|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-559 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1016.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 1 MEETNARSNFIWDAIEKDLEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEA 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 81 IKRDIHWLGFHWTGGEFYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKNSPWRDRPAEESLDLFRRM 160
Cdd:PRK05347 84 IKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 161 KAGEFPEGSKTLRMKIDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLY 240
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 241 DWVVEKSADmlPARPRQIEFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKA 320
Cdd:PRK05347 244 DWVLDNLPI--PPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 321 DSTVDYAVLEHCVRDVLGETSLRAMAVLNPLKVVLTNWPEGETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPV 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 401 KKYQRMFPGNEVRLKGAYIVRCDDCIKDADGNIVEVHCTVDMDSFSGSAGADRKIKGkTLHWVPVNDCIPFEARLYEPLL 480
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKG-TIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2028624937 481 NddvadeEEEEVDKKDFISRLNPESLKVCRGYAENVIAQAETGTSFQFLRTGYFCKDPDSTVGLPVYNRTVGLRDTFAK 559
Cdd:PRK05347 481 T------VPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-557 |
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: 652.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 27 IHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDKC 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 107 YEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKNSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMKIDMASPNIVMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 187 DPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKSAdmLPARPRQIEFSRLNMT 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH--IFPRPAQYEFSRLNLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 267 GTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGETSLRAMA 346
Cdd:TIGR00440 239 GTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 347 VLNPLKVVLTNWpEGETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPVKKYQRMFPGNEVRLKGAYIVRCDDCI 426
Cdd:TIGR00440 319 VIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 427 KDADGNIVEVHCTVDMDSFSGSAGADRKIKGkTLHWVPVNDCIPFEARLYEPLLNddvadeEEEEVDKKDFISRLNPESL 506
Cdd:TIGR00440 398 KDAAGKITTIFCTYDNKTLGKEPADGRKVKG-VIHWVSASSKYPTETRLYDRLFK------VPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2028624937 507 KVCRGYAENVIAQAETGTSFQFLRTGYFCKDP-DSTVGLPVYNRTVGLRDTF 557
Cdd:TIGR00440 471 VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-343 |
2.63e-126 |
|
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: 370.04 E-value: 2.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWtGGEFYASDYYDK 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 106 CYEIAEEWIRRGLAYVdelskdemreyrgtltepgknspwrdrpaeesldlfrrmkagefpegsktlrmkidmaspnivm 185
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 186 rdpamyrilykeHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKsadMLPARPRQIEFSRLNM 265
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDA---LRLYRPHQWEFSRLNL 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028624937 266 TGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGETSLR 343
Cdd:cd00807 161 TYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-337 |
2.64e-122 |
|
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: 362.79 E-value: 2.64e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDK 105
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 106 CYEIAEEWIRRGLAYVDELSKDEMREYRGTLtePGKNSPWRDRPAEESLDLFRR-MKAGEFPEGSKTLRMKIDMASPnIV 184
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 185 MRDPAMYRILYKE---HWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEksADMLPARPRQIEFS 261
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYD--ALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2028624937 262 RLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADS-TVDYAVLEHCVRDVL 337
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKL 312
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-413 |
1.24e-111 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 340.62 E-value: 1.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 25 TEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYD 104
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 105 KCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKN----SPWRDRPAEEsldLFRRMKAGEfpegSKTLRMKI---- 176
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 177 ----DMAS-----PNIVMRDPamyrILYKEHwrtGtkwciYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKs 247
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDP----VLYRAD---G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 248 admLPARPRqiEFSRLNMT----GTVMSKRYlrqlvegGYVagwddprmpTLSAMRRRGYPAMAIRNFVDTIGMSKADST 323
Cdd:COG0008 223 ---LGWEPP--EFAHLPLIlgpdGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 324 V--DYAVLEHCVRdvLGETSlRAMAVLNPLKVVLTNWP---EGETKTVTLENHPDHPEMG-----ERTLTFGRE------ 387
Cdd:COG0008 282 EifSLEELIEAFD--LDRVS-RSPAVFDPVKLVWLNGPyirALDDEELAELLAPELPEAGiredlERLVPLVREraktls 358
|
410 420 430
....*....|....*....|....*....|....
