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Conserved domains on  [gi|30682913|ref|NP_850070|]
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Nucleotidylyl transferase superfamily protein [Arabidopsis thaliana]

Protein Classification

nucleotidyl transferase family protein; glutamine/glutamate--tRNA ligase( domain architecture ID 10791485)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases| glutamine/glutamate--tRNA ligase catalyzes the attachment of glutamate or glutamine to tRNA(Glu) or tRNA(Gln); in some organisms, the non-discriminating form of glutamate--tRNA ligase aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02886 PLN02886
aminoacyl-tRNA ligase
 19-407 0e+00

aminoacyl-tRNA ligase


:

Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 722.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   19 SRLGSLTRLLSKPTSLSgsfssisVTGQGFRCCCSVATDDTS-------PSVKKRVVSGVQPTGSVHLGNYLGAIKNWVA 91
Cdd:PLN02886   1 SSLGSLGRLLSKPGPLS-------GSASSASCCSAATAATAPekeappkVARKKRVVSGVQPTGSIHLGNYLGAIKNWVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   92 LQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQSHVPAHVELMWLLCSSTPIGWLQKMIQF 171
Cdd:PLN02886  74 LQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  172 KEKSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIAQRVNHLYGGKKWKKLGGRGGSLFKIPEP 251
Cdd:PLN02886 154 KEKSRKAGDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNNLYGGRKWKKLGGRGGSVFKVPEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  252 LIPQAGARVMSLTDGLSKMSKSAPSDQSRINLLDSKDLIVDKIKRCKTDSFAGLEFDNAERPECNNLLSIYQIVSGKKKE 331
Cdd:PLN02886 234 LIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKE 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682913  332 EVMEECKDMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILSEGADRAEELGAVTMRNMYQAMGYYQRRR 407
Cdd:PLN02886 314 EVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFVQRRR 389
 
Name Accession Description Interval E-value
PLN02886 PLN02886
aminoacyl-tRNA ligase
 19-407 0e+00

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 722.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   19 SRLGSLTRLLSKPTSLSgsfssisVTGQGFRCCCSVATDDTS-------PSVKKRVVSGVQPTGSVHLGNYLGAIKNWVA 91
Cdd:PLN02886   1 SSLGSLGRLLSKPGPLS-------GSASSASCCSAATAATAPekeappkVARKKRVVSGVQPTGSIHLGNYLGAIKNWVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   92 LQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQSHVPAHVELMWLLCSSTPIGWLQKMIQF 171
Cdd:PLN02886  74 LQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  172 KEKSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIAQRVNHLYGGKKWKKLGGRGGSLFKIPEP 251
Cdd:PLN02886 154 KEKSRKAGDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNNLYGGRKWKKLGGRGGSVFKVPEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  252 LIPQAGARVMSLTDGLSKMSKSAPSDQSRINLLDSKDLIVDKIKRCKTDSFAGLEFDNAERPECNNLLSIYQIVSGKKKE 331
Cdd:PLN02886 234 LIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKE 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682913  332 EVMEECKDMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILSEGADRAEELGAVTMRNMYQAMGYYQRRR 407
Cdd:PLN02886 314 EVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFVQRRR 389
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 64-402 1.58e-176

Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 494.95  E-value: 1.58e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:COG0180   3 KKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIA 223
Cdd:COG0180  83 SDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 224 QRVNHLYggkkwkklggrgGSLFKIPEPLIPQAGARVMSLtDGLSKMSKsapSDQSRINLLDSKDLIVDKIKRCKTDSfA 303
Cdd:COG0180 163 RRFNHRY------------GEVFPEPEALIPEEGARIPGL-DGRKKMSK---SYGNTINLLDDPKEIRKKIKSAVTDS-E 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 304 GLEFDNAERPECNNLLSIYQIVSGK-KKEEVMEECK--DMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILSE 380
Cdd:COG0180 226 RLRYDDPGKPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAE 305

                       330       340
                ....*....|....*....|..
gi 30682913 381 GADRAEELGAVTMRNMYQAMGY 402
Cdd:COG0180 306 GAEKARAIAAKTLAEVREAMGL 327
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 64-401 4.81e-120

