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Conserved domains on  [gi|490520624|ref|WP_004386091|]
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MULTISPECIES: tyrosine--tRNA ligase [Cronobacter]

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: 667.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   4 SNLIKQLQERGLVAQVTDEEaLAQRLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162    1 MNLLLELIWRGLIEQITDEE-LREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  84 FKATERKLNTEDTVQEWVDKIRRQVAPFLDFDCgeNSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162   80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 164 DDvGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162  158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLAAAKRI 323
Cdd:COG0162  237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 324 TESLF-NGNLnalseadfeqlaQDGVPMIEMEK---GADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFS 399
Cdd:COG0162  317 FEALFgKGEL------------PDDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                        410       420
                 ....*....|....*....|....*
gi 490520624 400 DSDRLFGRYTLLRRGKKNYCLVCWK 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: 667.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   4 SNLIKQLQERGLVAQVTDEEaLAQRLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162    1 MNLLLELIWRGLIEQITDEE-LREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  84 FKATERKLNTEDTVQEWVDKIRRQVAPFLDFDCgeNSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162   80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 164 DDvGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162  158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLAAAKRI 323
Cdd:COG0162  237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 324 TESLF-NGNLnalseadfeqlaQDGVPMIEMEK---GADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFS 399
Cdd:COG0162  317 FEALFgKGEL------------PDDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                        410       420
                 ....*....|....*....|....*
gi 490520624 400 DSDRLFGRYTLLRRGKKNYCLVCWK 424
Cdd:COG0162  385 AGDLLHGGYLVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 2-424 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 581.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   2 ASSNLIKQLQERGLVAQVTDEEALAQRLAQG-PIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIG 80
Cdd:PRK13354   1 MKMNILEQLKWRGAINQETDEEKLRKSLKEGkPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  81 DPSFKATERKLNTEDTVQEWVDKIRRQVAPFLDFDcgenSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQR 160
Cdd:PRK13354  81 DPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE----KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 161 LNRDdVGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTE 240
Cdd:PRK13354 157 LERE-QGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 241 GGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEDKNsGKAPR-AQYVLAEQVTRLVHGEEGLAA 319
Cdd:PRK13354 236 GGAIWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLET-EPNPRdAKKVLAEEITKFVHGEEAAEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 320 AKRITESLFNGNLNALSeadfeqlaqDGVPMIEMEKGADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFS 399
Cdd:PRK13354 315 AEKIFKALFSGDVKPLK---------DIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIIN 385

                        410       420
                 ....*....|....*....|....*
gi 490520624 400 DSDRLFGRYTLLRRGKKNYCLVCWK 424
Cdd:PRK13354 386 PEDAFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 4-402 1.33e-163

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: 464.95  E-value: 1.33e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624    4 SNLIKQLQERGLVAQVTDEEALAQRLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPS 83
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   84 FKATERKLNTEDTVQEWVDKIRRQVAPFLDFDcgenSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:TIGR00234  82 GKSEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  164 ddvGISFTEFSYNLLQGYDFACLNKlhgvALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGA 243
Cdd:TIGR00234 158 ---NISLHEFIYPLLQAYDFVYLNV----DLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  244 VWLDPkktSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEdkNSGKAPRAQYVLAEQVTRLVHGEEGLAAAKRI 323
Cdd:TIGR00234 231 VSLDE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEI 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  324 TESLFNGNLNalseadfeqlaQDGVPMIEMEKGA---DLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSD 400
Cdd:TIGR00234 306 SEAIFSGGLN-----------PDEVPIFRPEKFGgpiTLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKE 374


                  ..
gi 490520624  401 SD 402
Cdd:TIGR00234 375 LE 376
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 34-310 2.31e-132

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: 381.18  E-value: 2.31e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  34 IALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPSFKATERKLNTEDTVQEWVDKIRRQVAPFLD 113
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 114 FDcGENSAIAANNYDWFGNMNVLTFLRdIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQGYDFACLNklhgVA 193
Cdd:cd00805   81 FI-PPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEEE-GISFSEFIYPLLQAYDFVYLD----VD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 194 LQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGAVWlDPKKTSPYKFYQFWINTADADVYRFLK 273
Cdd:cd00805  154 LQLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490520624 274 FFTFMSIDEINALEEEDKNSGKAPRAQYVLAEQVTRL 310
Cdd:cd00805  233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
29-328 3.29e-106

