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Conserved domains on  [gi|1900939932|dbj|GGJ91616|]
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tyrosine--tRNA ligase [Calditerricola satsumensis]

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)

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 ...
27-427 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: 615.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  27 QLAVIARGAAEILPEDELRRKLArsvatGRPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDP 106
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 107 TGKSETRKPLTEEQVKANARTYVEQFAKVLDMD--RVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKRYKAG 183
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 184 QPISLHEFFYPLMQGYDSVAL----ESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYI 259
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISE---PPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRMYHGEEAARQAEDY 336
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 337 FRTVFQERALPEDVPTVAVARaklEDGRMWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDVDAAVTVRD-----G 411
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSA---AEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDllhggY 393
                         410
                  ....*....|....*.
gi 1900939932 412 MVVQVGKRKFAKVVLQ 427
Cdd:COG0162   394 LVLRVGKKKFALVKLK 409
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
27-427 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: 615.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  27 QLAVIARGAAEILPEDELRRKLArsvatGRPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDP 106
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 107 TGKSETRKPLTEEQVKANARTYVEQFAKVLDMD--RVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKRYKAG 183
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 184 QPISLHEFFYPLMQGYDSVAL----ESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYI 259
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISE---PPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRMYHGEEAARQAEDY 336
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 337 FRTVFQERALPEDVPTVAVARaklEDGRMWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDVDAAVTVRD-----G 411
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSA---AEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDllhggY 393
                         410
                  ....*....|....*.
gi 1900939932 412 MVVQVGKRKFAKVVLQ 427
Cdd:COG0162   394 LVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
20-427 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 556.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  20 QEREVERQLAviargAAEILPEDELRRKLARSVATGRPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDF 99
Cdd:PRK13354    1 MKMNILEQLK-----WRGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 100 TGRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEK 178
Cdd:PRK13354   76 TGKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 179 RYKAGQPISLHEFFYPLMQGYDSVAL----ESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKS 254
Cdd:PRK13354  156 RLEREQGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADG-TKMGKS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 255 LGNYIGISE---PPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRMYHGEEAAR 331
Cdd:PRK13354  235 AGGAIWLDPektSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 332 QAEDYFRTVFQERALPE-DVPTVAVARAKLedgrmWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDVDAAVTVRD 410
Cdd:PRK13354  314 EAEKIFKALFSGDVKPLkDIPTFEVSAETK-----NLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388
                         410       420
                  ....*....|....*....|..
gi 1900939932 411 -----GMVVQVGKRKFAKVVLQ 427
Cdd:PRK13354  389 afdgkFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
23-402 1.80e-145

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: 419.11  E-value: 1.80e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  23 EVERQLAVIARGAAEILP--EDELRRKLARsvatgrPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFT 100
Cdd:TIGR00234   1 MNNILLLLTKRGLEVQTPeeEKDLLKLLER------PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 101 GRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKR 179
Cdd:TIGR00234  75 ALIGDPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIrLLGKIFTVNRMLRRDAFSSR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 180 YKAGqpISLHEFFYPLMQGYDSVALESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYI 259
Cdd:TIGR00234 155 FEEN--ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISEPPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQglaDGTLHPRDAKMKLAHTLVRMYHGEEAARQAEDYFRT 339
Cdd:TIGR00234 232 SLDEGKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE---LKGPNPREVKENLALEITKYVHGPEAALAAEEISEA 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900939932 340 VFQERALPEDVPTVAVARaklEDGRMWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDV 402
Cdd:TIGR00234 309 IFSGGLNPDEVPIFRPEK---FGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
58-323 2.70e-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: 2.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  58 LKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLD 137
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 138 MD---RVELHFNSTWLAPLTFADVVKLAAQVTVARMLERDDFEKRYKAGQPISLHEFFYPLMQGYDSVALESDIELGGTD 214
Cdd:cd00805    81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYIGIS--EPPNEMYGKAMSVPDELMVKYFELVTDLSN 292
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIWDPvlDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1900939932 293 EEIAAIRQGLADGTLhPRDAKMKLAHTLVRM 323
Cdd:cd00805   240 EEIEELEEEHAEGPL-PRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
55-342 3.88e-100

