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Conserved domains on  [gi|497575180|ref|WP_009889364|]
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tyrosine--tRNA ligase [Clostridioides difficile]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11486587)

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
EC:  6.1.1.1
Gene Ontology:  GO:0004831|GO:0006437
PubMed:  12458790|10447505
SCOP:  4003807

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-401 0e+00

tyrosyl-tRNA synthetase; Provisional


:

Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 568.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   1 MKSIDEQMRIimkgvDDLIDEKELREKLIKSEKEGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFT 80
Cdd:PRK13354   2 KMNILEQLKW-----RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  81 GKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLDKEKTIVRFNSEWLAKLNFEDVI-KLAATITVARMLEREDFKKR 159
Cdd:PRK13354  77 GKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 160 YEGQMPISVHEFFYPLMQAYDSIAL----EADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSL 235
Cdd:PRK13354 157 LEREQGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 236 GNYIGIDEE---AGIMYQKSMEIPDELIIKYYNLVTDVHPDEVNKIESQLKEGSvNPRDIKMNLAREIVTLYHGEESAKE 312
Cdd:PRK13354 236 GGAIWLDPEktsPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 313 AEERFKSVFQKGQIPE-DIQTIQVKEDGFDLIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESEL----- 386
Cdd:PRK13354 315 AEKIFKALFSGDVKPLkDIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAfdgkf 394

                        410
                 ....*....|....*.
gi 497575180 387 -VVQIGKKKFVKIELV 401
Cdd:PRK13354 395 vILRRGKKKFFLVKLK 410
 
Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-401 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 568.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   1 MKSIDEQMRIimkgvDDLIDEKELREKLIKSEKEGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFT 80
Cdd:PRK13354   2 KMNILEQLKW-----RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  81 GKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLDKEKTIVRFNSEWLAKLNFEDVI-KLAATITVARMLEREDFKKR 159
Cdd:PRK13354  77 GKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 160 YEGQMPISVHEFFYPLMQAYDSIAL----EADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSL 235
Cdd:PRK13354 157 LEREQGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 236 GNYIGIDEE---AGIMYQKSMEIPDELIIKYYNLVTDVHPDEVNKIESQLKEGSvNPRDIKMNLAREIVTLYHGEESAKE 312
Cdd:PRK13354 236 GGAIWLDPEktsPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 313 AEERFKSVFQKGQIPE-DIQTIQVKEDGFDLIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESEL----- 386
Cdd:PRK13354 315 AEKIFKALFSGDVKPLkDIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAfdgkf 394

                        410
                 ....*....|....*.
gi 497575180 387 -VVQIGKKKFVKIELV 401
Cdd:PRK13354 395 vILRRGKKKFFLVKLK 410
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 7-401 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: 563.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   7 QMRIIMKGVDDLIDEKELREKLiksekEGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDP 86
Cdd:COG0162    4 LLELIWRGLIEQITDEELREKL-----AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  87 TGKSKARKALTTEQVLANAKTYEEQIFKVLD--KEKTIVRFNSEWLAKLNFEDVI-KLAATITVARMLEREDFKKRYEGQ 163
Cdd:COG0162   79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDfdDNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 164 MPISVHEFFYPLMQAYDSIAL----EADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSLGNYI 239
Cdd:COG0162  159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGT-KMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 240 GIDEE---AGIMYQKSMEIPDELIIKYYNLVTDVHPDEVNKIESQLKEGSvNPRDIKMNLAREIVTLYHGEESAKEAEER 316
Cdd:COG0162  238 WLDEEktsPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 317 FKSVFQKGQIPEDIQTIQVK--EDGFDLIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESEL------VV 388
Cdd:COG0162  317 FEALFGKGELPDDLPEVELSaaEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLlhggylVL 396

                        410
                 ....*....|...
gi 497575180 389 QIGKKKFVKIELV 401
Cdd:COG0162  397 RVGKKKFALVKLK 409
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 21-385 5.34e-130

