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Conserved domains on  [gi|1049326241|ref|WP_065822972|]
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tyrosine--tRNA ligase [Photorhabdus australis]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11415010)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 4-424 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: 661.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   4 NNLIKQLQERGLIAQVTDEdALAERLAQGPVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162     1 MNLLLELIWRGLIEQITDE-ELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDCgeNSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162    80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 DDvGISFTEFSYNLLQSYDFVRLNEEHDVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162   158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEDKNSGKAPRAQYVLAEQVTGMVHGEEGLAAAKRI 323
Cdd:COG0162   237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 324 TESLFS-GAVAdlteadfaqlaqDGMPVIELEK---GADLQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFT 399
Cdd:COG0162   317 FEALFGkGELP------------DDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                         410       420
                  ....*....|....*....|....*
gi 1049326241 400 DNNCLFGRYTLLRRGKKHDCLICWK 424
Cdd:COG0162   385 AGDLLHGGYLVLRVGKKKFALVKLK 409
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 4-424 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: 661.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   4 NNLIKQLQERGLIAQVTDEdALAERLAQGPVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162     1 MNLLLELIWRGLIEQITDE-ELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDCgeNSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162    80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 DDvGISFTEFSYNLLQSYDFVRLNEEHDVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162   158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEDKNSGKAPRAQYVLAEQVTGMVHGEEGLAAAKRI 323
Cdd:COG0162   237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 324 TESLFS-GAVAdlteadfaqlaqDGMPVIELEK---GADLQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFT 399
Cdd:COG0162   317 FEALFGkGELP------------DDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                         410       420
                  ....*....|....*....|....*
gi 1049326241 400 DNNCLFGRYTLLRRGKKHDCLICWK 424
Cdd:COG0162   385 AGDLLHGGYLVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 5-424 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 573.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   5 NLIKQLQERGLIAQVTDEDALAERLAQG-PVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:PRK13354    4 NILEQLKWRGAINQETDEEKLRKSLKEGkPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDcgenSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:PRK13354   84 GKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE----KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLER 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 DdVGISFTEFSYNLLQSYDFVRLNEEHDVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:PRK13354  160 E-QGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEDKNsGKAPR-AQYVLAEQVTGMVHGEEGLAAAKR 322
Cdd:PRK13354  239 IWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLET-EPNPRdAKKVLAEEITKFVHGEEAAEEAEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 323 ITESLFSGAVADLTEADFAQLAQDGMPVIELekgadlqqaLVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTDNN 402
Cdd:PRK13354  318 IFKALFSGDVKPLKDIPTFEVSAETKNLVDL---------LVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388

                         410       420
                  ....*....|....*....|..
gi 1049326241 403 CLFGRYTLLRRGKKHDCLICWK 424
Cdd:PRK13354  389 AFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 4-401 1.90e-156

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: 446.84  E-value: 1.90e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   4 NNLIKQLQERGLIAQVTDEDALAERLAQGPVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDcgenSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:TIGR00234  82 GKSEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 ddvGISFTEFSYNLLQSYDFVRLNeehdVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:TIGR00234 158 ---NISLHEFIYPLLQAYDFVYLN----VDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPkktSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEdkNSGKAPRAQYVLAEQVTGMVHGEEGLAAAKRI 323
Cdd:TIGR00234 231 VSLDE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEI 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 324 TESLFSGavadlteadfaQLAQDGMPVIELEKGA---DLQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTD 400
Cdd:TIGR00234 306 SEAIFSG-----------GLNPDEVPIFRPEKFGgpiTLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKE 374


                  .
gi 1049326241 401 N 401
Cdd:TIGR00234 375 L 375
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 34-308 9.13e-131

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: 377.33  E-value: 9.13e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  34 VSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPSFKATERKLNTADTVKEWVEKIRRQVSPFLD 113
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 114 FDcGENSAKTANNYDWFGGMDVLTFLRdIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQSYDFVRLneehDVE 193
Cdd:cd00805    81 FI-PPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEEE-GISFSEFIYPLLQAYDFVYL----DVD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 194 LQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGAVWlDPKKTSPYKFYQFWINTADADVYRFLK 273
Cdd:cd00805   154 LQLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1049326241 274 FFTFMSLEDINALEEEDKNSGKAPRAQYVLAEQVT 308
Cdd:cd00805   233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELT 267
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
29-329 3.59e-105

