|
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
|
|
|