gi 2028624937 388 --------LYIEQDDfmEVPVKKyqrMFPGNEVR 413
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK---RLAPEEVR 387
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-559 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1016.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 1 MEETNARSNFIWDAIEKDLEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEA 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 81 IKRDIHWLGFHWTGGEFYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKNSPWRDRPAEESLDLFRRM 160
Cdd:PRK05347 84 IKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 161 KAGEFPEGSKTLRMKIDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLY 240
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 241 DWVVEKSADmlPARPRQIEFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKA 320
Cdd:PRK05347 244 DWVLDNLPI--PPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 321 DSTVDYAVLEHCVRDVLGETSLRAMAVLNPLKVVLTNWPEGETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPV 400
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 401 KKYQRMFPGNEVRLKGAYIVRCDDCIKDADGNIVEVHCTVDMDSFSGSAGADRKIKGkTLHWVPVNDCIPFEARLYEPLL 480
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKG-TIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2028624937 481 NddvadeEEEEVDKKDFISRLNPESLKVCRGYAENVIAQAETGTSFQFLRTGYFCKDPDSTVGLPVYNRTVGLRDTFAK 559
Cdd:PRK05347 481 T------VPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
5-565 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 794.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 5 NARSNFIWDAIEKDLEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRD 84
Cdd:PRK14703 10 LVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 85 IHWLGFHWTGGEFYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKNSPWRDRPAEESLDLFRRMKAGE 164
Cdd:PRK14703 90 VRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 165 FPEGSKTLRMKIDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVV 244
Cdd:PRK14703 170 FPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 245 EKSADmLPARPRQIEFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTV 324
Cdd:PRK14703 250 DHLGP-WPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 325 DYAVLEHCVRDVLGETSLRAMAVLNPLKVVLTNWPEGETKTVTLENHP-DHPEMGERTLTFGRELYIEQDDFMEVPVKKY 403
Cdd:PRK14703 329 DIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPhDVPKEGSRKVPFTRELYIERDDFSEDPPKGF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 404 QRMFPGNEVRLKGAYIVRCDDCIKDADGNIVEVHCTVDMDSFSGsAGADRKIKGkTLHWVPVNDCIPFEARLYEPLLndd 483
Cdd:PRK14703 409 KRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKG-EDTGRKAAG-VIHWVSAKHALPAEVRLYDRLF--- 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 484 vaDEEEEEVDKKDFISRLNPESLKVCRGYAENVIAQAETGTSFQFLRTGYFCKDP-DSTVGLPVYNRTVGLRDTFAKQAT 562
Cdd:PRK14703 484 --KVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGARAR 561
|
...
gi 2028624937 563 QQA 565
Cdd:PRK14703 562 EAA 564
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-557 |
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: 652.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 27 IHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDKC 106
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 107 YEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKNSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMKIDMASPNIVMR 186
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 187 DPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKSAdmLPARPRQIEFSRLNMT 266
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH--IFPRPAQYEFSRLNLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 267 GTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGETSLRAMA 346
Cdd:TIGR00440 239 GTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 347 VLNPLKVVLTNWpEGETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPVKKYQRMFPGNEVRLKGAYIVRCDDCI 426
Cdd:TIGR00440 319 VIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 427 KDADGNIVEVHCTVDMDSFSGSAGADRKIKGkTLHWVPVNDCIPFEARLYEPLLNddvadeEEEEVDKKDFISRLNPESL 506
Cdd:TIGR00440 398 KDAAGKITTIFCTYDNKTLGKEPADGRKVKG-VIHWVSASSKYPTETRLYDRLFK------VPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2028624937 507 KVCRGYAENVIAQAETGTSFQFLRTGYFCKDP-DSTVGLPVYNRTVGLRDTF 557
Cdd:TIGR00440 471 VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
13-559 |
3.13e-173 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 510.07 E-value: 3.13e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 13 DAIEKDLEE--GRyteIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLG- 89
Cdd:PLN02859 252 EILEKHLKAtgGK---VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGw 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 90 --FHWTggefYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRgtltEPGKNSPWRDRPAEESLDLFRRMKAGEFPE 167
Cdd:PLN02859 329 epFKIT----YTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 168 GSKTLRMKIDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEkS 247
Cdd:PLN02859 401 GKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLD-S 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 248 ADMLpaRPRQIEFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKAD-STVDY 326
Cdd:PLN02859 480 LGLY--QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 327 AVLEHCVRDVLGETSLRAMAVLNPLKVVLTNWPEGETKTVTLENHPDHPEMGERT---LTFGRELYIEQDDFMEVPVKKY 403
Cdd:PLN02859 558 DRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAfykVPFSRVVYIERSDFRLKDSKDY 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 404 QRMFPGNEVRLKGAYIVRCDDCI-KDADGNIVEVHCTVDmdsfsgsagADRKIKGK-TLHWV----PVNDCIPFEARLYE 477
Cdd:PLN02859 638 YGLAPGKSVLLRYAFPIKCTDVVlADDNETVVEIRAEYD---------PEKKTKPKgVLHWVaepsPGVEPLKVEVRLFD 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 478 PLLNddvadeEEEEVDKKDFISRLNPESLKVCRG-YAENVIAQAETGTSFQFLRTGYFCKDPDSTVGLPVYNRTVGLRDT 556
Cdd:PLN02859 709 KLFL------SENPAELEDWLEDLNPQSKEVISGaYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDS 782
|
...