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 351.63  E-value: 4.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913    64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQ-LGKATTDTAALYLACGIDVSKASVFV 142
Cdd:TIGR00233   2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQTDPDaLRKAREELAADYLAVGLDPEKTFIFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   143 QSHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGVenaSVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREI 222
Cdd:TIGR00233  82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKSQAENV---PIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   223 AQRVNHLYGGKkwkklggrggslFKIPEPLIPQAGARVMSLTDglSKMSKSAPSdqSRINLLDSKDLIVDKIKRCKTDSF 302
Cdd:TIGR00233 159 AERFNKKFKNF------------FPKPESLISKFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   303 AGLEFDNAERPECNNLLSIYQIVS-----GKKKEEVMEECKD--MSWGTFKPLLADALIEHLSPIQARYQEIIAepEYLD 375
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSfflidDDKLKEIYEAYKSgkLGYGECKKALIEVLQEFLKEIQERRAEIAE--EILD 300

                         330       340
                  ....*....|....*....|....*.
gi 30682913   376 KILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:TIGR00233 301 KILEPGAKKARETANKTLADVYKAMG 326
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 66-356 8.48e-118

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it 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 class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 344.18  E-value: 8.48e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  66 RVVSGVQPTGSVHLGNYLGAIKNWVALQDT-YETLFIIVDHHAITLPY-DTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:cd00806   1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAgYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKegVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIA 223
Cdd:cd00806  81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQ--GESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 224 QRVNHLYGGkkwkklggrggsLFKIPEPLIPQaGARVMSLTDGLSKMSKSAPSdqSRINLLDSKDLIVDKIKRCKTDSFA 303
Cdd:cd00806 159 RRFNKLYGE------------IFPKPAALLSK-GAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGR 223

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30682913 304 GLEFDNAERPECNNLLSIYQIVSGKKKEEV--MEECK--DMSWGTFKPLLADALIEH 356
Cdd:cd00806 224 TEHRRDGGGPGVSNLVEIYSAFFNDDDEELeeIDEYRsgGLGYGECKKLLAEAIQEF 280
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
66-358 1.51e-92

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 280.32  E-value: 1.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913    66 RVVSGVQPTGSVHLGnYLGAIKNWVALQ-DTYETLFIIVDHHAITLPYD---TRQLGKATTDTAAL---YLACGIDVSKA 138
Cdd:pfam00579   7 RVYSGIDPTGPLHLG-YLVPLMKLRQFQqAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPEKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   139 SVFVQSHVPAHVELMWLLCSSTPIGWLQKMIQFKE-KSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIE 217
Cdd:pfam00579  86 EIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDvKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   218 LAREIAQRVNHlyggkkwkklggrggSLFKIPEPLIPqagaRVMSLTDGLSKMSKSAPSdqSRINLLDSKDLIVDKIKRC 297
Cdd:pfam00579 166 LGRDLARRFNK---------------KIFKKPVGLTN----PLLTGLDGGKKMSKSAGN--SAIFLDDDPESVYKKIQKA 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682913   298 KTDSFAGLEFDNAERPECNN-LLSIYQIVSGKKK----EEVMEECKDM--SWGTFKPLLADALIEHLS 358
Cdd:pfam00579 225 YTDPDREVRKDLKLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGlvHGGDLKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
PLN02886 PLN02886
aminoacyl-tRNA ligase
 19-407 0e+00

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 722.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   19 SRLGSLTRLLSKPTSLSgsfssisVTGQGFRCCCSVATDDTS-------PSVKKRVVSGVQPTGSVHLGNYLGAIKNWVA 91
Cdd:PLN02886   1 SSLGSLGRLLSKPGPLS-------GSASSASCCSAATAATAPekeappkVARKKRVVSGVQPTGSIHLGNYLGAIKNWVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   92 LQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQSHVPAHVELMWLLCSSTPIGWLQKMIQF 171
Cdd:PLN02886  74 LQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  172 KEKSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIAQRVNHLYGGKKWKKLGGRGGSLFKIPEP 251
Cdd:PLN02886 154 KEKSRKAGDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNNLYGGRKWKKLGGRGGSVFKVPEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  252 LIPQAGARVMSLTDGLSKMSKSAPSDQSRINLLDSKDLIVDKIKRCKTDSFAGLEFDNAERPECNNLLSIYQIVSGKKKE 331
Cdd:PLN02886 234 LIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKE 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682913  332 EVMEECKDMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILSEGADRAEELGAVTMRNMYQAMGYYQRRR 407
Cdd:PLN02886 314 EVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFVQRRR 389
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 64-405 0e+00