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 313.06  E-value: 3.59e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  29 LAQGPVSLYCGFDPTADsLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPSfKATERKLNTADTVKEWVekIRRQV 108
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 109 SPFLDFDCgensAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQSYDFVRLNe 188
Cdd:pfam00579  77 ACGLDPEK----AEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGP-GISLGEFTYPLLQAYDILLLK- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 189 ehdVELQIGGSDQWGNITSGIDLTRRINQK---QVFGMTVPLITKSDGT-KFGKTEGG-AVWLDPKKTSPYKFYQFWINT 263
Cdd:pfam00579 151 ---ADLQPGGSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTD 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049326241 264 ADADVYRFLKFFTFMSLEDINALEEEDKNSgKAPRAQYVLAEQVTGMVHGEEGLAAAKRITESLFS 329
Cdd:pfam00579 228 PDREVRKDLKLFTFLSNEEIEILEAELGKS-PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
359-416 2.69e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 49.90  E-value: 2.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049326241  359 LQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTDNNCLFGRYTLLRRGKK 416
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 60
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 4-424 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: 661.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   4 NNLIKQLQERGLIAQVTDEdALAERLAQGPVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162     1 MNLLLELIWRGLIEQITDE-ELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDCgeNSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162    80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 DDvGISFTEFSYNLLQSYDFVRLNEEHDVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162   158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEDKNSGKAPRAQYVLAEQVTGMVHGEEGLAAAKRI 323
Cdd:COG0162   237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 324 TESLFS-GAVAdlteadfaqlaqDGMPVIELEK---GADLQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFT 399
Cdd:COG0162   317 FEALFGkGELP------------DDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                         410       420
                  ....*....|....*....|....*
gi 1049326241 400 DNNCLFGRYTLLRRGKKHDCLICWK 424
Cdd:COG0162   385 AGDLLHGGYLVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 5-424 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 573.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   5 NLIKQLQERGLIAQVTDEDALAERLAQG-PVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:PRK13354    4 NILEQLKWRGAINQETDEEKLRKSLKEGkPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDcgenSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:PRK13354   84 GKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE----KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLER 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 DdVGISFTEFSYNLLQSYDFVRLNEEHDVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:PRK13354  160 E-QGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEDKNsGKAPR-AQYVLAEQVTGMVHGEEGLAAAKR 322
Cdd:PRK13354  239 IWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLET-EPNPRdAKKVLAEEITKFVHGEEAAEEAEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 323 ITESLFSGAVADLTEADFAQLAQDGMPVIELekgadlqqaLVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTDNN 402
Cdd:PRK13354  318 IFKALFSGDVKPLKDIPTFEVSAETKNLVDL---------LVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPED 388

                         410       420
                  ....*....|....*....|..
gi 1049326241 403 CLFGRYTLLRRGKKHDCLICWK 424
Cdd:PRK13354  389 AFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 4-401 1.90e-156

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: 446.84  E-value: 1.90e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241   4 NNLIKQLQERGLIAQVTDEDALAERLAQGPVSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPS 83
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  84 FKATERKLNTADTVKEWVEKIRRQVSPFLDFDcgenSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:TIGR00234  82 GKSEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 164 ddvGISFTEFSYNLLQSYDFVRLNeehdVELQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGA 243
Cdd:TIGR00234 158 ---NISLHEFIYPLLQAYDFVYLN----VDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 244 VWLDPkktSPYKFYQFWINTADADVYRFLKFFTFMSLEDINALEEEdkNSGKAPRAQYVLAEQVTGMVHGEEGLAAAKRI 323
Cdd:TIGR00234 231 VSLDE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEI 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 324 TESLFSGavadlteadfaQLAQDGMPVIELEKGA---DLQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTD 400
Cdd:TIGR00234 306 SEAIFSG-----------GLNPDEVPIFRPEKFGgpiTLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKE 374


                  .
gi 1049326241 401 N 401
Cdd:TIGR00234 375 L 375
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 34-308 9.13e-131

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: 377.33  E-value: 9.13e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  34 VSLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPSFKATERKLNTADTVKEWVEKIRRQVSPFLD 113
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 114 FDcGENSAKTANNYDWFGGMDVLTFLRdIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQSYDFVRLneehDVE 193
Cdd:cd00805    81 FI-PPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEEE-GISFSEFIYPLLQAYDFVYL----DVD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 194 LQIGGSDQWGNITSGIDLTRRINQKQVFGMTVPLITKSDGTKFGKTEGGAVWlDPKKTSPYKFYQFWINTADADVYRFLK 273
Cdd:cd00805   154 LQLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1049326241 274 FFTFMSLEDINALEEEDKNSGKAPRAQYVLAEQVT 308
Cdd:cd00805   233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELT 267
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 35-308 8.47e-111