gi 2028624937 557 FAK 559
Cdd:PLN02859 783 YGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
30-561 |
1.01e-147 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 437.11 E-value: 1.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 30 RFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFH--WTGgefYASDYYDKCY 107
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdWVT---FSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 108 EIAEEWIRRGLAYVDELSKDEMREYRgtltEPGKNSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMKIDMASPNIVMRD 187
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 188 PAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKsadMLPARPRQIEFSRLNMTG 267
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEE---LNLWRPHVWEFSRLNVTG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 268 TVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGETSLRAMAV 347
Cdd:PTZ00437 285 SLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 348 LNPLKVVLTNWpEGEtKTVTLENHPDHPEMGERTLTFGRELYIEQDDF-MEVPVKKYQRMFPGNE-VRLKGAYIVRCDDC 425
Cdd:PTZ00437 365 IDPIKVVVDNW-KGE-REFECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 426 IKDADGNIVEVHCTVDMdsfsgsagaDRKIKGKT-LHWVPVNDCIPFEARLYEPLLNddvadeEEEEVDKKDFISRLNPE 504
Cdd:PTZ00437 443 EVDAAGQPSVIHVDIDF---------ERKDKPKTnISWVSATACTPVEVRLYNALLK------DDRAAIDPEFLKFIDED 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2028624937 505 SLKVCRGYAENVIAQAETGTSFQFLRTGYFCKDPDSTVGLPVYNRTVGLRDTFAKQA 561
Cdd:PTZ00437 508 SEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKAT 564
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-343 |
2.63e-126 |
|
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: 370.04 E-value: 2.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWtGGEFYASDYYDK 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 106 CYEIAEEWIRRGLAYVdelskdemreyrgtltepgknspwrdrpaeesldlfrrmkagefpegsktlrmkidmaspnivm 185
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 186 rdpamyrilykeHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKsadMLPARPRQIEFSRLNM 265
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDA---LRLYRPHQWEFSRLNL 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028624937 266 TGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGETSLR 343
Cdd:cd00807 161 TYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-337 |
2.64e-122 |
|
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: 362.79 E-value: 2.64e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDK 105
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 106 CYEIAEEWIRRGLAYVDELSKDEMREYRGTLtePGKNSPWRDRPAEESLDLFRR-MKAGEFPEGSKTLRMKIDMASPnIV 184
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 185 MRDPAMYRILYKE---HWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEksADMLPARPRQIEFS 261
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYD--ALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2028624937 262 RLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADS-TVDYAVLEHCVRDVL 337
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKL 312
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-413 |
1.24e-111 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 340.62 E-value: 1.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 25 TEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYD 104
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 105 KCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEPGKN----SPWRDRPAEEsldLFRRMKAGEfpegSKTLRMKI---- 176
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 177 ----DMAS-----PNIVMRDPamyrILYKEHwrtGtkwciYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKs 247
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDP----VLYRAD---G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 248 admLPARPRqiEFSRLNMT----GTVMSKRYlrqlvegGYVagwddprmpTLSAMRRRGYPAMAIRNFVDTIGMSKADST 323
Cdd:COG0008 223 ---LGWEPP--EFAHLPLIlgpdGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 324 V--DYAVLEHCVRdvLGETSlRAMAVLNPLKVVLTNWP---EGETKTVTLENHPDHPEMG-----ERTLTFGRE------ 387
Cdd:COG0008 282 EifSLEELIEAFD--LDRVS-RSPAVFDPVKLVWLNGPyirALDDEELAELLAPELPEAGiredlERLVPLVREraktls 358
|
410 420 430
....*....|....*....|....*....|....
