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Conserved domains on  [gi|97202191|sp|Q8DS44|]
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RecName: Full=Tyrosine--tRNA ligase; AltName: Full=Tyrosyl-tRNA synthetase; Short=TyrRS

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 ...
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
 
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
 
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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