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: 378.66  E-value: 5.34e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   21 EKELREKLiksekeGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTGKSKARKALTTEQ 100
Cdd:TIGR00234  21 EKDLLKLL------ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTREE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  101 VLANAKTYEEQIFKVLDKEKTIVRFNSEWLAKLNFEDVIKLAATI-TVARMLEREDFKKRYegQMPISVHEFFYPLMQAY 179
Cdd:TIGR00234  95 VQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRF--EENISLHEFIYPLLQAY 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  180 DSIALEADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGkEKMSKSLGNYIGIDEEAGIMYQKSMEIPDEL 259
Cdd:TIGR00234 173 DFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEGKYDFYQKVINTPDEL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  260 IIKYYNLVTdvhPDEVNKIESQLKEGSVNPRDIKMNLAREIVTLYHGEESAKEAEERFKSVFQKGQIPEDIQTIQVKEDG 339
Cdd:TIGR00234 252 VKKYLKLFT---FLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDEVPIFRPEKFG 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 497575180  340 FD--LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESE 385
Cdd:TIGR00234 329 GPitLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKELE 376
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 40-303 9.12e-101

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: 300.29  E-value: 9.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  40 VKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLD-- 117
Cdd:cd00805    3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILDfi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 118 -KEKTIVRFNSEWLAKLNFEDVIKLAATITVARMLEREDFKKRYEGQMPISVHEFFYPLMQAYDSIALEADIELGGTDQR 196
Cdd:cd00805   83 pPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 197 FNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSLGNYIGID--EEAGIMYQKSMEIPDELIIKYYNLVTDVHPDE 274
Cdd:cd00805  163 GNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIWDPvlDSPYDVYQKIRNAFDPDVLEFLKLFTFLDYEE 241

                        250       260
                 ....*....|....*....|....*....
gi 497575180 275 VNKIESQLKEGsVNPRDIKMNLAREIVTL 303
Cdd:cd00805  242 IEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
33-322 1.84e-89

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 272.23  E-value: 1.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   33 KEGKPMIVKLGLDPSAPdIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTgKSKARKALTTEQVLANAktYEEQI 112
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  113 FKVLDKEKTIVRFNSEWLAKLNFEDVIKLAATI-TVARMLEREDFKKRYEGQMPISVHEFFYPLMQAYDSIALEADIELG 191
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  192 GTDQRFNLLMGRSLQREFGMES---QIVIMMPLIEGLDGKEKMSKSLGN-YIGIDEEAGI---MYQKSMEIPDELIIKYY 264
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKIfkkPVGLTNPLLTGLDGGKKMSKSAGNsAIFLDDDPESvykKIQKAYTDPDREVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 497575180  265 NLVTDVHPDEVNKIESQLKEGsvNPRDIKMNLAREIVTLYHGEESAKEAEERFKSVFQ 322
Cdd:pfam00579 237 KLFTFLSNEEIEILEAELGKS--PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
342-397 6.72e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 6.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 497575180   342 LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESELV-VQIGKKKFVK 397
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVIsVRGKELKRLK 59
 
Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-401 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 568.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   1 MKSIDEQMRIimkgvDDLIDEKELREKLIKSEKEGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFT 80
Cdd:PRK13354   2 KMNILEQLKW-----RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  81 GKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLDKEKTIVRFNSEWLAKLNFEDVI-KLAATITVARMLEREDFKKR 159
Cdd:PRK13354  77 GKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 160 YEGQMPISVHEFFYPLMQAYDSIAL----EADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSL 235
Cdd:PRK13354 157 LEREQGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 236 GNYIGIDEE---AGIMYQKSMEIPDELIIKYYNLVTDVHPDEVNKIESQLKEGSvNPRDIKMNLAREIVTLYHGEESAKE 312
Cdd:PRK13354 236 GGAIWLDPEktsPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 313 AEERFKSVFQKGQIPE-DIQTIQVKEDGFDLIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESEL----- 386
Cdd:PRK13354 315 AEKIFKALFSGDVKPLkDIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAfdgkf 394