gi 2028624937 388 --------LYIEQDDfmEVPVKKyqrMFPGNEVR 413
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK---RLAPEEVR 387
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
16-547 |
1.37e-101 |
|
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: 317.92 E-value: 1.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 16 EKDLEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTgG 95
Cdd:TIGR00463 83 LRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-E 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 96 EFYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRgtltEPGKNSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMK 175
Cdd:TIGR00463 162 VVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELR----NRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 176 IDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEY--EIHRPLYDWvveksaDMLPA 253
Cdd:TIGR00463 238 TDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIY------RYFGW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 254 RPRQI---EFSRLNMTGTVMSKRYLRQLVEGGYVaGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLE 330
Cdd:TIGR00463 312 EPPEFihwGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 331 HCVRDVLGETSLRAMAVLNPLKVVLTNWPegETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPvkkyqrmfpgN 410
Cdd:TIGR00463 391 ALNRKIIDEEARRYFFIWNPVKIEIVGLP--EPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------E 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 411 EVRLKGAyivrcddcikdadGNIV--EVHCTVDMDSFSGsagaDRKIKGKTLHWVPVNDCIPFEArlyepllnddvadee 488
Cdd:TIGR00463 459 PVRLMDA-------------VNVIysKKELRYHSEGLEG----ARKLGKSIIHWLPAKDAVKVKV--------------- 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2028624937 489 eeevdkkdfisrLNPESLKVcRGYAENVIAQAETGTSFQFLRTGYFCKDPDSTVGLPVY 547
Cdd:TIGR00463 507 ------------IMPDASIV-EGVIEADASELEVGDVVQFERFGFARLDSADKDGMVFV 552
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
29-536 |
5.44e-100 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 314.10 E-value: 5.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 29 TRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPA--KEDTEYVEAIKRDIHWLGFHWTGgEFYASDYYDKC 106
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE-VVIQSDRLEIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 107 YEIAEEWIRRGLAYVDELSKDEMREYRgtltEPGKNSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMKIDMASPNIVMR 186
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 187 DPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEY----EIHRPLYD---WVVeksadmlparPRQIE 259
Cdd:PRK04156 259 DWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYDyfgWEY----------PETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 260 FSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLGE 339
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 340 TSLRAMAVLNPLKVVLTNWPEGETKtvtLENHPDHPEMGERTLTFGRELYIEQDDFMEVpvkkyqrmfpGNEVRLKGAYI 419
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRLMDLFN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 420 VRcddcIKDADGNIVEVHcTVDMDsfsgsagADRKIKGKTLHWVPVNDCIPFEArlyepllnddvadeeeeevdkkdfis 499
Cdd:PRK04156 476 VE----ITGVSVDKARYH-SDDLE-------EARKNKAPIIQWVPEDESVPVRV-------------------------- 517
|
490 500 510
....*....|....*....|....*....|....*..
