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Conserved domains on  [gi|524688481|emb|CDD93815|]
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tyrosyl-tRNA synthetase [Akkermansia sp. CAG:344]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11415010)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
3-383 3.35e-154

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: 440.62  E-value: 3.35e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   3 GTAVVISREELKERLKlGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLS 82
Cdd:COG0162   11 GLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  83 REQVLENAETYTKQAFKILDRD--RTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYP 159
Cdd:COG0162   90 EEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 160 IMQGWDSVEI----RSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVDE---APEM 232
Cdd:COG0162  170 LLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEektSPYE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 233 MFGKMMSASDELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLaA 302
Cdd:COG0162  249 FYQKWMNISDADVWRYLKLFtflpleeieeLEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGEL-P 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 303 ADLPEVEIASLPAGMNAL-ALVAFLFEnvfqvkKSNGVLRKeHFTPGAIQLNDAKVTDPAAVPELAPGS-----VLRLSK 376
Cdd:COG0162  328 DDLPEVELSAAEGGIPLVdLLVEAGLA------ASKSEARR-LIKQGGVSVNGEKVTDPDAVLTAGDLLhggylVLRVGK 400

                 ....*..
gi 524688481 377 KHAVRFK 383
Cdd:COG0162  401 KKFALVK 407
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
3-383 3.35e-154

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: 440.62  E-value: 3.35e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   3 GTAVVISREELKERLKlGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLS 82
Cdd:COG0162   11 GLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  83 REQVLENAETYTKQAFKILDRD--RTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYP 159
Cdd:COG0162   90 EEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 160 IMQGWDSVEI----RSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVDE---APEM 232
Cdd:COG0162  170 LLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEektSPYE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 233 MFGKMMSASDELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLaA 302
Cdd:COG0162  249 FYQKWMNISDADVWRYLKLFtflpleeieeLEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGEL-P 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 303 ADLPEVEIASLPAGMNAL-ALVAFLFEnvfqvkKSNGVLRKeHFTPGAIQLNDAKVTDPAAVPELAPGS-----VLRLSK 376
Cdd:COG0162  328 DDLPEVELSAAEGGIPLVdLLVEAGLA------ASKSEARR-LIKQGGVSVNGEKVTDPDAVLTAGDLLhggylVLRVGK 400

                 ....*..
gi 524688481 377 KHAVRFK 383
Cdd:COG0162  401 KKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
10-383 3.25e-130

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 379.63  E-value: 3.25e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  10 REELKERLKLGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLEN 89
Cdd:PRK13354  21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  90 AETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVE 168
Cdd:PRK13354 101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 169 IR----SDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEA---PEMMFGKMMSAS 241
Cdd:PRK13354 181 LNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 242 DELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAAADLPEVEIA 311
Cdd:PRK13354 260 DRDVVKYLKLFtdlspdeideLEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFEVS 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688481 312 SlpagmNALALVAFLFENVFQvkKSNGVLRkEHFTPGAIQLNDAKVTDPAAVPELAP-----GSVLRLSKKHAVRFK 383
Cdd:PRK13354 340 A-----ETKNLVDLLVDLGLE--PSKREAR-RLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLVK 408
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
6-360 4.38e-103

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: 309.33  E-value: 4.38e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481    6 VVISREELKERLK-LGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSRE 84
Cdd:TIGR00234  14 EVQTPEEEKDLLKlLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTRE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   85 QVLENAETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVLKLNSR-VTMQQMLAREDFKARVEggKEVRLHEMQYPIMQG 163
Cdd:TIGR00234  94 EVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFE--ENISLHEFIYPLLQA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  164 WDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEAPEMMFGKMMSASDE 243
Cdd:TIGR00234 172 YDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE-KMGKSLGGAVSLDEGKYDFYQKVINTPDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  244 LMDRYYQVL----LGEKRDM----GLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAaadlPEVEIASLPA 315
Cdd:TIGR00234 251 LVKKYLKLFtflgLEEIEQLvelkGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP----DEVPIFRPEK 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 524688481  316 GMNALALVAFLFENVFQVKKSNGvlrKEHFTPGAIQLNDAKVTDP 360
Cdd:TIGR00234 327 FGGPITLADLLVLSGLFPSKSEA---RRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
23-277 5.02e-91

