIQADIRWLGFDWagdvryassyfhq 116
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 117 lydwacdliDQGlayvcdlsadearlyrgtLTEPGRNSPYRERSveenrtlfaamRAGEFDDGAKVLRAKIDmaspnmnl 196
Cdd:cd00808 68 ---------DEG------------------PDVGGPYGPYRQSE-----------RLEIYRKYAEKLLEKGD-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 197 rdpilyrirrvvhhqtGsewviYPTYDFAHGQGDAIEGITHSIcslEFEDHRP-------LYDWFIKNLPVpsephqyeF 269
Cdd:cd00808 102 ----------------G-----FPTYHLANVVDDHLMGITHVI---RGEEHLSstpkqilLYEALGWEPPK--------F 149
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 270 GRLNLNYTVT----SKRKLKQLVDDavvagwddprmptiagMRRRGYSPAAIRTFCDMIG 325
Cdd:cd00808 150 AHLPLILNPDgkklSKRKGDTSISD----------------YREEGYLPEALLNYLALLG 193
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
10-139 |
8.07e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 67.84 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 10 SPVSEPSRPMHFLETLVAKDLEEGKIKKVVTRFPPEPNGYLHVGHAKSICLNFGLAQRFGGDCHLRFDDTNPEKESDEFI 89
Cdd:PLN02627 18 PPFLRRSRSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799124277 90 QAIQADIRWLGFDW------AGDV-RYASSYFHQLY-DWACDLIDQGLAYVCDLSADE 139
Cdd:PLN02627 98 EAVLRDLKWLGLDWdegpdvGGEYgPYRQSERNAIYkQYAEKLLESGHVYPCFCTDEE 155
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
39-106 |
1.06e-09 |
|
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: 57.10 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 39 VTRFPPEPNGYLHVGHAKSICLNFGLAQ-----RFGGDCHLRFDDTN-------------PEKESDEFIQAIQADIRWLg 100
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQayrklGYKVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM- 79
|
....*.
gi 1799124277 101 FDWAGD 106
Cdd:cd00802 80 FLQAAD 85
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
39-126 |
2.04e-09 |
|
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: 55.24 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799124277 39 VTRFPPEPnGYLHVGHAKSICLNFGLAqrfgGDCHLRFDDTNPEK------ESDEFIQAIQADIRWLGFDWAGDVRyass 112
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRE---- 71
|
90
....*....|....
gi 1799124277 113 yfhqLYDWACDLID 126
Cdd:cd02156 72 ----LYRWVKDNIT 81
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
237-283 |
1.24e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 44.45 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1799124277 237 HSICSLEFEDHRPLYDWFIKNLPVPSEPHQYEFGRLNLNYTVTSKRK 283
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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|
| |