gi 2028624937 500 rLNPESLKVcRGYAENVIAQAETGTSFQFLRTGyFCK 536
Cdd:PRK04156 518 -LKPDGGDI-EGLAEPDVADLEVDDIVQFERFG-FVR 551
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
16-538 |
1.79e-98 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 314.35 E-value: 1.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 16 EKDLEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHW--- 92
Cdd:PLN02907 203 EVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYdav 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 93 TggefYASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEpgknSPWRDRPAEESLDLFRRMKAGEfPEGSK-T 171
Cdd:PLN02907 283 T----YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGS-ERGLQcC 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 172 LRMKIDMASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEksadML 251
Cdd:PLN02907 354 VRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE----DM 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 252 PARPRQI-EFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLE 330
Cdd:PLN02907 430 GLRKVHIwEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLW 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 331 HCVRDVLGETSLRAMAVLNPLKVVLT--NWPEgETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFMEVPVkkyqrmfp 408
Cdd:PLN02907 510 TINKKIIDPVCPRHTAVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISE-------- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 409 GNEVRLK--GAYIVRcdDCIKDADGNIVEVHCTVDMdsfsgsAGADRKIKGKtLHWVP-VNDCIPFEarlyepLLNDDVA 485
Cdd:PLN02907 581 GEEVTLMdwGNAIIK--EITKDEGGAVTALSGELHL------EGSVKTTKLK-LTWLPdTNELVPLS------LVEFDYL 645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2028624937 486 DEEEEEVDKKDFISRLNPESLKVCRGYAENVIAQAETGTSFQFLRTGYF-CKDP 538
Cdd:PLN02907 646 ITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYrCDAP 699
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
20-539 |
1.18e-96 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 306.50 E-value: 1.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 20 EEGRyteIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYA 99
Cdd:PTZ00402 49 EEGK---VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 100 SDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTltepGKNSPWRDRPAEESLDLFRRMKAGEfPEGSKT-LRMKIDM 178
Cdd:PTZ00402 126 SDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 179 ASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVveksADMLPARPRQI 258
Cdd:PTZ00402 201 DNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWF----CDALGIRKPIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 259 E-FSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVL 337
Cdd:PTZ00402 277 EdFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQIL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 338 GETSLRAMAVLNPLKVVLTnwPEGETKTVTLEN--HPDHPEMGERTLTFGRELYIEQDDfmeVPVKKyqrmfPGNEVRLK 415
Cdd:PTZ00402 357 DPSVPRYTVVSNTLKVRCT--VEGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAED---VALLK-----EGDEVTLM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 416 ---GAYIVrcDDCIKDADGNIVEVHCTVDMDsfsgsaGADRKIKGKtLHWVPVND-CIPFEARLYEPLLNDDVADEEEEE 491
Cdd:PTZ00402 427 dwgNAYIK--NIRRSGEDALITDADIVLHLE------GDVKKTKFK-LTWVPESPkAEVMELNEYDHLLTKKKPDPEESI 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2028624937 492 VDKKDFISRLNPESlkvcrgYAENVIAQAETGTSFQFLRTGYFCKDPD 539
Cdd:PTZ00402 498 DDIIAPVTKYTQEV------YGEEALSVLKKGDIIQLERRGYYIVDDV 539
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-394 |
1.60e-81 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 264.56 E-value: 1.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 19 LEEGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHwTGGEFY 98
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 99 ASDYYDKCYEIAEEWIRRGLAYVDELSKDEMREYRGTLTEpgknSPWRDRPAEESLDLFRRMKAGEFPEGSKTLRMKIDM 178
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 179 ASPNIVMRDPAMYRILYKEHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVeKSADMlpARPRQI 258
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQ-KALGL--RRPRIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 259 EFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDVLG 338
Cdd:PLN03233 236 AFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEID 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2028624937 339 ETSLRAMAV--LNPLKVVLTNWPEG-ETKTVTLENHPDHPEMGERTLTFGRELYIEQDD 394
Cdd:PLN03233 316 KRAKRFMAIdkADHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD 374
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
343-537 |
1.74e-68 |
|
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: 218.68 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 343 RAMAVLNPLKVVLTNWPEGETKTVTLENHPDHPEMGERTLTFGRELYIEQDDFmevpvkkyQRMFPGNEVRLKGAYIVRC 422
Cdd:pfam03950 3 RYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNIKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 423 DDCIKDADGNIVEVHCTVDMDSFSGsagaDRKIKGKTLHWVPVNDCIPFEARLYEPLLNDDVADEeeeevdkkdfiSRLN 502
Cdd:pfam03950 75 TEVVKDEDGNVTELHCTYDGDDLGG----ARKVKGKIIHWVSASDAVPAEVRLYDRLFKDEDDAD-----------FLLN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 2028624937 503 PESLKVC-RGYAENVIAQAETGTSFQFLRTGYFCKD 537
Cdd:pfam03950 140 PDSLKVLtEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-339 |
4.65e-55 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 185.75 E-value: 4.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 27 IHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDKC 106
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 107 YEIAEEWIRRGlayvdelskdemreyrgtltepgknspwrdrpaeesldlfrrmkagefpegsktlrmkidmaspnivmr 186
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 187 dpamyrilykehwrtgtkwcIYPMYDFSHPIGDALEGISHSMCSLEYEIHRPLYDWVVEKsadMLPARPRQIEFSRLNM- 265
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEA---LGWEPPRFYHFPRLLLe 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 266 TGTVMSKRYLRqlveggyvagwddprmPTLSAMRRRGYPAMAIRNFVDTIGMSK-----------------------ADS 322
Cdd:cd00418 150 DGTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADA 213
|
330
....*....|....*..