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 531.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:PRK00927   1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGvENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIA 223
Cdd:PRK00927  81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQK-ENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  224 QRVNHLYggkkwkklggrgGSLFKIPEPLIPQAGARVMSLTDGLSKMSKSAPSDQSRINLLDSKDLIVDKIKRCKTDS-- 301
Cdd:PRK00927 160 RRFNNLY------------GEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSer 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  302 FAGLEFDNAERPECNNLLSIYQIVSGKKKEEVMEECKDMS--WGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILS 379
Cdd:PRK00927 228 LREIRYDLPNKPEVSNLLTIYSALSGESIEELEAEYEAGGkgYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILA 307

                        330       340
                 ....*....|....*....|....*.
gi 30682913  380 EGADRAEELGAVTMRNMYQAMGYYQR 405
Cdd:PRK00927 308 EGAEKARAVASKTLKEVREAMGLLRK 333
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 64-402 1.58e-176

Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 494.95  E-value: 1.58e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:COG0180   3 KKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIA 223
Cdd:COG0180  83 SDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 224 QRVNHLYggkkwkklggrgGSLFKIPEPLIPQAGARVMSLtDGLSKMSKsapSDQSRINLLDSKDLIVDKIKRCKTDSfA 303
Cdd:COG0180 163 RRFNHRY------------GEVFPEPEALIPEEGARIPGL-DGRKKMSK---SYGNTINLLDDPKEIRKKIKSAVTDS-E 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 304 GLEFDNAERPECNNLLSIYQIVSGK-KKEEVMEECK--DMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLDKILSE 380
Cdd:COG0180 226 RLRYDDPGKPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAE 305

                       330       340
                ....*....|....*....|..
gi 30682913 381 GADRAEELGAVTMRNMYQAMGY 402
Cdd:COG0180 306 GAEKARAIAAKTLAEVREAMGL 327
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 64-401 4.81e-120

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 351.63  E-value: 4.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913    64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQ-LGKATTDTAALYLACGIDVSKASVFV 142
Cdd:TIGR00233   2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQTDPDaLRKAREELAADYLAVGLDPEKTFIFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   143 QSHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGVenaSVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREI 222
Cdd:TIGR00233  82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKSQAENV---PIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   223 AQRVNHLYGGKkwkklggrggslFKIPEPLIPQAGARVMSLTDglSKMSKSAPSdqSRINLLDSKDLIVDKIKRCKTDSF 302
Cdd:TIGR00233 159 AERFNKKFKNF------------FPKPESLISKFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   303 AGLEFDNAERPECNNLLSIYQIVS-----GKKKEEVMEECKD--MSWGTFKPLLADALIEHLSPIQARYQEIIAepEYLD 375
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSfflidDDKLKEIYEAYKSgkLGYGECKKALIEVLQEFLKEIQERRAEIAE--EILD 300

                         330       340
                  ....*....|....*....|....*.
gi 30682913   376 KILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:TIGR00233 301 KILEPGAKKARETANKTLADVYKAMG 326
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 66-356 8.48e-118

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it 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 class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 344.18  E-value: 8.48e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  66 RVVSGVQPTGSVHLGNYLGAIKNWVALQDT-YETLFIIVDHHAITLPY-DTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:cd00806   1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAgYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKegVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREIA 223
Cdd:cd00806  81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQ--GESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 224 QRVNHLYGGkkwkklggrggsLFKIPEPLIPQaGARVMSLTDGLSKMSKSAPSdqSRINLLDSKDLIVDKIKRCKTDSFA 303
Cdd:cd00806 159 RRFNKLYGE------------IFPKPAALLSK-GAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGR 223

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30682913 304 GLEFDNAERPECNNLLSIYQIVSGKKKEEV--MEECK--DMSWGTFKPLLADALIEH 356
Cdd:cd00806 224 TEHRRDGGGPGVSNLVEIYSAFFNDDDEELeeIDEYRsgGLGYGECKKLLAEAIQEF 280
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
66-358 1.51e-92

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 280.32  E-value: 1.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913    66 RVVSGVQPTGSVHLGnYLGAIKNWVALQ-DTYETLFIIVDHHAITLPYD---TRQLGKATTDTAAL---YLACGIDVSKA 138
Cdd:pfam00579   7 RVYSGIDPTGPLHLG-YLVPLMKLRQFQqAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPEKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   139 SVFVQSHVPAHVELMWLLCSSTPIGWLQKMIQFKE-KSRKEGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIE 217
Cdd:pfam00579  86 EIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDvKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   218 LAREIAQRVNHlyggkkwkklggrggSLFKIPEPLIPqagaRVMSLTDGLSKMSKSAPSdqSRINLLDSKDLIVDKIKRC 297
Cdd:pfam00579 166 LGRDLARRFNK---------------KIFKKPVGLTN----PLLTGLDGGKKMSKSAGN--SAIFLDDDPESVYKKIQKA 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682913   298 KTDSFAGLEFDNAERPECNN-LLSIYQIVSGKKK----EEVMEECKDM--SWGTFKPLLADALIEHLS 358
Cdd:pfam00579 225 YTDPDREVRKDLKLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGlvHGGDLKKAAAEAVNKLLQ 292
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 64-401 5.19e-82

