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Conserved domains on  [gi|1141160747|ref|WP_076925247|]
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MULTISPECIES: tyrosine--tRNA ligase [Pseudoalteromonas]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11415010)

tyrosine--tRNA ligase catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr)

CATH:  1.10.240.10|3.40.50.620
EC:  6.1.1.1
Gene Ontology:  GO:0004831|GO:0006437|GO:0005524|GO:0003723
PubMed:  12458790|10447505|8274143|1852601|2053131|11590011|10704480

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 1-399 0e+00

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


:

Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 601.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747   1 MDLQtaLAEIKRGAEEILIEDELVEKLKsGKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGD 80
Cdd:COG0162     1 MNLL--LELIWRGLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  81 PTGKNVTRKPLTREDVLANAETYKEQVFKILDP--AKTTVAFNSTWMEKLGAAGMI-KLAANQTVARMLERDDFKKRYGS 157
Cdd:COG0162    78 PSGKSEERKLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 158 GQPIAIHEFLYPLVQGWDSVAL----ESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNY 233
Cdd:COG0162   158 GQGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 234 IGITD---APNDMFGKIMSISDVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIARFHSEADAQGAHDD 310
Cdd:COG0162   237 IWLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 311 FIQRFQKKALPDEIPELTITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAK-----GTTAI 385
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGE-KVTDPDAVLTAgdllhGGYLV 395

                         410
                  ....*....|....
gi 1141160747 386 YQVGKRKFANITVA 399
Cdd:COG0162   396 LRVGKKKFALVKLK 409
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 1-399 0e+00

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


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 601.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747   1 MDLQtaLAEIKRGAEEILIEDELVEKLKsGKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGD 80
Cdd:COG0162     1 MNLL--LELIWRGLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  81 PTGKNVTRKPLTREDVLANAETYKEQVFKILDP--AKTTVAFNSTWMEKLGAAGMI-KLAANQTVARMLERDDFKKRYGS 157
Cdd:COG0162    78 PSGKSEERKLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 158 GQPIAIHEFLYPLVQGWDSVAL----ESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNY 233
Cdd:COG0162   158 GQGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 234 IGITD---APNDMFGKIMSISDVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIARFHSEADAQGAHDD 310
Cdd:COG0162   237 IWLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 311 FIQRFQKKALPDEIPELTITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAK-----GTTAI 385
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGE-KVTDPDAVLTAgdllhGGYLV 395

                         410
                  ....*....|....
gi 1141160747 386 YQVGKRKFANITVA 399
Cdd:COG0162   396 LRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 20-399 1.97e-147

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 423.93  E-value: 1.97e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  20 EDELVEKLKSGKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGKNVTRKPLTREDVLAN 99
Cdd:PRK13354   21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 100 AETYKEQVFKILDPAKTTVAFNSTWMEKLGAAGMI-KLAANQTVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVA 178
Cdd:PRK13354  101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 179 L----ESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGVqKMSKSLGNYIGITDA---PNDMFGKIMSIS 251
Cdd:PRK13354  181 LnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 252 DVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQKKALPD-EIPelTIT 330
Cdd:PRK13354  260 DRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLkDIP--TFE 337

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141160747 331 IAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAK-----GTTAIYQVGKRKFANITVA 399
Cdd:PRK13354  338 VSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGE-KVTDVDAIINPedafdGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 7-373 3.65e-133

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 386.75  E-value: 3.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747   7 LAEIKRGAEEIL--IEDELVEKLKsgKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGK 84
Cdd:TIGR00234   6 LLLTKRGLEVQTpeEEKDLLKLLE--RPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  85 NVTRKPLTREDVLANAETYKEQVFKILDPAKTTVAFNSTWMEKLGAAGMIKLAANQ-TVARMLERDDFKKRYGSGqpIAI 163
Cdd:TIGR00234  84 SEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEEN--ISL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 164 HEFLYPLVQGWDSVALESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNYIGITDAPNDM 243
Cdd:TIGR00234 162 HEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEGKYDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 244 FGKIMSISDVLMWRYYDLLSALSIEEIAAQKErvEQGTNPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQKKALPDE 323
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1141160747 324 IPELTITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITD 373
Cdd:TIGR00234 319 VPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGE-KVED 367
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 33-297 1.02e-107

