|
Name |
Accession |
Description |
Interval |
E-value |
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
1-417 |
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: 650.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 1 MTIFEELKARGLVFQTTDEEaLKKSLDDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPS 80
Cdd:COG0162 1 MNLLLELIWRGLIEQITDEE-LREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 81 FKDDERSLQTKETVKNWVQSIRSQLERFIDFkhGDNKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIE- 159
Cdd:COG0162 80 GKSEERKLLTEEQVAENAETIKEQVFKFLDF--DDNKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLEs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 160 -TGISYTEFAYQIMQGYDFYVLNQEHAVTLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAV 238
Cdd:COG0162 158 gQGISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNAI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 239 WLDADKTSPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKIT 318
Cdd:COG0162 238 WLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 319 EQLFaghikslSAKELKQglsNVPNYAV-KSNDNHNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:COG0162 318 EALF-------GKGELPD---DLPEVELsAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGD 387
|
410 420
....*....|....*....|
gi 97202191 398 KIDNELTVIRRGKKKYFVLT 417
Cdd:COG0162 388 LLHGGYLVLRVGKKKFALVK 407
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
1-414 |
0e+00 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 558.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 1 MTIFEELKARGLVFQTTDEEALKKSL-DDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDP 79
Cdd:PRK13354 3 MNILEQLKWRGAINQETDEEKLRKSLkEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 80 SFKDDERSLQTKETVKNWVQSIRSQLERFIDFkhgdNKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRI- 158
Cdd:PRK13354 83 SGKSKERKLLTDEQVQHNAKTYTEQIFKLFDF----EKTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 159 -ETGISYTEFAYQIMQGYDFYVLNQEHAVTLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNA 237
Cdd:PRK13354 159 rEQGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 238 VWLDADKTSPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKI 317
Cdd:PRK13354 239 IWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 318 TEQLFAGHIKSlsakelkqgLSNVPNYAVkSNDNHNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:PRK13354 319 FKALFSGDVKP---------LKDIPTFEV-SAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388
|
410
....*....|....*..
gi 97202191 398 KIDNELTVIRRGKKKYF 414
Cdd:PRK13354 389 AFDGKFVILRRGKKKFF 405
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
3-397 |
1.26e-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: 388.68 E-value: 1.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 3 IFEELKARGLVFQTTDEEALKKSLDDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSFK 82
Cdd:TIGR00234 4 ILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 83 DDERSLQTKETVKNWVQSIRSQLERFIDFKhgdnKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIETGI 162
Cdd:TIGR00234 84 SEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 163 SYTEFAYQIMQGYDFYVLNQEhavtLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAVWLDA 242
Cdd:TIGR00234 160 SLHEFIYPLLQAYDFVYLNVD----LQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGAVSLDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 243 DktsPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIrvKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKITEQLF 322
Cdd:TIGR00234 236 G---KYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQL--VELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIF 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 97202191 323 AGHIK--SLSAKELKQGLSNVpnyavksndnhNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:TIGR00234 311 SGGLNpdEVPIFRPEKFGGPI-----------TLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKELE 376
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
31-304 |
6.08e-122 |
|
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: 354.60 E-value: 6.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 31 VSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSFKDDERSLQTKETVKNWVQSIRSQLERFID 110
Cdd:cd00805 1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 111 FkHGDNKAQMVNNYDWMGKITFIDFLRdVGKYFTVNYMMSKESVKKRIET--GISYTEFAYQIMQGYDFYVLNqehaVTL 188
Cdd:cd00805 81 F-IPPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEeeGISFSEFIYPLLQAYDFVYLD----VDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 189 QVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAVWlDADKTSPYEMYQFWLNVMDADAIRFLKI 268
Cdd:cd00805 155 QLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLKL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 97202191 269 FTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTF 304
Cdd:cd00805 234 FTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
26-323 |
1.92e-87 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 267.61 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 26 LDDGQVSFYTGYDPTADsLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSfKDDERSLQTKETVKNWvqSIRSQL 105
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 106 ERFIDFKhgdnKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIET--GISYTEFAYQIMQGYDFYVLNQe 183
Cdd:pfam00579 77 ACGLDPE----KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQgpGISLGEFTYPLLQAYDILLLKA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 184 havTLQVGGSDQWGNMTAGTELIRR---KANKTAHVITVPLITDATG-KKFGKSEGN-AVWLDADKTSPYEMYQFWLNVM 258
Cdd:pfam00579 152 ---DLQPGGSDQWGNIELGRDLARRfnkKIFKKPVGLTNPLLTGLDGgKKMSKSAGNsAIFLDDDPESVYKKIQKAYTDP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 97202191 259 DADAIRFLKIFTFLSLDEIEDIrVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKITEQLFA 323
Cdd:pfam00579 229 DREVRKDLKLFTFLSNEEIEIL-EAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
357-411 |