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 300.35  E-value: 3.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  55 GRPLKVKLGLDPSAPdIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDPTgKSETRKPLTEEQVKANArtYVEQFAK 134
Cdd:pfam00579   3 NRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLAC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 135 VLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKRYKAGQPISLHEFFYPLMQGYDSVALESDIELGGT 213
Cdd:pfam00579  79 GLDPEKAEIVNNSDWLEHLELAWLLrDLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 214 DQKFNLLMGRHLQEAFGQE---PQVILMMPLLEGLDGVKKMSKSLGN----YIGISEPPNEMYGKAMSVPDELMVKYFEL 286
Cdd:pfam00579 159 DQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLKL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939932 287 VTDLSNEEIAAIRQGLADGTlhPRDAKMKLAHTLVRMYHGEEAARQAEDYFRTVFQ 342
Cdd:pfam00579 239 FTFLSNEEIEILEAELGKSP--YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
365-420 2.39e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 44.51  E-value: 2.39e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939932  365 MWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTdvDAAVTVRDGMVVQVGKRK 420
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVT--KPSYIVKPGDVISVRGKE 54
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
27-427 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: 615.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  27 QLAVIARGAAEILPEDELRRKLArsvatGRPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDP 106
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 107 TGKSETRKPLTEEQVKANARTYVEQFAKVLDMD--RVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKRYKAG 183
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 184 QPISLHEFFYPLMQGYDSVAL----ESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYI 259
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISE---PPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRMYHGEEAARQAEDY 336
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 337 FRTVFQERALPEDVPTVAVARaklEDGRMWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDVDAAVTVRD-----G 411
Cdd:COG0162   317 FEALFGKGELPDDLPEVELSA---AEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDllhggY 393
                         410
                  ....*....|....*.
gi 1900939932 412 MVVQVGKRKFAKVVLQ 427
Cdd:COG0162   394 LVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
20-427 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 556.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  20 QEREVERQLAviargAAEILPEDELRRKLARSVATGRPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDF 99
Cdd:PRK13354    1 MKMNILEQLK-----WRGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 100 TGRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEK 178
Cdd:PRK13354   76 TGKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 179 RYKAGQPISLHEFFYPLMQGYDSVAL----ESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKS 254
Cdd:PRK13354  156 RLEREQGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADG-TKMGKS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 255 LGNYIGISE---PPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRMYHGEEAAR 331
Cdd:PRK13354  235 AGGAIWLDPektSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 332 QAEDYFRTVFQERALPE-DVPTVAVARAKLedgrmWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDVDAAVTVRD 410
Cdd:PRK13354  314 EAEKIFKALFSGDVKPLkDIPTFEVSAETK-----NLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388
                         410       420
                  ....*....|....*....|..
gi 1900939932 411 -----GMVVQVGKRKFAKVVLQ 427
Cdd:PRK13354  389 afdgkFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
23-402 1.80e-145

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: 419.11  E-value: 1.80e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  23 EVERQLAVIARGAAEILP--EDELRRKLARsvatgrPLKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFT 100
Cdd:TIGR00234   1 MNNILLLLTKRGLEVQTPeeEKDLLKLLER------PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 101 GRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKR 179
Cdd:TIGR00234  75 ALIGDPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIrLLGKIFTVNRMLRRDAFSSR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 180 YKAGqpISLHEFFYPLMQGYDSVALESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYI 259
Cdd:TIGR00234 155 FEEN--ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISEPPNEMYGKAMSVPDELMVKYFELVTDLSNEEIAAIRQglaDGTLHPRDAKMKLAHTLVRMYHGEEAARQAEDYFRT 339
Cdd:TIGR00234 232 SLDEGKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE---LKGPNPREVKENLALEITKYVHGPEAALAAEEISEA 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900939932 340 VFQERALPEDVPTVAVARaklEDGRMWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTDV 402
Cdd:TIGR00234 309 IFSGGLNPDEVPIFRPEK---FGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
58-323 2.70e-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: 2.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  58 LKVKLGLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLD 137
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 138 MD---RVELHFNSTWLAPLTFADVVKLAAQVTVARMLERDDFEKRYKAGQPISLHEFFYPLMQGYDSVALESDIELGGTD 214
Cdd:cd00805    81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGvKKMSKSLGNYIGIS--EPPNEMYGKAMSVPDELMVKYFELVTDLSN 292
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIWDPvlDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1900939932 293 EEIAAIRQGLADGTLhPRDAKMKLAHTLVRM 323
Cdd:cd00805   240 EEIEELEEEHAEGPL-PRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
55-342 3.88e-100