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: 274.48  E-value: 5.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  23 LRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILD 102
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RD---RTEIVYNGDWFRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTD 179
Cdd:cd00805   81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYV--GVDEAPEMMFGKMMSASDELMDRYYQVLL---- 253
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTfldy 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 524688481 254 -------GEKRDmGLHPMEAKKLLAWKITAR 277
Cdd:cd00805  240 eeieeleEEHAE-GPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
18-279 1.05e-75

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 236.02  E-value: 1.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   18 KLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgRSVTRPPLSREQVLENAetYTKQA 97
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   98 FKILDRDRTEIVYNGDWFRKMTYEEVLKLNSRV-TMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELG 176
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  177 GTDQLFNILVGRDLQK---EEGMLPQIAMTMPLLEGLDGVRKMSKSYGN----YVGVDEAPEMMFGKMMSASDELMDRYY 249
Cdd:pfam00579 157 GSDQWGNIELGRDLARrfnKKIFKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 524688481  250 QVLLGE-----KRDMGLH----PMEAKKLLAWKITARYH 279
Cdd:pfam00579 237 KLFTFLsneeiEILEAELgkspYREAEELLAREVTGLVH 275
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
3-383 3.35e-154

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: 440.62  E-value: 3.35e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   3 GTAVVISREELKERLKlGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLS 82
Cdd:COG0162   11 GLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  83 REQVLENAETYTKQAFKILDRD--RTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYP 159
Cdd:COG0162   90 EEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 160 IMQGWDSVEI----RSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVDE---APEM 232
Cdd:COG0162  170 LLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEektSPYE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 233 MFGKMMSASDELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLaA 302
Cdd:COG0162  249 FYQKWMNISDADVWRYLKLFtflpleeieeLEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGEL-P 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 303 ADLPEVEIASLPAGMNAL-ALVAFLFEnvfqvkKSNGVLRKeHFTPGAIQLNDAKVTDPAAVPELAPGS-----VLRLSK 376
Cdd:COG0162  328 DDLPEVELSAAEGGIPLVdLLVEAGLA------ASKSEARR-LIKQGGVSVNGEKVTDPDAVLTAGDLLhggylVLRVGK 400

                 ....*..
gi 524688481 377 KHAVRFK 383
Cdd:COG0162  401 KKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
10-383 3.25e-130

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 379.63  E-value: 3.25e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  10 REELKERLKLGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLEN 89
Cdd:PRK13354  21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  90 AETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVE 168
Cdd:PRK13354 101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 169 IR----SDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEA---PEMMFGKMMSAS 241
Cdd:PRK13354 181 LNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 242 DELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAAADLPEVEIA 311
Cdd:PRK13354 260 DRDVVKYLKLFtdlspdeideLEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFEVS 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688481 312 SlpagmNALALVAFLFENVFQvkKSNGVLRkEHFTPGAIQLNDAKVTDPAAVPELAP-----GSVLRLSKKHAVRFK 383
Cdd:PRK13354 340 A-----ETKNLVDLLVDLGLE--PSKREAR-RLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLVK 408
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
6-360 4.38e-103