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 254.78  E-value: 5.19e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITL-PYDTRQLGKATTDTAALYLACGIDVSKASVFV 142
Cdd:PRK12282   2 KPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTDnAKNPEKIRRNILEVALDYLAVGIDPAKSTIFI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  143 QSHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRKEGVENA-SVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELARE 221
Cdd:PRK12282  82 QSQIPELAELTMYYMNLVTVARLERNPTVKTEIAQKGFGRSiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQTRE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  222 IAQRVNHLYggkkwkklggrGGSLFKIPEPLIPQAGaRVMSLtDGLSKMSKsapSDQSRINLLDSKDLIVDKIKRCKTDS 301
Cdd:PRK12282 162 IVRRFNSLY-----------GTDVLVEPEALLPEAG-RLPGL-DGKAKMSK---SLGNAIYLSDDADTIKKKVMSMYTDP 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  302 fAGLEFDNAERPECNNLLSIYQIVSGKKK--EEVMEECK-----DMswgTFKPLLADALIEHLSPIQARYQEIIAEPEYL 374
Cdd:PRK12282 226 -NHIRVEDPGKVEGNVVFTYLDAFDPDKAevAELKAHYQrgglgDV---KCKRYLEEVLQELLAPIRERRAEFAKDPGYV 301

                        330       340
                 ....*....|....*....|....*..
gi 30682913  375 DKILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:PRK12282 302 LEILKAGSEKAREVAAQTLSEVKDAMG 328
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 65-401 1.33e-74

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 237.54  E-value: 1.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   65 KRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYETLFIIVDHHAITLPYDTRQ-LGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:PRK12283   3 DRVLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTTHYETPEvIEKNVWDMVIDWLAAGVDPAQATLFIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  144 SHVPAHVELMWLLCSSTPIGWLQKMIQFKEKSRK-EGVENASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIELAREI 222
Cdd:PRK12283  83 SKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKlKEKDLSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  223 AQRVNHLY-----------------------------------------------GGKKWKKLGGRGGSLF-------KI 248
Cdd:PRK12283 163 ARRFNHLYgrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqaralLQEQQNLSMGDRERLFgylegagKI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  249 ----PEPLIPQAgARVMSLtDGlSKMSKSApsdQSRINLLDSKDLIVDKIKRCKTDSfAGLEFDNAERPECNNLLSIYQI 324
Cdd:PRK12283 243 ilpePQALLTEA-SKMPGL-DG-QKMSKSY---GNTIGLREDPESVTKKIRTMPTDP-ARVRRTDPGDPEKCPVWQLHQV 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  325 VSGKK-KEEVMEECKDMSWGTF--KPLLADALIEHLSPIQARYQEIIAEPEYLDKILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:PRK12283 316 YSDEEtKEWVQKGCRSAGIGCLecKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREAMG 395
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
 64-401 2.59e-74

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 235.00  E-value: 2.59e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   64 KKRVVSGVQPTGSVHLGNYLGAIKNWVALQDTYE--TLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVF 141
Cdd:PRK12556   3 EKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEgkALYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVIFY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  142 VQSHVPAHVELMWLLCSSTPIGWLQKMIQFK---EKSRKEGVE-NASV--GLFTYPDLMTADILLYQSDFVPVGEDQKQH 215
Cdd:PRK12556  83 RQSDVPEIFELAWILSCLTPKGLMNRAHAYKakvDQNKEAGLDlDAGVnmGLYTYPILMAADILLFQATHVPVGKDQIQH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  216 IELAREIAQRVNHLYGGKkwkklggrggslFKIPEPLIPQAGArVMSLTDGlSKMSKSApsdQSRINLLDSKDLIVDKIK 295
Cdd:PRK12556 163 IEIARDIATYFNHTFGDT------------FTLPEYVIQEEGA-ILPGLDG-RKMSKSY---GNVIPLFAEQEKLRKLIF 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  296 RCKTDSfagLEFDNAERPECNNLLSIYQIVSGKKKEEVMEE--CKDMSWGTFKPLLADALIEHLSPIQARYQEIIAEPEY 373
Cdd:PRK12556 226 KIKTDS---SLPNEPKDPETSALFTIYKEFATEEEVQSMREkyETGIGWGDVKKELFRVVDRELAGPREKYAMYMNEPSL 302