                        410
                 ....*....|....*.
gi 497575180 387 -VVQIGKKKFVKIELV 401
Cdd:PRK13354 395 vILRRGKKKFFLVKLK 410
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 7-401 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: 563.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   7 QMRIIMKGVDDLIDEKELREKLiksekEGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDP 86
Cdd:COG0162    4 LLELIWRGLIEQITDEELREKL-----AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  87 TGKSKARKALTTEQVLANAKTYEEQIFKVLD--KEKTIVRFNSEWLAKLNFEDVI-KLAATITVARMLEREDFKKRYEGQ 163
Cdd:COG0162   79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDfdDNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 164 MPISVHEFFYPLMQAYDSIAL----EADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSLGNYI 239
Cdd:COG0162  159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGT-KMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 240 GIDEE---AGIMYQKSMEIPDELIIKYYNLVTDVHPDEVNKIESQLKEGSvNPRDIKMNLAREIVTLYHGEESAKEAEER 316
Cdd:COG0162  238 WLDEEktsPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 317 FKSVFQKGQIPEDIQTIQVK--EDGFDLIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESEL------VV 388
Cdd:COG0162  317 FEALFGKGELPDDLPEVELSaaEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLlhggylVL 396

                        410
                 ....*....|...
gi 497575180 389 QIGKKKFVKIELV 401
Cdd:COG0162  397 RVGKKKFALVKLK 409
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 21-385 5.34e-130

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: 378.66  E-value: 5.34e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   21 EKELREKLiksekeGKPMIVKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTGKSKARKALTTEQ 100
Cdd:TIGR00234  21 EKDLLKLL------ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTREE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  101 VLANAKTYEEQIFKVLDKEKTIVRFNSEWLAKLNFEDVIKLAATI-TVARMLEREDFKKRYegQMPISVHEFFYPLMQAY 179
Cdd:TIGR00234  95 VQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRF--EENISLHEFIYPLLQAY 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  180 DSIALEADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGkEKMSKSLGNYIGIDEEAGIMYQKSMEIPDEL 259
Cdd:TIGR00234 173 DFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEGKYDFYQKVINTPDEL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  260 IIKYYNLVTdvhPDEVNKIESQLKEGSVNPRDIKMNLAREIVTLYHGEESAKEAEERFKSVFQKGQIPEDIQTIQVKEDG 339
Cdd:TIGR00234 252 VKKYLKLFT---FLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDEVPIFRPEKFG 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 497575180  340 FD--LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESE 385
Cdd:TIGR00234 329 GPitLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRKELE 376
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 40-303 9.12e-101

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: 300.29  E-value: 9.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  40 VKLGLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLD-- 117
Cdd:cd00805    3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILDfi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 118 -KEKTIVRFNSEWLAKLNFEDVIKLAATITVARMLEREDFKKRYEGQMPISVHEFFYPLMQAYDSIALEADIELGGTDQR 196
Cdd:cd00805   83 pPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 197 FNLLMGRSLQREFGMESQIVIMMPLIEGLDGKeKMSKSLGNYIGID--EEAGIMYQKSMEIPDELIIKYYNLVTDVHPDE 274
Cdd:cd00805  163 GNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIWDPvlDSPYDVYQKIRNAFDPDVLEFLKLFTFLDYEE 241

                        250       260
                 ....*....|....*....|....*....
gi 497575180 275 VNKIESQLKEGsVNPRDIKMNLAREIVTL 303
Cdd:cd00805  242 IEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
33-322 1.84e-89