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: 309.33  E-value: 4.38e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481    6 VVISREELKERLK-LGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSRE 84
Cdd:TIGR00234  14 EVQTPEEEKDLLKlLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTRE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   85 QVLENAETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVLKLNSR-VTMQQMLAREDFKARVEggKEVRLHEMQYPIMQG 163
Cdd:TIGR00234  94 EVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFE--ENISLHEFIYPLLQA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  164 WDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEAPEMMFGKMMSASDE 243
Cdd:TIGR00234 172 YDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE-KMGKSLGGAVSLDEGKYDFYQKVINTPDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  244 LMDRYYQVL----LGEKRDM----GLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAaadlPEVEIASLPA 315
Cdd:TIGR00234 251 LVKKYLKLFtflgLEEIEQLvelkGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP----DEVPIFRPEK 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 524688481  316 GMNALALVAFLFENVFQVKKSNGvlrKEHFTPGAIQLNDAKVTDP 360
Cdd:TIGR00234 327 FGGPITLADLLVLSGLFPSKSEA---RRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
23-277 5.02e-91

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: 274.48  E-value: 5.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  23 LRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILD 102
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RD---RTEIVYNGDWFRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTD 179
Cdd:cd00805   81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYV--GVDEAPEMMFGKMMSASDELMDRYYQVLL---- 253
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTfldy 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 524688481 254 -------GEKRDmGLHPMEAKKLLAWKITAR 277
Cdd:cd00805  240 eeieeleEEHAE-GPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
18-279 1.05e-75

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 236.02  E-value: 1.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   18 KLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgRSVTRPPLSREQVLENAetYTKQA 97
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   98 FKILDRDRTEIVYNGDWFRKMTYEEVLKLNSRV-TMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELG 176
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  177 GTDQLFNILVGRDLQK---EEGMLPQIAMTMPLLEGLDGVRKMSKSYGN----YVGVDEAPEMMFGKMMSASDELMDRYY 249
Cdd:pfam00579 157 GSDQWGNIELGRDLARrfnKKIFKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 524688481  250 QVLLGE-----KRDMGLH----PMEAKKLLAWKITARYH 279
Cdd:pfam00579 237 KLFTFLsneeiEILEAELgkspYREAEELLAREVTGLVH 275
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
28-275 1.55e-31

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: 120.49  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  28 GVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILDRD--- 104
Cdd:cd00395    5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFEdpt 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 105 RTEIVYNGDWFRKMTYEEVLK-LNSRVTMQQMLAREDFKARVEGGkeVRLHEMQYPIMQGWD----SVEIRSDVELGGTD 179
Cdd:cd00395   85 QATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPGGSD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDL-QKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVD---EAPEMMFGKMMSASDELMDRYYQVL--- 252
Cdd:cd00395  163 QWGNITLGRELaRRFNGFTIAEGLTIPLVTKLDG-PKFGKSESGPKWLDtekTSPYEFYQFWINAVDSDVINILKYFtfl 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 524688481 253 -------LGEKRDMGLHPMEAKKLLAWKIT 275
Cdd:cd00395  242 skeeierLEQEQYEAPGYRVAQKTLAEEVT 271
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
4-240 1.17e-27

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 111.11  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   4 TAVVISREELKERLKLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgrsvtrpplSR 83
Cdd:PRK08560  12 TEEVVTEEELRELLESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLNDKG---------DL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  84 EQVLENAEtYTKQAFKI--LDRDRTEIVYNGDWFRKMTY-EEVLKLNSRVTMQQM------LAREDfkarveggKEVRLH 154
Cdd:PRK08560  82 EEIRKVAE-YNKKVFEAlgLDPDKTEFVLGSEFQLDKEYwLLVLKLAKNTTLARArrsmtiMGRRM--------EEPDVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 155 EMQYPIMQGWDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGV-RKMSKS-YGNYVGVDEAPEM 232
Cdd:PRK08560 153 KLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgIKMSKSkPGSAIFVHDSPEE 232

                 ....*...
gi 524688481 233 MFGKMMSA 240
Cdd:PRK08560 233 IRRKIKKA 240
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
28-240 5.73e-13