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 300.35  E-value: 3.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  55 GRPLKVKLGLDPSAPdIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDPTgKSETRKPLTEEQVKANArtYVEQFAK 134
Cdd:pfam00579   3 NRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLAC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 135 VLDMDRVELHFNSTWLAPLTFADVV-KLAAQVTVARMLERDDFEKRYKAGQPISLHEFFYPLMQGYDSVALESDIELGGT 213
Cdd:pfam00579  79 GLDPEKAEIVNNSDWLEHLELAWLLrDLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 214 DQKFNLLMGRHLQEAFGQE---PQVILMMPLLEGLDGVKKMSKSLGN----YIGISEPPNEMYGKAMSVPDELMVKYFEL 286
Cdd:pfam00579 159 DQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLKL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939932 287 VTDLSNEEIAAIRQGLADGTlhPRDAKMKLAHTLVRMYHGEEAARQAEDYFRTVFQ 342
Cdd:pfam00579 239 FTFLSNEEIEILEAELGKSP--YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
63-323 1.07e-39

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: 143.21  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  63 GLDPSAPDIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRIGDPTGKSETRKPLTEEQVKANARTYVEQFAKVLDMD--- 139
Cdd:cd00395     5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFEdpt 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 140 RVELHFNSTWLAPLTFADVVK-LAAQVTVARMLERDDFEKRYKAGqpISLHEFFYPLMQGYD----SVALESDIELGGTD 214
Cdd:cd00395    85 QATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPGGSD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGRHLQEAF-GQEPQVILMMPLLEGLDGvKKMSKSLGN---YIGISEPPNEMYGKAMSVPDELMVKYFELVTDL 290
Cdd:cd00395   163 QWGNITLGRELARRFnGFTIAEGLTIPLVTKLDG-PKFGKSESGpkwLDTEKTSPYEFYQFWINAVDSDVINILKYFTFL 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1900939932 291 SNEEIAAIRQGLADGTlHPRDAKMKLAHTLVRM 323
Cdd:cd00395   242 SKEEIERLEQEQYEAP-GYRVAQKTLAEEVTKT 273
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
24-323 2.13e-26

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 108.41  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  24 VERQLAVIARGAAEILPEDELRRKLArsvaTGRPLKVKLGLDPSAPdIHIGHTVVLQKLRQFQELGHTVQLIIGDFTGRI 103
Cdd:PRK08560    1 IEERLELITRNTEEVVTEEELRELLE----SKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 104 GDptgKSetrkplTEEQVKANARTYVEQFAKV-LDMDRVELHFNSTW-LAPLTFADVVKLAAQVTVARMLERDDFEKRyK 181
Cdd:PRK08560   76 ND---KG------DLEEIRKVAEYNKKVFEALgLDPDKTEFVLGSEFqLDKEYWLLVLKLAKNTTLARARRSMTIMGR-R 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 182 AGQPiSLHEFFYPLMQGYDSVALESDIELGGTDQKFNLLMGRHLQEAFGQEPQVILMMPLLEGLDGV-KKMSKS-LGNYI 259
Cdd:PRK08560  146 MEEP-DVSKLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgIKMSKSkPGSAI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 260 GISEPPNEMYGKAMSV---PDEL-------MVKYF------ELVT--------DLSNEEIAAIRQGLADGTLHPRDAKMK 315
Cdd:PRK08560  225 FVHDSPEEIRRKIKKAycpPGEVegnpvleIAKYHifprydPFVIerpekyggDLEYESYEELERDYAEGKLHPMDLKNA 304

                  ....*...
gi 1900939932 316 LAHTLVRM 323
Cdd:PRK08560  305 VAEYLIEI 312
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
63-323 1.99e-12