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS 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 formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 317.63  E-value: 1.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  33 LKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGKNVTRKPLTREDVLANAETYKEQVFKILD 112
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 113 ---PAKTTVAFNSTWMEKLGAAGMIKLAANQTVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVALESDVELGGTD 189
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 190 QRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNYI--GITDAPNDMFGKIMSISDVLMWRYYDLLSALSI 267
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1141160747 268 EEIAAQKERVEQGTNPRDIKIELAKELIAR 297
Cdd:cd00805   240 EEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
28-316 1.52e-95

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 287.64  E-value: 1.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  28 KSGKKLKIKAGFDPTAPdLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTgKNVTRKPLTREDVLANAetYKEQV 107
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 108 FKILDPAKTTVAFNSTWMEKLGAAGMIKLAANQ-TVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVALESDVELG 186
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 187 GTDQRFNLLMGRELQKVEGQR---PQTVLMMPLLEGTDGVQKMSKSLGN----YIGITDAPNDMFGKIMSISDVLMWRYY 259
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1141160747 260 DLLSALSIEEIAAQKERVEQGTnPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQ 316
Cdd:pfam00579 237 KLFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
340-393 4.22e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 43.74  E-value: 4.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1141160747  340 NLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAKGTTAIYQVGKRKF 393
Cdd:smart00363   5 KFLARLGLAPSRSQARRLIEQGRVKVNGK-KVTKPSYIVKPGDVISVRGKELKR 57
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 1-399 0e+00

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


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 601.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747   1 MDLQtaLAEIKRGAEEILIEDELVEKLKsGKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGD 80
Cdd:COG0162     1 MNLL--LELIWRGLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  81 PTGKNVTRKPLTREDVLANAETYKEQVFKILDP--AKTTVAFNSTWMEKLGAAGMI-KLAANQTVARMLERDDFKKRYGS 157
Cdd:COG0162    78 PSGKSEERKLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 158 GQPIAIHEFLYPLVQGWDSVAL----ESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNY 233
Cdd:COG0162   158 GQGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 234 IGITD---APNDMFGKIMSISDVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIARFHSEADAQGAHDD 310
Cdd:COG0162   237 IWLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 311 FIQRFQKKALPDEIPELTITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAK-----GTTAI 385
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGE-KVTDPDAVLTAgdllhGGYLV 395

                         410
                  ....*....|....
gi 1141160747 386 YQVGKRKFANITVA 399
Cdd:COG0162   396 LRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 20-399 1.97e-147

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 423.93  E-value: 1.97e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  20 EDELVEKLKSGKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGKNVTRKPLTREDVLAN 99
Cdd:PRK13354   21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 100 AETYKEQVFKILDPAKTTVAFNSTWMEKLGAAGMI-KLAANQTVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVA 178
Cdd:PRK13354  101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 179 L----ESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGVqKMSKSLGNYIGITDA---PNDMFGKIMSIS 251
Cdd:PRK13354  181 LnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 252 DVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQKKALPD-EIPelTIT 330
Cdd:PRK13354  260 DRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLkDIP--TFE 337

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141160747 331 IAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAK-----GTTAIYQVGKRKFANITVA 399
Cdd:PRK13354  338 VSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGE-KVTDVDAIINPedafdGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 7-373 3.65e-133

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 386.75  E-value: 3.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747   7 LAEIKRGAEEIL--IEDELVEKLKsgKKLKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGK 84
Cdd:TIGR00234   6 LLLTKRGLEVQTpeEEKDLLKLLE--RPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  85 NVTRKPLTREDVLANAETYKEQVFKILDPAKTTVAFNSTWMEKLGAAGMIKLAANQ-TVARMLERDDFKKRYGSGqpIAI 163
Cdd:TIGR00234  84 SEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEEN--ISL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 164 HEFLYPLVQGWDSVALESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNYIGITDAPNDM 243
Cdd:TIGR00234 162 HEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEGKYDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 244 FGKIMSISDVLMWRYYDLLSALSIEEIAAQKErvEQGTNPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQKKALPDE 323
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1141160747 324 IPELTITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITD 373
Cdd:TIGR00234 319 VPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGE-KVED 367
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 33-297 1.02e-107