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 272.23  E-value: 1.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   33 KEGKPMIVKLGLDPSAPdIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTgKSKARKALTTEQVLANAktYEEQI 112
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  113 FKVLDKEKTIVRFNSEWLAKLNFEDVIKLAATI-TVARMLEREDFKKRYEGQMPISVHEFFYPLMQAYDSIALEADIELG 191
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  192 GTDQRFNLLMGRSLQREFGMES---QIVIMMPLIEGLDGKEKMSKSLGN-YIGIDEEAGI---MYQKSMEIPDELIIKYY 264
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKIfkkPVGLTNPLLTGLDGGKKMSKSAGNsAIFLDDDPESvykKIQKAYTDPDREVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 497575180  265 NLVTDVHPDEVNKIESQLKEGsvNPRDIKMNLAREIVTLYHGEESAKEAEERFKSVFQ 322
Cdd:pfam00579 237 KLFTFLSNEEIEILEAELGKS--PYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 43-303 2.74e-33

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: 125.49  E-value: 2.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  43 GLDPSAPDIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKIGDPTGKSKARKALTTEQVLANAKTYEEQIFKVLDKE--- 119
Cdd:cd00395    5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFEdpt 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 120 KTIVRFNSEWLAKLNFEDVIK-LAATITVARMLEREDFKKRYEgqMPISVHEFFYPLMQAYDSI----ALEADIELGGTD 194
Cdd:cd00395   85 QATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSRSE--EGISATEFTYPPLQAADFLllntTEGCDIQPGGSD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 195 QRFNLLMGRSLQREFGMESQ-IVIMMPLIEGLDGKeKMSKSLGNYIGIDEE---AGIMYQKSMEIPDELIIKYYNLVTDV 270
Cdd:cd00395  163 QWGNITLGRELARRFNGFTIaEGLTIPLVTKLDGP-KFGKSESGPKWLDTEktsPYEFYQFWINAVDSDVINILKYFTFL 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 497575180 271 HPDEVNKIESQLKEGSvNPRDIKMNLAREIVTL 303
Cdd:cd00395  242 SKEEIERLEQEQYEAP-GYRVAQKTLAEEVTKT 273
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 4-303 7.63e-28

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 111.88  E-value: 7.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   4 IDEQMRIIMKGVDDLIDEKELREKLikseKEGKPMIVKLGLDPSAPdIHLGHTVVLRKMKQLQDLGHQIVIIIGDFTGKI 83
Cdd:PRK08560   1 IEERLELITRNTEEVVTEEELRELL----ESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  84 GDptgKSkarkalTTEQVLANAKTYEEQIFKV-LDKEKTIVRFNSEWLAKLNF-EDVIKLAATITVARMLEREDFKKRYE 161
Cdd:PRK08560  76 ND---KG------DLEEIRKVAEYNKKVFEALgLDPDKTEFVLGSEFQLDKEYwLLVLKLAKNTTLARARRSMTIMGRRM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 162 GQMPISvhEFFYPLMQAYDSIALEADIELGGTDQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKE-KMSKS-LGNYI 239
Cdd:PRK08560 147 EEPDVS--KLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGiKMSKSkPGSAI 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 240 GIDEEAGIMYQK---------------SMEIPDELIIKYYNLVT---------DVHPDEVNKIESQLKEGSVNPRDIKMN 295
Cdd:PRK08560 225 FVHDSPEEIRRKikkaycppgevegnpVLEIAKYHIFPRYDPFVierpekyggDLEYESYEELERDYAEGKLHPMDLKNA 304


                 ....*...
gi 497575180 296 LAREIVTL 303
Cdd:PRK08560 305 VAEYLIEI 312
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 46-244 1.17e-08