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: 67.22  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  63 GLDPSAPdIHIGHTV-VLQKLRQFQELGHTVQLIIGDFtgrigdptgKSETRKPLTEEQVKANARTYVEQFAKV-LDMDR 140
Cdd:cd00806     5 GIQPSGS-LHLGHYLgAFRFWVWLQEAGYELFFFIADL---------HALTVKQLDPEELRQNTRENAKDYLACgLDPEK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 141 VELHFNSTW--LAPLtfadVVKLAAQVTVARmLER----DDfEKRYKAGQPISLheFFYPLMQGYDSVALESDIELGGTD 214
Cdd:cd00806    75 STIFFQSDVpeHYEL----AWLLSCVVTFGE-LERmtgfKD-KSAQGESVNIGL--LTYPVLQAADILLYKACLVPVGID 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGRHLQEAFGQ-------EPQVIL-----MMPLLeglDGVKKMSKSLG-NYIGISEPPNEMYGKAMS------- 274
Cdd:cd00806   147 QDPHLELTRDIARRFNKlygeifpKPAALLskgafLPGLQ---GPSKKMSKSDPnNAIFLTDSPKEIKKKIMKaatdggr 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1900939932 275 --------VPDEL-MVKYFELVTDLSNEEIAAIRQGLAdGTLHPRDAKMKLAHTLVRM 323
Cdd:cd00806   224 tehrrdggGPGVSnLVEIYSAFFNDDDEELEEIDEYRS-GGLGYGECKKLLAEAIQEF 280
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
215-323 7.56e-09

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: 56.98  E-value: 7.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGRHLQEafgqePQVIL--MMPLLEGLDGVKKMSKSLGNYIGISEPPNEMYGKAMSV---PDEL---------- 279
Cdd:COG0180   163 RRFNHRYGEVFPE-----PEALIpeEGARIPGLDGRKKMSKSYGNTINLLDDPKEIRKKIKSAvtdSERLryddpgkpev 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1900939932 280 --MVKYFELVTDlsNEEIAAIRQGLADGTLHPRDAKMKLAHTLVRM 323
Cdd:COG0180   238 cnLFTIYSAFSG--KEEVEELEAEYRAGGIGYGDLKKALAEAVVEF 281
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
63-274 1.92e-08

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: 55.80  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  63 GLDPSAPdIHIGHTVVLQKLRQFQELGHTVQLIIGD---FTGRIGDPtgksETRKPLTEEQVKanarTYVeqfAKVLDMD 139
Cdd:TIGR00233   8 GIQPSGK-MHLGHYLGAIQTKWLQQFGVELFICIADlhaITVKQTDP----DALRKAREELAA----DYL---AVGLDPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 140 RVELHFNSTWLAplTFADVVKLAAQVTVARMLERDDF-EKRYKAGQPISLheFFYPLMQGYDSVALESDIELGGTDQKFN 218
Cdd:TIGR00233  76 KTFIFLQSDYPE--HYELAWLLSCQVTFGELKRMTQFkDKSQAENVPIGL--LSYPVLQAADILLYQADLVPVGIDQDQH 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939932 219 LLMGRHLQEAFGQE-------PQVIL--MMPLLEGLDGvKKMSKSLGN-YIGISEPPNEMYGKAMS 274
Cdd:TIGR00233 152 LELTRDLAERFNKKfknffpkPESLIskFFPRLMGLSG-KKMSKSDPNsAIFLTDTPKQIKKKIRK 216
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
365-426 2.02e-08

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: 50.71  E-value: 2.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900939932 365 MWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTdvDAAVTVRDGMVVQVGKRKFAKVVL 426
Cdd:cd00165     1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVT--KPSYKVKPGDVIEVDGKSIEEDIV 60
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
165-274 7.81e-08

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 53.70  E-value: 7.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 165 VTVARmLERD----------DFEKRYKAGqpislheFF-YPLMQGYDSVALESDIELGGTDQ------------KFNLLM 221
Cdd:PRK12282   99 VTVAR-LERNptvkteiaqkGFGRSIPAG-------FLtYPVSQAADITAFKATLVPVGDDQlpmieqtreivrRFNSLY 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900939932 222 GRhlqeAFGQEPQVIL-MMPLLEGLDGVKKMSKSLGNYIGISEPPNEMYGKAMS 274
Cdd:PRK12282  171 GT----DVLVEPEALLpEAGRLPGLDGKAKMSKSLGNAIYLSDDADTIKKKVMS 220
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
184-350 2.68e-07