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: 326.57  E-value: 8.47e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  35 SLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPSFKATERKLNTADTVKEWVEKIRRQVSPFLDF 114
Cdd:cd00395     1 TLYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 115 DCGeNSAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNRddvGISFTEFSYNLLQSYDFVRLNEEHDVEL 194
Cdd:cd00395    81 EDP-TQATLFNNSDWPGPLAHIQFLRDLGKHVYVNYMERKTSFQSRSEE---GISATEFTYPPLQAADFLLLNTTEGCDI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 195 QIGGSDQWGNITSGIDLTRRIN-QKQVFGMTVPLITKSDGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLK 273
Cdd:cd00395   157 QPGGSDQWGNITLGRELARRFNgFTIAEGLTIPLVTKLDGPKFGKSESGPKWLDTEKTSPYEFYQFWINAVDSDVINILK 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1049326241 274 FFTFMSLEDINALEEEdKNSGKAPR-AQYVLAEQVT 308
Cdd:cd00395   237 YFTFLSKEEIERLEQE-QYEAPGYRvAQKTLAEEVT 271
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
29-329 3.59e-105

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 313.06  E-value: 3.59e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  29 LAQGPVSLYCGFDPTADsLHLGHLVPLLCLKRFQLAGHKPVALVGGATGLIGDPSfKATERKLNTADTVKEWVekIRRQV 108
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 109 SPFLDFDCgensAKTANNYDWFGGMDVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQSYDFVRLNe 188
Cdd:pfam00579  77 ACGLDPEK----AEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGP-GISLGEFTYPLLQAYDILLLK- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 189 ehdVELQIGGSDQWGNITSGIDLTRRINQK---QVFGMTVPLITKSDGT-KFGKTEGG-AVWLDPKKTSPYKFYQFWINT 263
Cdd:pfam00579 151 ---ADLQPGGSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTD 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049326241 264 ADADVYRFLKFFTFMSLEDINALEEEDKNSgKAPRAQYVLAEQVTGMVHGEEGLAAAKRITESLFS 329
Cdd:pfam00579 228 PDREVRKDLKLFTFLSNEEIEILEAELGKS-PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 36-240 4.29e-13

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: 66.35  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241  36 LYCGFDPTAdSLHLGHLVPLLCLKRFQLA------GHKPVALVGGATGLIGDPSFKATErklNTADTVKEWVEKIRRQvs 109
Cdd:cd00802     2 TFSGITPNG-YLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPANKKGE---NAKAFVERWIERIKED-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326241 110 pfldfdcgensaktannydwfggmdvltflrdigkhfsvnqminkeavkqrlnrddvgisfteFSYNLLQSYDFVRLNEE 189
Cdd:cd00802    76 ---------------------------------------------------------------VEYMFLQAADFLLLYET 92

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1049326241 190 HDvELQIGGSDQWGNITSGIDLTRRIN-QKQVFGMTVPLITKSDGTKFGKTE 240
Cdd:cd00802    93 EC-DIHLGGSDQLGHIELGLELLKKAGgPARPFGLTFGRVMGADGTKMSKSK 143
S4 smart00363
S4 RNA-binding domain;
359-416 2.69e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 49.90  E-value: 2.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049326241  359 LQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEYVFTDNNCLFGRYTLLRRGKK 416
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 60
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 359-396 7.65e-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: 49.17  E-value: 7.65e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1049326241 359 LQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEY 396
Cdd:cd00165     3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSY 40
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 359-396 4.10e-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: 43.63  E-value: 4.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1049326241 359 LQQALVNAGLVPSRGQARTMISSNAVAVNGEKQSEPEY 396
Cdd:pfam01479   3 LDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSY 40
S4_2 pfam13275
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 359-416 1.24e-03

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


Pssm-ID: 433078 [Multi-domain]  Cd Length: 65  Bit Score: 37.03  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049326241 359 LQQALVNAGLVPSRGQARTMISSNAVAVNGekqsEPEYvftdnnclfgrytllRRGKK 416
Cdd:pfam13275  10 LGQLLKLAGLVESGGEAKWFIAEGEVLVNG----EVET---------------RRGKK 48
PLN02486 PLN02486
aminoacyl-tRNA ligase
 36-64 7.62e-03

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 38.19  E-value: 7.62e-03
                          10        20
                  ....*....|....*....|....*....
gi 1049326241  36 LYCGFDPTADSLHLGHLVPLLCLKRFQLA 64
Cdd:PLN02486   76 LYTGRGPSSEALHLGHLIPFMFTKYLQDA 104
 
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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