                        330       340
                 ....*....|....*....|....*...
gi 30682913  374 LDKILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:PRK12556 303 LDEALEKGAERAREIAKPNLAEIKKAIG 330
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
 66-401 4.53e-61

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 203.70  E-value: 4.53e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   66 RVVSGVQPTGSVHLGNYLGAIKNWVA--LQDTYETLFIIVDHHAITLPYDTRQLGKATTDTAALYLACGIDVSKASVFVQ 143
Cdd:PRK12284   4 RVLTGITTTGTPHLGNYAGAIRPAIAasRQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  144 SHVPAHVELMWLLCSSTPIGWLQKMIQFK---EKSRKEGVE---NASVGLFTYPDLMTADILLYQSDFVPVGEDQKQHIE 217
Cdd:PRK12284  84 SDIPEIPELTWLLTCVAGKGLLNRAHAYKaavDKNVAAGEDpdaGVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  218 LAREIAQRVNHLYggkkwkklggrGGSLFKIPEPLIPQAGARVMSLtDGlSKMSKSApsdQSRINLLDSKDLIVDKIKRC 297
Cdd:PRK12284 164 MARDIAQRFNHLY-----------GGEFFVLPEAVIEESVATLPGL-DG-RKMSKSY---DNTIPLFAPREELKKAIFSI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  298 KTDSFAGLEfdnAERPECNNLLSIYQIVSGKKKEEVM-EECKD-MSWGTFKPLLADALIEHLSPIQARYQEIIAEPEYLD 375
Cdd:PRK12284 228 VTDSRAPGE---PKDTEGSALFQLYQAFATPEETAAFrQALADgIGWGDAKQRLFERIDRELAPMRERYEALIARPADIE 304

                        330       340
                 ....*....|....*....|....*.
gi 30682913  376 KILSEGADRAEELGAVTMRNMYQAMG 401
Cdd:PRK12284 305 DILLAGAAKARRIATPFLAELREAVG 330
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 69-355 4.58e-35

catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, 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 class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173893 [Multi-domain]  Cd Length: 273  Bit Score: 130.50  E-value: 4.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  69 SGVQPTG-SVHLGNYLGaIKNWVALQDT-YETLFIIVDHHAIT----------LPYDTRQLGKATTDTAALYLACGIDVS 136
Cdd:cd00395   4 CGIDPTAdSLHIGHLIG-LLTFRRFQHAgHRPIFLIGGQTGIIgdpsgkkserTLNDPEEVRQNIRRIAAQYLAVGIFED 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 137 --KASVFVQSHVP---AHVELMWLLCSSTPIGWLQKMIQFKEKSrKEGVenaSVGLFTYPDLMTADILLYQS----DFVP 207
Cdd:cd00395  83 ptQATLFNNSDWPgplAHIQFLRDLGKHVYVNYMERKTSFQSRS-EEGI---SATEFTYPPLQAADFLLLNTtegcDIQP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 208 VGEDQKQHIELAREIAQRVNhlyggkkwkklggrggsLFKIPEPLIPqagARVMSLTDglSKMSKSAPSDQSRINLLDSK 287
Cdd:cd00395 159 GGSDQWGNITLGRELARRFN-----------------GFTIAEGLTI---PLVTKLDG--PKFGKSESGPKWLDTEKTSP 216

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682913 288 DLIVDKIKRcKTDSfaglefdnaerpecnNLLSIYQIVSGKKKEEV----MEECKDMSWGTFKPLLADALIE 355
Cdd:cd00395 217 YEFYQFWIN-AVDS---------------DVINILKYFTFLSKEEIerleQEQYEAPGYRVAQKTLAEEVTK 272
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 67-381 1.75e-14