2.99e-06 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 44.12 E-value: 2.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 97202191 357 LLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQDKIDNELTVIRRGKK 411
Cdd:smart00363 6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 60
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
1-417 |
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: 650.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 1 MTIFEELKARGLVFQTTDEEaLKKSLDDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPS 80
Cdd:COG0162 1 MNLLLELIWRGLIEQITDEE-LREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 81 FKDDERSLQTKETVKNWVQSIRSQLERFIDFkhGDNKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIE- 159
Cdd:COG0162 80 GKSEERKLLTEEQVAENAETIKEQVFKFLDF--DDNKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLEs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 160 -TGISYTEFAYQIMQGYDFYVLNQEHAVTLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAV 238
Cdd:COG0162 158 gQGISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNAI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 239 WLDADKTSPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKIT 318
Cdd:COG0162 238 WLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 319 EQLFaghikslSAKELKQglsNVPNYAV-KSNDNHNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:COG0162 318 EALF-------GKGELPD---DLPEVELsAAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGD 387
|
410 420
....*....|....*....|
gi 97202191 398 KIDNELTVIRRGKKKYFVLT 417
Cdd:COG0162 388 LLHGGYLVLRVGKKKFALVK 407
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
1-414 |
0e+00 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 558.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 1 MTIFEELKARGLVFQTTDEEALKKSL-DDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDP 79
Cdd:PRK13354 3 MNILEQLKWRGAINQETDEEKLRKSLkEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 80 SFKDDERSLQTKETVKNWVQSIRSQLERFIDFkhgdNKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRI- 158
Cdd:PRK13354 83 SGKSKERKLLTDEQVQHNAKTYTEQIFKLFDF----EKTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 159 -ETGISYTEFAYQIMQGYDFYVLNQEHAVTLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNA 237
Cdd:PRK13354 159 rEQGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 238 VWLDADKTSPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKI 317
Cdd:PRK13354 239 IWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 318 TEQLFAGHIKSlsakelkqgLSNVPNYAVkSNDNHNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:PRK13354 319 FKALFSGDVKP---------LKDIPTFEV-SAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388
|
410
....*....|....*..
gi 97202191 398 KIDNELTVIRRGKKKYF 414
Cdd:PRK13354 389 AFDGKFVILRRGKKKFF 405
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
3-397 |
1.26e-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: 388.68 E-value: 1.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 3 IFEELKARGLVFQTTDEEALKKSLDDGQVSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSFK 82
Cdd:TIGR00234 4 ILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 83 DDERSLQTKETVKNWVQSIRSQLERFIDFKhgdnKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIETGI 162
Cdd:TIGR00234 84 SEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 163 SYTEFAYQIMQGYDFYVLNQEhavtLQVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAVWLDA 242
Cdd:TIGR00234 160 SLHEFIYPLLQAYDFVYLNVD----LQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGAVSLDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 243 DktsPYEMYQFWLNVMDADAIRFLKIFTFLSLDEIEDIrvKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKITEQLF 322
Cdd:TIGR00234 236 G---KYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQL--VELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIF 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 97202191 323 AGHIK--SLSAKELKQGLSNVpnyavksndnhNIVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQD 397
Cdd:TIGR00234 311 SGGLNpdEVPIFRPEKFGGPI-----------TLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKELE 376
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
31-304 |
6.08e-122 |
|
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: 354.60 E-value: 6.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 31 VSFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSFKDDERSLQTKETVKNWVQSIRSQLERFID 110
Cdd:cd00805 1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 111 FkHGDNKAQMVNNYDWMGKITFIDFLRdVGKYFTVNYMMSKESVKKRIET--GISYTEFAYQIMQGYDFYVLNqehaVTL 188
Cdd:cd00805 81 F-IPPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEeeGISFSEFIYPLLQAYDFVYLD----VDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 189 QVGGSDQWGNMTAGTELIRRKANKTAHVITVPLITDATGKKFGKSEGNAVWlDADKTSPYEMYQFWLNVMDADAIRFLKI 268
Cdd:cd00805 155 QLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLKL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 97202191 269 FTFLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTF 304
Cdd:cd00805 234 FTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
32-304 |
3.02e-106 |
|
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: 315.01 E-value: 3.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 32 SFYTGYDPTADSLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSFKDDERSLQTKETVKNWVQSIRSQLERFIDF 111
Cdd:cd00395 1 TLYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 112 KhGDNKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIETGISYTEFAYQIMQGYDFYVLNQEHAVTLQVG 191
Cdd:cd00395 81 E-DPTQATLFNNSDWPGPLAHIQFLRDLGKHVYVNYMERKTSFQSRSEEGISATEFTYPPLQAADFLLLNTTEGCDIQPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 192 GSDQWGNMTAGTELIRRKANKT-AHVITVPLITDATGKKFGKSEGNAVWLDADKTSPYEMYQFWLNVMDADAIRFLKIFT 270
Cdd:cd00395 160 GSDQWGNITLGRELARRFNGFTiAEGLTIPLVTKLDGPKFGKSESGPKWLDTEKTSPYEFYQFWINAVDSDVINILKYFT 239
|
250 260 270
....*....|....*....|....*....|....