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 52.39  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 184 QPISlhEFFYPLMQGYDSVALESDIELGGTDQ-KFNLLMGRHLQEAFGQEPQVILMMPLLEGL-DGVKKMSKSLGN---Y 258
Cdd:PTZ00126  191 QPCA--QILYPCMQCADIFYLKADICQLGMDQrKVNMLAREYCDKKKIKKKPIILSHHMLPGLlEGQEKMSKSDPNsaiF 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 259 IGISE------------PPNEMYGK-AMSVPDELMVKYFELVTDLSNEE---------IAAIRQGLADGTLHPRDAKMKL 316
Cdd:PTZ00126  269 MEDSEedvnrkikkaycPPGVIEGNpILAYFKSIVFPAFNSFTVLRKEKnggdvtyttYEELEKDYLSGALHPGDLKPAL 348
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1900939932 317 AHTLVRMYhgeEAARqaeDYFRTVFQERALPEDV 350
Cdd:PTZ00126  349 AKYLNLML---QPVR---DHFQNNPEAKSLLSEV 376
S4 smart00363
S4 RNA-binding domain;
365-420 2.39e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 44.51  E-value: 2.39e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939932  365 MWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTdvDAAVTVRDGMVVQVGKRK 420
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVT--KPSYIVKPGDVISVRGKE 54
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
365-414 4.88e-06

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: 43.25  E-value: 4.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1900939932 365 MWIVRLLVELGLVGSNGEGRRMIQQGGVRIDGEKVTdvDAAVTVRDGMVV 414
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVK--DPSYRVKPGDEI 48
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
215-323 7.90e-06

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 47.39  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 215 QKFNLLMGrhlqEAFgQEPQVIL--MMPLLEGLDG-VKKMSKSLG---NYIGISEPPNEMYGKAMSV---PDELMVKYFE 285
Cdd:PRK00927  160 RRFNNLYG----EVF-PVPEPLIpkVGARVMGLDGpTKKMSKSDPndnNTINLLDDPKTIAKKIKKAvtdSERLREIRYD 234
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1900939932 286 LVTD------------LSNEEIAAIRQGLADGTLHPRDAKMKLAHTLVRM 323
Cdd:PRK00927  235 LPNKpevsnlltiysaLSGESIEELEAEYEAGGKGYGDFKKDLAEAVVEF 284
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
46-274 3.69e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 42.54  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932  46 RKLARSVATGRPLKVKLGLDPSAPdIHIGHTVVLQKLRQFQELGHTVQLIIGDFtgrigdptgKSETRKPLTEEQVKANA 125
Cdd:PRK12285   55 DKILEAYRNGKPFAVYTGFMPSGP-MHIGHKMVFDELKWHQEFGANVYIPIADD---------EAYAARGLSWEETREWA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 126 RTYVEQFAKV-LDMDRVELHFNS--TWLAPLTFadvvKLAAQVTVARMlerddfEKRYKAGQPISLHEFFYPLMQGYDsv 202
Cdd:PRK12285  125 YEYILDLIALgFDPDKTEIYFQSenIKVYDLAF----ELAKKVNFSEL------KAIYGFTGETNIGHIFYPATQAAD-- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 203 ALESDIELG--------GTDQKFNLLMGRHLQEAFGQEPQVI----LMMPLLEGLDGvKKMSKSLGN-YIGISEPPNEMY 269
Cdd:PRK12285  193 ILHPQLEEGpkptlvpvGIDQDPHIRLTRDIAERLHGGYGFIkpssTYHKFMPGLTG-GKMSSSKPEsAIYLTDDPETVK 271

                  ....*
gi 1900939932 270 GKAMS 274
Cdd:PRK12285  272 KKIMK 276
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
191-268 5.21e-04

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 42.02  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939932 191 FFYPLMQGYDSVALESDIELGGTDQ------------KFNLLMGrhlqEAFGQePQVIL-----MMPlleGLDGvKKMSK 253
Cdd:PRK12556  135 YTYPILMAADILLFQATHVPVGKDQiqhieiardiatYFNHTFG----DTFTL-PEYVIqeegaILP---GLDG-RKMSK 205
                          90
                  ....*....|....*
gi 1900939932 254 SLGNYIGISEPPNEM 268
Cdd:PRK12556  206 SYGNVIPLFAEQEKL 220
 
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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