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 56.02  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  46 PSAPdIHLGHTV-VLRKMKQLQDLGHQIvIIIGDftgkigdptgkskaRKALTTeqvlaNAKTYE---EQIFKV------ 115
Cdd:PRK12282  11 PTGK-LHLGHYVgSLKNRVALQNEHEQF-VLIAD--------------QQALTD-----NAKNPEkirRNILEValdyla 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 116 --LDKEKTIVRFNSEW--LAKL-----NFedviklaatITVARmLER------EDFKKRYEGQMPISvheFF-YPLMQAY 179
Cdd:PRK12282  70 vgIDPAKSTIFIQSQIpeLAELtmyymNL---------VTVAR-LERnptvktEIAQKGFGRSIPAG---FLtYPVSQAA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 180 DSIALEADIELGGTDQ------------RFNLLMGRslqrEFGMESQIVI-MMPLIEGLDGKEKMSKSLGN--YIGIDEE 244
Cdd:PRK12282 137 DITAFKATLVPVGDDQlpmieqtreivrRFNSLYGT----DVLVEPEALLpEAGRLPGLDGKAKMSKSLGNaiYLSDDAD 212
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 171-370 6.04e-08

Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 53.90  E-value: 6.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 171 FFYPLMQAYDSIALEADIELGGTDQ------------RFNLLMGrslqrEFGMESQIVI--MMPLIEGLDGKEKMSKSLG 236
Cdd:COG0180  127 LTYPVLMAADILLYKADLVPVGEDQkqhleltrdiarRFNHRYG-----EVFPEPEALIpeEGARIPGLDGRKKMSKSYG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 237 NYIGIDEEAGIMYQKSMEIpdeliikyynlVTD---VHPDEVNKIEsqlkegsVNPrdikmnlareIVTLY---HGEESA 310
Cdd:COG0180  202 NTINLLDDPKEIRKKIKSA-----------VTDserLRYDDPGKPE-------VCN----------LFTIYsafSGKEEV 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497575180 311 KEAEERFKSvfqkgqipEDIQTIQVKEdgfDLIEVLVS---------NEIVKSKSEVRRLASQGGVKVN 370
Cdd:COG0180  254 EELEAEYRA--------GGIGYGDLKK---ALAEAVVEflapirerrAELLADPAELDEILAEGAEKAR 311
S4 smart00363
S4 RNA-binding domain;
342-397 6.72e-08

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 6.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 497575180   342 LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESELV-VQIGKKKFVK 397
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVIsVRGKELKRLK 59
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 342-402 1.37e-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: 48.40  E-value: 1.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497575180 342 LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESElVVQIGKKKFVKIELVK 402
Cdd:cd00165    3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGD-VIEVDGKSIEEDIVYE 62
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 342-387 7.33e-07

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: 45.56  E-value: 7.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 497575180  342 LIEVLVSNEIVKSKSEVRRLASQGGVKVNGEKVEDLSTIVKESELV 387
Cdd:pfam01479   3 LDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPGDEI 48
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 138-300 1.76e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 49.69  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 138 VIKLAATITVARMLEREDFKKRYEG-QMPISvhEFFYPLMQAYDSIALEADIELGGTDQR-FNLlmgrsLQREFGMESQI 215
Cdd:PTZ00126 164 VMDIARSFNITRIKRCSQIMGRSEGdEQPCA--QILYPCMQCADIFYLKADICQLGMDQRkVNM-----LAREYCDKKKI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 216 ----VI----MMPlieGL-DGKEKMSKSlgnyigiDEEAGIMYQKS-----------------------MEIPDELIIKY 263
Cdd:PTZ00126 237 kkkpIIlshhMLP---GLlEGQEKMSKS-------DPNSAIFMEDSeedvnrkikkaycppgviegnpiLAYFKSIVFPA 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 497575180 264 YNLVTdVHPDEVN----------KIESQLKEGSVNPRDIKMNLAREI 300
Cdd:PTZ00126 307 FNSFT-VLRKEKNggdvtyttyeELEKDYLSGALHPGDLKPALAKYL 352
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 3-234 2.10e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 40.27  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180   3 SIDEQMRIIMKGVDDLIDEKELREKLiksekEGKPMI-VKLGLDPSApDIHLGHTVVLR-KMKQLQDLGHQIVIIIGDFT 80
Cdd:PTZ00348   2 NTDERYKLLRSVGEECIQESELRNLI-----EKKPLIrCYDGFEPSG-RMHIAQGIFKAvNVNKCTQAGCEFVFWVADWF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  81 GKIGDPTGKSKARKALTTEqvlanaktYEEQIFKV--LDKEKTIVRFNSEWL---AKLNFEDVIKLAATITVARMLERED 155
Cdd:PTZ00348  76 ALMNDKVGGELEKIRIVGR--------YLIEVWKAagMDMDKVLFLWSSEEItnhANTYWRTVLDIGRQNTIARIKKCCT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 156 FKKRYEGQMpiSVHEFFYPLMQAYDSIALEADIELGGTDQRFNLLMGRSLQREFGMESQIVIMM-PLIEGL-DGKEKMSK 233
Cdd:PTZ00348 148 IMGKTEGTL--TAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKLKPVILShHMLAGLkQGQAKMSK 225