gi 97202191 271 FLSLDEIEDIRVKFEAAPHERLAQKILAKEVVTF 304
Cdd:cd00395 240 FLSKEEIERLEQEQYEAPGYRVAQKTLAEEVTKT 273
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
26-323 |
1.92e-87 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 267.61 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 26 LDDGQVSFYTGYDPTADsLHLGHLVPILVMRHLQLAGHKPYALVGGATGLIGDPSfKDDERSLQTKETVKNWvqSIRSQL 105
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 106 ERFIDFKhgdnKAQMVNNYDWMGKITFIDFLRDVGKYFTVNYMMSKESVKKRIET--GISYTEFAYQIMQGYDFYVLNQe 183
Cdd:pfam00579 77 ACGLDPE----KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQgpGISLGEFTYPLLQAYDILLLKA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 184 havTLQVGGSDQWGNMTAGTELIRR---KANKTAHVITVPLITDATG-KKFGKSEGN-AVWLDADKTSPYEMYQFWLNVM 258
Cdd:pfam00579 152 ---DLQPGGSDQWGNIELGRDLARRfnkKIFKKPVGLTNPLLTGLDGgKKMSKSAGNsAIFLDDDPESVYKKIQKAYTDP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 97202191 259 DADAIRFLKIFTFLSLDEIEDIrVKFEAAPHERLAQKILAKEVVTFVHGQTAYQEAVKITEQLFA 323
Cdd:pfam00579 229 DREVRKDLKLFTFLSNEEIEIL-EAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
34-234 |
4.44e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 49.02 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 34 YTGYDPTAdSLHLGHLVPILVMRHLQLA------GHKPYALVGGATGLIGDPSfkdderslqtketVKNWvQSIRSQLER 107
Cdd:cd00802 3 FSGITPNG-YLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPA-------------NKKG-ENAKAFVER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 108 FIdfkhgdnkAQMVNNYDWMgkitfidflrdvgkyftvnymmskesvkkrietgisyTEFAYQIMQGYDFYvlnqehaVT 187
Cdd:cd00802 68 WI--------ERIKEDVEYM-------------------------------------FLQAADFLLLYETE-------CD 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 97202191 188 LQVGGSDQWGNMTAGTELIRR-KANKTAHVITVPLITDATGKKFGKSE 234
Cdd:cd00802 96 IHLGGSDQLGHIELGLELLKKaGGPARPFGLTFGRVMGADGTKMSKSK 143
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
354-416 |
5.45e-07 |
|
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: 46.86 E-value: 5.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 97202191 354 IVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQDKI----DNELTVIRRGKKKYFVL 416
Cdd:cd00165 3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIevdgKSIEEDIVYEDKKLLVV 69
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
357-411 |
2.99e-06 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 44.12 E-value: 2.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 97202191 357 LLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQDKIDNELTVIRRGKK 411
Cdd:smart00363 6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 60
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
354-399 |
1.38e-05 |
|
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: 42.09 E-value: 1.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 97202191 354 IVELLVTAGIVNSKRQAREDLQNGAIYINGERIQDLTYNLSQQDKI 399
Cdd:pfam01479 3 LDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPGDEI 48
|
|
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
10-88 |
2.48e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 46.28 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 97202191 10 RGLVFQTTDEEALKKSLDDGQVSF-YTGYDPTADSLHLGHLVPILVMRHLQLAGHKPyaLVGGATgligdpsfkDDERSL 88
Cdd:PLN02486 52 RGVFFAHRDLEEILDAYEKGEKFYlYTGRGPSSEALHLGHLIPFMFTKYLQDAFKVP--LVIQLT---------DDEKFL 120
|
|
|