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 74.13  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   67 VVSGVQPTGSVHLGNYLgAIKNWVALQDTYETLFI-IVDHHAitlpYDTRQLGKATTDTAAL-----YLACGIDVSKASV 140
Cdd:PRK12285  69 VYTGFMPSGPMHIGHKM-VFDELKWHQEFGANVYIpIADDEA----YAARGLSWEETREWAYeyildLIALGFDPDKTEI 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  141 FVQShvpAHVELMWLlcsSTPIGwlqKMIQFKEKSRKEGV-ENASVGLFTYPDLMTADILLYQSDF------VPVGEDQK 213
Cdd:PRK12285 144 YFQS---ENIKVYDL---AFELA---KKVNFSELKAIYGFtGETNIGHIFYPATQAADILHPQLEEgpkptlVPVGIDQD 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  214 QHIELAREIAQRVNHLYggkkwkklggrggslfkipePLIPQAG--ARVM-SLTDGlsKMSKSAPsdQSRINLLDSKDLI 290
Cdd:PRK12285 215 PHIRLTRDIAERLHGGY--------------------GFIKPSStyHKFMpGLTGG--KMSSSKP--ESAIYLTDDPETV 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  291 VDKIKRCKTDSFAGLEFD-----NAErpECnnllSIYQ------IVSGKKKEEVMEECK--DMSWGTFKPLLADALIEHL 357
Cdd:PRK12285 271 KKKIMKALTGGRATLEEQrklggEPD--EC----VVYElllyhlEEDDKELKEIYEECRsgELLCGECKKEAAEKIAEFL 344

                        330       340
                 ....*....|....*....|....
gi 30682913  358 SPIQARYQEIIaepEYLDKILSEG 381
Cdd:PRK12285 345 KEHQEKREEAR---EILEKYLYDG 365
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 67-273 1.89e-06

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: 47.09  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  67 VVSGVQPTGSVHLGNYLGAIKNWVALQ----DTYETLFI--IVDHHAITlpydtrqlgkattdtaalylacgidVSKASV 140
Cdd:cd00802   2 TFSGITPNGYLHIGHLRTIVTFDFLAQayrkLGYKVRCIalIDDAGGLI-------------------------GDPANK 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913 141 FVQSHvPAHVELMwllcsstpigwlqkMIQFKEksrkegvenasvgLFTYPDLMTADILL---YQSDFVPVGEDQKQHIE 217
Cdd:cd00802  57 KGENA-KAFVERW--------------IERIKE-------------DVEYMFLQAADFLLlyeTECDIHLGGSDQLGHIE 108

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30682913 218 LAREIAQRVNhlyggkkwkklggrggsLFKIPEPLIPqagARVMSltDGLSKMSKS 273
Cdd:cd00802 109 LGLELLKKAG-----------------GPARPFGLTF---GRVMG--ADGTKMSKS 142
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 64-296 9.75e-06

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 47.17  E-value: 9.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913   64 KKRVVSGVQPTGSVHLGNYLGAIKnwVA-LQDT-YETLFIIVDHHA-ITLPYDTRQLGKATTDTAALYLACGIDVSKASv 140
Cdd:PRK08560  30 EPKAYIGFEPSGKIHLGHLLTMNK--LAdLQKAgFKVTVLLADWHAyLNDKGDLEEIRKVAEYNKKVFEALGLDPDKTE- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  141 FV-----QSHVPAHVELMWLLCSSTpigwLQKMIQ-FKEKSRKEgvENASVGLFTYPDLMTADILLYQSDFVPVGEDQ-K 213
Cdd:PRK08560 107 FVlgsefQLDKEYWLLVLKLAKNTT----LARARRsMTIMGRRM--EEPDVSKLVYPLMQVADIFYLDVDIAVGGMDQrK 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  214 QHIeLAREIAQRVNhlyggkkwkklggrggslFKIP----EPLIPqagarvmSLTDGLSKMSKSAPsdQSRINLLDSKDL 289
Cdd:PRK08560 181 IHM-LAREVLPKLG------------------YKKPvcihTPLLT-------GLDGGGIKMSKSKP--GSAIFVHDSPEE 232


                 ....*..
gi 30682913  290 IVDKIKR 296
Cdd:PRK08560 233 IRRKIKK 239
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 176-295 7.65e-05

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 44.68  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682913  176 RKEGVENASVGLFtYPDLMTADILLYQSDFVPVGEDQKQHIELAREIAQRVnhlyggkkwkklggrggslfKIPEPLIPQ 255
Cdd:PTZ00126 185 RSEGDEQPCAQIL-YPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDKK--------------------KIKKKPIIL 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30682913  256 AGARVMSLTDGLSKMSKSAPSdqSRINLLDSKDLIVDKIK 295
Cdd:PTZ00126 244 SHHMLPGLLEGQEKMSKSDPN--SAIFMEDSEEDVNRKIK 281
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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