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS 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 formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 317.63  E-value: 1.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  33 LKIKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGKNVTRKPLTREDVLANAETYKEQVFKILD 112
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 113 ---PAKTTVAFNSTWMEKLGAAGMIKLAANQTVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVALESDVELGGTD 189
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 190 QRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGNYI--GITDAPNDMFGKIMSISDVLMWRYYDLLSALSI 267
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1141160747 268 EEIAAQKERVEQGTNPRDIKIELAKELIAR 297
Cdd:cd00805   240 EEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
28-316 1.52e-95

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 287.64  E-value: 1.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  28 KSGKKLKIKAGFDPTAPdLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTgKNVTRKPLTREDVLANAetYKEQV 107
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 108 FKILDPAKTTVAFNSTWMEKLGAAGMIKLAANQ-TVARMLERDDFKKRYGSGQPIAIHEFLYPLVQGWDSVALESDVELG 186
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 187 GTDQRFNLLMGRELQKVEGQR---PQTVLMMPLLEGTDGVQKMSKSLGN----YIGITDAPNDMFGKIMSISDVLMWRYY 259
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1141160747 260 DLLSALSIEEIAAQKERVEQGTnPRDIKIELAKELIARFHSEADAQGAHDDFIQRFQ 316
Cdd:pfam00579 237 KLFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 35-295 6.64e-36

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: 132.43  E-value: 6.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  35 IKAGFDPTAPDLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDPTGKNVTRKPLTREDVLANAETYKEQVFKIL--- 111
Cdd:cd00395     2 LYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGife 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 112 DPAKTTVAFNSTWMEKLGAAGMIK-LAANQTVARMLERDDFKKRYGSGqpIAIHEFLYPLVQGWD----SVALESDVELG 186
Cdd:cd00395    82 DPTQATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 187 GTDQRFNLLMGREL-QKVEGQRPQTVLMMPLLEGTDGvQKMSKSLGN---YIGITDAPNDMFGKIMSISDVLMWRYYDLL 262
Cdd:cd00395   160 GSDQWGNITLGRELaRRFNGFTIAEGLTIPLVTKLDG-PKFGKSESGpkwLDTEKTSPYEFYQFWINAVDSDVINILKYF 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1141160747 263 SALSIEEIAAQKERVEQGTNPRDIKIELAKELI 295
Cdd:cd00395   239 TFLSKEEIERLEQEQYEAPGYRVAQKTLAEEVT 271
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 10-248 1.83e-26

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 108.03  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  10 IKRGAEEILIEDELVEKLKSGKKLKIKAGFDPTAPdLHLGHTVLINKMKTFQDLGHEVIFLIGDFTGMIGDptgKNvtrk 89
Cdd:PRK08560    8 ITRNTEEVVTEEELRELLESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND---KG---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  90 plTREDVLANAETYKEqVFKI--LDPAKTTVAFNST-------WMEklgaagMIKLAANQTVARMLERDDFKKRYGSGQP 160
Cdd:PRK08560   80 --DLEEIRKVAEYNKK-VFEAlgLDPDKTEFVLGSEfqldkeyWLL------VLKLAKNTTLARARRSMTIMGRRMEEPD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 161 IAihEFLYPLVQGWDSVALESDVELGGTDQRFNLLMGRELQKVEGQRPQTVLMMPLLEGTDGVQ-KMSKS-LGNYIGITD 238
Cdd:PRK08560  151 VS--KLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGiKMSKSkPGSAIFVHD 228

                         250
                  ....*....|
gi 1141160747 239 APNDMFGKIM 248
Cdd:PRK08560  229 SPEEIRRKIK 238
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 38-296 9.29e-14

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: 71.08  E-value: 9.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  38 GFDPTAPdLHLGHTV-LINKMKTFQDLGHEVIFLIGD---FTGMIGDPTgknvtrkpLTREDVLANAETYkeqvfkI--- 110
Cdd:cd00806     5 GIQPSGS-LHLGHYLgAFRFWVWLQEAGYELFFFIADlhaLTVKQLDPE--------ELRQNTRENAKDY------Lacg 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 111 LDPAKTTVAFNSTWME--KLgaagMIKLAANQTVARmLER-DDFKKRYGSGQPIAIHEFLYPLVQGWDSVALESDVELGG 187
Cdd:cd00806    70 LDPEKSTIFFQSDVPEhyEL----AWLLSCVVTFGE-LERmTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 188 TDQ------------RFNLLMGRELQKVEGQRPQTVLMMPLlegTDGVQKMSKSLG-NYIGITDAPNDMFGKIMSI---- 250
Cdd:cd00806   145 IDQdphleltrdiarRFNKLYGEIFPKPAALLSKGAFLPGL---QGPSKKMSKSDPnNAIFLTDSPKEIKKKIMKAatdg 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1141160747 251 ------------SDVLMWRYYDLLSALSIEEIAAQKERVEQGTNPRDIKIELAKELIA 296
Cdd:cd00806   222 grtehrrdgggpGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQE 279
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 31-249 1.69e-10