                 .
gi 497575180 234 S 234
Cdd:PTZ00348 226 S 226
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 43-235 5.03e-03

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: 37.07  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  43 GLDPSAPdIHLGHTVVLRKMKQLQDL------GHQIVIIIGDFTGKIGDPtgkskarkaltteqvlANAKTyeeqifkvl 116
Cdd:cd00802    5 GITPNGY-LHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDP----------------ANKKG--------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 117 dkeKTIVRFNSEWLAKlnfedviklaatitvarmleredFKKRYEgqmpisvheffYPLMQAYDSIAL---EADIELGGT 193
Cdd:cd00802   59 ---ENAKAFVERWIER-----------------------IKEDVE-----------YMFLQAADFLLLyetECDIHLGGS 101

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 497575180 194 DQRFNLLMGRSLQREFGMESQIVIMMPLIEGLDGKEKMSKSL 235
Cdd:cd00802  102 DQLGHIELGLELLKKAGGPARPFGLTFGRVMGADGTKMSKSK 143
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 43-365 6.07e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 38.53  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180  43 GLDPSApDIHLGHTV-VLRKMKQLQDlGHQIVIIIGDFtgkigdptgkskarKALTTEQvlaNAKTYEEQIFKV------ 115
Cdd:PRK00927   7 GIQPTG-KLHLGNYLgAIKNWVELQD-EYECFFCIADL--------------HALTVPQ---DPEELRENTRELaadyla 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 116 --LDKEKTIVRFNSE--------WLakLNfedviklaatiTVARM--LER-EDFK-KRYEGQMPISVHEFFYPLMQAyds 181
Cdd:PRK00927  68 cgIDPEKSTIFVQSHvpehaelaWI--LN-----------CITPLgeLERmTQFKdKSAKQKENVSAGLFTYPVLMA--- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 182 ialeADIELGGTD-------------------QRFNLLMGrslqrEFGMESQIVI--MMPLIEGLDGKE-KMSKSLG--- 236
Cdd:PRK00927 132 ----ADILLYKADlvpvgedqkqhleltrdiaRRFNNLYG-----EVFPVPEPLIpkVGARVMGLDGPTkKMSKSDPndn 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 237 NYIGIDEEAGIMYQKSMEIpdeliikyynlVTDvhPDEVNKIESQLKEgsvNPrDIKmNLareiVTLYHG--EESAKEAE 314
Cdd:PRK00927 203 NTINLLDDPKTIAKKIKKA-----------VTD--SERLREIRYDLPN---KP-EVS-NL----LTIYSAlsGESIEELE 260

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575180 315 ERFKSvfqkgqipEDIQTIQVKEdgfDLIEVLVS---------NEIVKSKSEVRRLASQG 365
Cdd:PRK00927 261 AEYEA--------GGKGYGDFKK---DLAEAVVEflapireryEELLADPAYLDEILAEG 309
 
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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