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 315.76  E-value: 3.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   29 LAQGPIALYCGFDPTADsLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPSfKATERKLNTEDTVQEWVdkIRRQV 108
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  109 APFLDFDCgensAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQGYDFACLNK 188
Cdd:pfam00579  77 ACGLDPEK----AEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGP-GISLGEFTYPLLQAYDILLLKA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  189 lhgvALQIGGSDQWGNITSGIDLTRRLHQN---QVFGLTVPLITKSDGT-KFGKTEGG-AVWLDPKKTSPYKFYQFWINT 263
Cdd:pfam00579 152 ----DLQPGGSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTD 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490520624  264 ADADVYRFLKFFTFMSIDEINALEEEDKNSgKAPRAQYVLAEQVTRLVHGEEGLAAAKRITESLF 328
Cdd:pfam00579 228 PDREVRKDLKLFTFLSNEEIEILEAELGKS-PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
S4 smart00363
S4 RNA-binding domain;
363-416 9.34e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.36  E-value: 9.34e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 490520624   363 LVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSDSDRLFGRYTLLRRGKK 416
Cdd:smart00363   7 LARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 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: 667.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   4 SNLIKQLQERGLVAQVTDEEaLAQRLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPS 83
Cdd:COG0162    1 MNLLLELIWRGLIEQITDEE-LREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  84 FKATERKLNTEDTVQEWVDKIRRQVAPFLDFDCgeNSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:COG0162   80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDD--NKAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLES 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 164 DDvGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGA 243
Cdd:COG0162  158 GQ-GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 244 VWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLAAAKRI 323
Cdd:COG0162  237 IWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 324 TESLF-NGNLnalseadfeqlaQDGVPMIEMEK---GADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFS 399
Cdd:COG0162  317 FEALFgKGEL------------PDDLPEVELSAaegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLT 384

                        410       420
                 ....*....|....*....|....*
gi 490520624 400 DSDRLFGRYTLLRRGKKNYCLVCWK 424
Cdd:COG0162  385 AGDLLHGGYLVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 2-424 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 581.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   2 ASSNLIKQLQERGLVAQVTDEEALAQRLAQG-PIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIG 80
Cdd:PRK13354   1 MKMNILEQLKWRGAINQETDEEKLRKSLKEGkPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  81 DPSFKATERKLNTEDTVQEWVDKIRRQVAPFLDFDcgenSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQR 160
Cdd:PRK13354  81 DPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE----KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 161 LNRDdVGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTE 240
Cdd:PRK13354 157 LERE-QGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 241 GGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEDKNsGKAPR-AQYVLAEQVTRLVHGEEGLAA 319
Cdd:PRK13354 236 GGAIWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLET-EPNPRdAKKVLAEEITKFVHGEEAAEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 320 AKRITESLFNGNLNALSeadfeqlaqDGVPMIEMEKGADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFS 399
Cdd:PRK13354 315 AEKIFKALFSGDVKPLK---------DIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIIN 385

                        410       420
                 ....*....|....*....|....*
gi 490520624 400 DSDRLFGRYTLLRRGKKNYCLVCWK 424
Cdd:PRK13354 386 PEDAFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 4-402 1.33e-163

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: 464.95  E-value: 1.33e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624    4 SNLIKQLQERGLVAQVTDEEALAQRLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPS 83
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   84 FKATERKLNTEDTVQEWVDKIRRQVAPFLDFDcgenSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR 163
Cdd:TIGR00234  82 GKSEVRKILTREEVQENAENIKKQIARFLDFE----KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  164 ddvGISFTEFSYNLLQGYDFACLNKlhgvALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGA 243
Cdd:TIGR00234 158 ---NISLHEFIYPLLQAYDFVYLNV----DLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  244 VWLDPkktSPYKFYQFWINTADADVYRFLKFFTFMSIDEINALEEEdkNSGKAPRAQYVLAEQVTRLVHGEEGLAAAKRI 323
Cdd:TIGR00234 231 VSLDE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEI 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  324 TESLFNGNLNalseadfeqlaQDGVPMIEMEKGA---DLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSD 400
Cdd:TIGR00234 306 SEAIFSGGLN-----------PDEVPIFRPEKFGgpiTLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKE 374


                  ..
gi 490520624  401 SD 402
Cdd:TIGR00234 375 LE 376
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 34-310 2.31e-132