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 61.79  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  31 KKLKIKAGFDPTAPdLHLGHTV--LINKMKtFQDlGHEVIFLIGD---FTGMIGDPT--GKNVTRKPLtreDVLANAety 103
Cdd:PRK12282    1 TKPIILTGDRPTGK-LHLGHYVgsLKNRVA-LQN-EHEQFVLIADqqaLTDNAKNPEkiRRNILEVAL---DYLAVG--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 104 keqvfkiLDPAKTTVAFNS--------TWMeklgaagMIKLAanqTVARmLERD----DFKKRYGSGQPIAIHEFLYPLV 171
Cdd:PRK12282   72 -------IDPAKSTIFIQSqipelaelTMY-------YMNLV---TVAR-LERNptvkTEIAQKGFGRSIPAGFLTYPVS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 172 QGWDSVALESDVELGGTDQ------------RFNLLMGRE-LQKVEGQRPQTvlmmPLLEGTDGVQKMSKSLGNYIGITD 238
Cdd:PRK12282  134 QAADITAFKATLVPVGDDQlpmieqtreivrRFNSLYGTDvLVEPEALLPEA----GRLPGLDGKAKMSKSLGNAIYLSD 209

                         250
                  ....*....|.
gi 1141160747 239 APNDMFGKIMS 249
Cdd:PRK12282  210 DADTIKKKVMS 220
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 190-298 7.26e-10

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: 59.68  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 190 QRFNLLMGRELQKVEGQRPQTVLMMPlleGTDGVQKMSKSLGNYIGITDAPNDMFGKIMSI---SDVL------------ 254
Cdd:COG0180   163 RRFNHRYGEVFPEPEALIPEEGARIP---GLDGRKKMSKSYGNTINLLDDPKEIRKKIKSAvtdSERLryddpgkpevcn 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1141160747 255 MWRYYDLLS-ALSIEEIAAQKERVEQGTnpRDIKIELAKELIARF 298
Cdd:COG0180   240 LFTIYSAFSgKEEVEELEAEYRAGGIGY--GDLKKALAEAVVEFL 282
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 14-249 1.61e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 49.69  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  14 AEEILIEDELVEKLKSGKKLKIKAGFDPTApDLHLGHTVL----INKMKtfqDLGHEVIFLIGDFTGMIGDPTGKNVTRK 89
Cdd:PTZ00126   48 GEECIQPEELRELLKLKERPICYDGFEPSG-RMHIAQGILkainVNKLT---KAGCVFVFWVADWFALLNNKMGGDLEKI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747  90 PLTREdvlanaetYKEQVFKILDPAKTTVAF-----------NSTWMEklgaagMIKLAANQTVARM------LERDDfk 152
Cdd:PTZ00126  124 RKVGE--------YFIEVWKAAGMDMDNVRFlwaseeinknpNDYWLR------VMDIARSFNITRIkrcsqiMGRSE-- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 153 kryGSGQPIAihEFLYPLVQGWDSVALESDVELGGTDQR-FNLLmGREL--QKVEGQRPQTVL--MMP-LLEGTdgvQKM 226
Cdd:PTZ00126  188 ---GDEQPCA--QILYPCMQCADIFYLKADICQLGMDQRkVNML-AREYcdKKKIKKKPIILShhMLPgLLEGQ---EKM 258

                         250       260
                  ....*....|....*....|....
gi 1141160747 227 SKSLGNY-IGITDAPNDMFGKIMS 249
Cdd:PTZ00126  259 SKSDPNSaIFMEDSEEDVNRKIKK 282
S4 smart00363
S4 RNA-binding domain;
340-393 4.22e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 43.74  E-value: 4.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1141160747  340 NLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAKGTTAIYQVGKRKF 393
Cdd:smart00363   5 KFLARLGLAPSRSQARRLIEQGRVKVNGK-KVTKPSYIVKPGDVISVRGKELKR 57
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 338-381 2.52e-05