gi 2028624937 323 TVDYAVLEHCVRDVLGE 339
Cdd:cd00418 214 TFDWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
26-343 |
2.63e-40 |
|
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: 146.34 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNP--AKEDTEYVEAIKRDIHWLGFHWTGgEFYASDYY 103
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDE-VVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 104 DKCYEIAEEWIRRGLAYVdelskdemreyrgtltepgknspwrdrpaeesldlfrrmkagefpegsktlrmkidmaspni 183
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 184 vmrdpamyrilykeHWRTGTKWCIYPMYDFSHPIGDALEGISHSMCSLEY----EIHRPLYD---WvveksadmlpARPR 256
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYEyfgW----------EYPE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 257 QIEFSRLNMTGTVMSKRYLRQLVEGGYVAGWDDPRMPTLSAMRRRGYPAMAIRNFVDTIGMSKADSTVDYAVLEHCVRDV 336
Cdd:cd09287 154 TIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKL 233
|
....*..
gi 2028624937 337 LGETSLR 343
Cdd:cd09287 234 IDPRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
29-120 |
7.23e-15 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 75.27 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 29 TRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHWTGGEFYASDYYDKcYE 108
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDA-YR 86
|
90
....*....|...
gi 2028624937 109 IA-EEWIRRGLAY 120
Cdd:PRK05710 87 AAlDRLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
26-117 |
1.60e-12 |
|
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: 67.23 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 26 EIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHW-----TGGE---F 97
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegpdVGGPygpY 80
|
90 100
....*....|....*....|
gi 2028624937 98 YASDYYDKCYEIAEEWIRRG 117
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-226 |
5.12e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 68.23 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 21 EGRYTEIHTRFPPEPNGYMHIGHCKALIMDFLTAEKFGGKCNLRFDDTNPAKEDTEYVEAIKRDIHWLGFHW-----TGG 95
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdVGG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 96 EF--Y-ASDYYDKCYEIAEEWIRRGLAY-----VDELskDEMRE----------YRGTLT---------EPGKNSPWRDR 148
Cdd:PLN02627 120 EYgpYrQSERNAIYKQYAEKLLESGHVYpcfctDEEL--EAMKEeaelkklpprYTGKWAtasdeevqaELAKGTPYTYR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028624937 149 ---PAEESL---DLFRrmkaGEfpegsktLRMKIDMASPNIVMRDPAMyrilykehwrtgtkwciyPMYDFSHPIGDALE 222
Cdd:PLN02627 198 frvPKEGSVkidDLIR----GE-------VSWNTDTLGDFVLLRSNGQ------------------PVYNFCVAVDDATM 248
|
....
gi 2028624937 223 GISH 226
Cdd:PLN02627 249 GITH 252
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-88 |
1.55e-05 |
|
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: 45.16 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2028624937 28 HTRFPPEPNGYMHIGHCKALI-MDFLTAE----KFGGKCNLRFDDTNPAKEDT-------------EYVEAIKRDIHWL 88
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVtFDFLAQAyrklGYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
28-94 |
7.74e-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: 42.14 E-value: 7.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2028624937 28 HTRFPPEPnGYMHIGHCKALIMdfltAEKFGGKCNLRFDDTNPAK------EDTEYVEAIKRDIHWLGFHWTG 94
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICR----AKGIADQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQ 68
|
|
| |