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: 381.18  E-value: 2.31e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  34 IALYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPSFKATERKLNTEDTVQEWVDKIRRQVAPFLD 113
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 114 FDcGENSAIAANNYDWFGNMNVLTFLRdIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQGYDFACLNklhgVA 193
Cdd:cd00805   81 FI-PPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEEE-GISFSEFIYPLLQAYDFVYLD----VD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 194 LQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKSDGTKFGKTEGGAVWlDPKKTSPYKFYQFWINTADADVYRFLK 273
Cdd:cd00805  154 LQLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490520624 274 FFTFMSIDEINALEEEDKNSGKAPRAQYVLAEQVTRL 310
Cdd:cd00805  233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 36-310 1.38e-108

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: 321.17  E-value: 1.38e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  36 LYCGFDPTADSLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPSFKATERKLNTEDTVQEWVDKIRRQVAPFLDFD 115
Cdd:cd00395    2 LYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 116 CGeNSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRddvGISFTEFSYNLLQGYDFACLNKLHGVALQ 195
Cdd:cd00395   82 DP-TQATLFNNSDWPGPLAHIQFLRDLGKHVYVNYMERKTSFQSRSEE---GISATEFTYPPLQAADFLLLNTTEGCDIQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 196 IGGSDQWGNITSGIDLTRRLH-QNQVFGLTVPLITKSDGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKF 274
Cdd:cd00395  158 PGGSDQWGNITLGRELARRFNgFTIAEGLTIPLVTKLDGPKFGKSESGPKWLDTEKTSPYEFYQFWINAVDSDVINILKY 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490520624 275 FTFMSIDEINALEEEdKNSGKAPR-AQYVLAEQVTRL 310
Cdd:cd00395  238 FTFLSKEEIERLEQE-QYEAPGYRvAQKTLAEEVTKT 273
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
29-328 3.29e-106

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 315.76  E-value: 3.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624   29 LAQGPIALYCGFDPTADsLHLGHLVPLLCLKRFQMAGHKPVALVGGATGLIGDPSfKATERKLNTEDTVQEWVdkIRRQV 108
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  109 APFLDFDCgensAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDvGISFTEFSYNLLQGYDFACLNK 188
Cdd:pfam00579  77 ACGLDPEK----AEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGP-GISLGEFTYPLLQAYDILLLKA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  189 lhgvALQIGGSDQWGNITSGIDLTRRLHQN---QVFGLTVPLITKSDGT-KFGKTEGG-AVWLDPKKTSPYKFYQFWINT 263
Cdd:pfam00579 152 ----DLQPGGSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTD 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490520624  264 ADADVYRFLKFFTFMSIDEINALEEEDKNSgKAPRAQYVLAEQVTRLVHGEEGLAAAKRITESLF 328
Cdd:pfam00579 228 PDREVRKDLKLFTFLSNEEIEILEAELGKS-PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 36-240 1.38e-10

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: 59.03  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624  36 LYCGFDPTAdSLHLGHLVPLLCLKRFQMA------GHKPVALVGGATGLIGDPSFKATErklNTEDTVQEWVDKIRRQVA 109
Cdd:cd00802    2 TFSGITPNG-YLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPANKKGE---NAKAFVERWIERIKEDVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520624 110 pfLDFDCgensaiaannydwfgnmnVLTFLRDIGKHFsvnqminkeavkqrlnrddvgisftefsynllqgydfaclnkl 189
Cdd:cd00802   78 --YMFLQ------------------AADFLLLYETEC------------------------------------------- 94

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490520624 190 hgvALQIGGSDQWGNITSGIDLTRRLH-QNQVFGLTVPLITKSDGTKFGKTE 240
Cdd:cd00802   95 ---DIHLGGSDQLGHIELGLELLKKAGgPARPFGLTFGRVMGADGTKMSKSK 143
S4 smart00363
S4 RNA-binding domain;
363-416 9.34e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.36  E-value: 9.34e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 490520624   363 LVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSDSDRLFGRYTLLRRGKK 416
Cdd:smart00363   7 LARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLKK 60
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 359-404 1.98e-05

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: 42.24  E-value: 1.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490520624 359 LMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSDSDRL 404
Cdd:cd00165    3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVI 48
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 359-404 1.91e-04

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: 39.01  E-value: 1.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 490520624  359 LMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYTFSDSDRL 404
Cdd:pfam01479   3 LDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPGDEI 48
PLN02486 PLN02486
aminoacyl-tRNA ligase
 33-64 5.81e-03

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 38.57  E-value: 5.81e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490520624  33 PIALYCGFDPTADSLHLGHLVPLLCLKRFQMA 64
Cdd:PLN02486  73 KFYLYTGRGPSSEALHLGHLIPFMFTKYLQDA 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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