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 41.85  E-value: 2.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1141160747 338 IANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAKG 381
Cdd:cd00165     3 LDKILARLGLAPSRSEARQLIKHGHVLVNGK-VVTKPSYKVKPG 45
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 190-298 1.25e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 43.54  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 190 QRFNLLMGrELQKVegqrPQTVL--MMPLLEGTDG-VQKMSKSLG---NYIGITDAPNDMFGKIMS-------------- 249
Cdd:PRK00927  160 RRFNNLYG-EVFPV----PEPLIpkVGARVMGLDGpTKKMSKSDPndnNTINLLDDPKTIAKKIKKavtdserlreiryd 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1141160747 250 ------ISDVLMwrYYDLLSALSIEEIAAQKERVEQGTNprDIKIELAKELIARF 298
Cdd:PRK00927  235 lpnkpeVSNLLT--IYSALSGESIEELEAEYEAGGKGYG--DFKKDLAEAVVEFL 285
S4_2 pfam13275
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 329-368 2.09e-04

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4.


Pssm-ID: 433078 [Multi-domain]  Cd Length: 65  Bit Score: 38.96  E-value: 2.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1141160747 329 ITIAEDTILIANLLKEANLVVSTSEAMRMIKQGAVKLNGE 368
Cdd:pfam13275   1 IKIRGEYITLGQLLKLAGLVESGGEAKWFIAEGEVLVNGE 40
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 338-381 3.41e-04

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 37.86  E-value: 3.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1141160747 338 IANLLKEANLVVSTSEAMRMIKQGAVKLNGEdKITDTKLEVAKG 381
Cdd:pfam01479   3 LDKVLARLGLASSRSQARQLIEHGRVLVNGK-VVKDPSYRVKPG 45
PLN02886 PLN02886
aminoacyl-tRNA ligase
 166-299 1.71e-03

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 40.18  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 166 FLYPLVQGWDSVALESDVELGGTDQ------------RFNLLMGRELQKVEGQRPQTVLMMP----------LLEGTDGV 223
Cdd:PLN02886  170 LTYPVLMASDILLYQADLVPVGEDQkqhleltrdiaeRVNNLYGGRKWKKLGGRGGSVFKVPealippagarVMSLTDGT 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 224 QKMSKSL---GNYIGITDAPNDMFGKIMSIS----DVLMWR------------YYDLLSALSIEEIAAQKERVEQGtnpr 284
Cdd:PLN02886  250 SKMSKSApsdQSRINLLDPPDVIANKIKRCKtdsfPGLEFDnperpecnnllsIYQLVTGKTKEEVLAECGDMRWG---- 325

                         170
                  ....*....|....*
gi 1141160747 285 DIKIELAKELIARFH 299
Cdd:PLN02886  326 DFKPLLTDALIEHLS 340
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 172-247 3.78e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 39.16  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 172 QGwDSVALESDVELGGTDQrfNLLMG---RELQKVEGQR------PQTVLM----MPlleGTDGvQKMSKSLGNYIGITD 238
Cdd:PRK12283  205 EG-DDEALEQARALLQEQQ--NLSMGdreRLFGYLEGAGkiilpePQALLTeaskMP---GLDG-QKMSKSYGNTIGLRE 277


                  ....*....
gi 1141160747 239 APNDMFGKI 247
Cdd:PRK12283  278 DPESVTKKI 286
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 224-311 7.79e-03

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


Pssm-ID: 439985 [Multi-domain]  Cd Length: 465  Bit Score: 38.16  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141160747 224 QKMSKSLGNYIGITDApNDMFGkimsiSDVLmwRYYdLLSA-------LSIEEI-AAQK---------ERVEQGTNPRDI 286
Cdd:COG0215   264 EKMSKSLGNFFTVRDL-LKKYD-----PEVL--RFF-LLSAhyrspldFSEEALeEAEKalerlynalRRLEEALGAADS 334

                          90       100
                  ....*....|....*....|....*
gi 1141160747 287 KIELAKELIARFHSEADaqgahDDF 311
Cdd:COG0215   335 SAEEIEELREEFIAAMD-----DDF 354
 
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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