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS 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 formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 68.38  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  28 GVDPTAPdIHLGHTV-AIEKLRQFQELGHQAILLIGD---FTATIGDPSGRsvtrpplsREQVLENAETYtkqafkI--- 100
Cdd:cd00806    5 GIQPSGS-LHLGHYLgAFRFWVWLQEAGYELFFFIADlhaLTVKQLDPEEL--------RQNTRENAKDY------Lacg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 101 LDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTDQ 180
Cdd:cd00806   70 LDPEKSTIFFQSD--VPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688481 181 L------------FNILVGRDLQKEEGMLPQIAMTMPLLeglDGVRKMSKSYG-NYVGVDEAPEMMFGKMMSA 240
Cdd:cd00806  148 DphleltrdiarrFNKLYGEIFPKPAALLSKGAFLPGLQ---GPSKKMSKSDPnNAIFLTDSPKEIKKKIMKA 217
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
28-222 3.77e-10

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 60.51  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  28 GVDPTApDIHLGHTV-AIE-KLRQFQELGHQAILLIGDFTA--TIGDPSG-RSVTRpplsreqvlENAETYTKQAfkiLD 102
Cdd:PRK12556   9 GIKPTG-YPHLGNYIgAIKpALQMAKNYEGKALYFIADYHAlnAVHDPEQfRSYTR---------EVAATWLSLG---LD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RDRTeIVYngdwfRKMTYEEVLKLN---SRVTMQQMLAR-EDFKARVEGGKE--------VRLHEMQYPIMQGWDSVEIR 170
Cdd:PRK12556  76 PEDV-IFY-----RQSDVPEIFELAwilSCLTPKGLMNRaHAYKAKVDQNKEagldldagVNMGLYTYPILMAADILLFQ 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688481 171 SDVELGGTDQL------------FNILVGRDLQKEEGMLPQIAMTMPlleGLDGvRKMSKSYGN 222
Cdd:PRK12556 150 ATHVPVGKDQIqhieiardiatyFNHTFGDTFTLPEYVIQEEGAILP---GLDG-RKMSKSYGN 209
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
22-240 8.18e-07

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 50.41  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   22 PLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGD---FTATIGDPSGRsvtrpplsREQVLENAETYTKQAF 98
Cdd:TIGR00233   2 KFRVLTGIQPSGK-MHLGHYLGAIQTKWLQQFGVELFICIADlhaITVKQTDPDAL--------RKAREELAADYLAVGL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481   99 kilDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGgKEVRLHEMQYPIMQGWDSVEIRSDVELGGT 178
Cdd:TIGR00233  73 ---DPEKTFIFLQSD--YPEHYELAWLLSCQVTFGELKRMTQFKDKSQA-ENVPIGLLSYPVLQAADILLYQADLVPVGI 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688481  179 DQ------------LFNILVGRDLQKEEGMLPQiamTMPLLEGLDGvRKMSKSYGN-YVGVDEAPEMMFGKMMSA 240
Cdd:TIGR00233 147 DQdqhleltrdlaeRFNKKFKNFFPKPESLISK---FFPRLMGLSG-KKMSKSDPNsAIFLTDTPKQIKKKIRKA 217
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
182-240 2.17e-06

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: 48.89  E-value: 2.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 524688481 182 FNILVGRDLQKEEGMLPQIAMTMPlleGLDGVRKMSKSYGNYVGVDEAPEMMFGKMMSA 240
Cdd:COG0180  165 FNHRYGEVFPEPEALIPEEGARIP---GLDGRKKMSKSYGNTINLLDDPKEIRKKIKSA 220
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
158-240 6.53e-05

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 44.46  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 158 YPIMQGWDSVEIRSDVELGGTDQL------------FNILVGRDLQKE-EGMLPQiamtMPLLEGLDGVRKMSKSYGNYV 224
Cdd:PRK12282 130 YPVSQAADITAFKATLVPVGDDQLpmieqtreivrrFNSLYGTDVLVEpEALLPE----AGRLPGLDGKAKMSKSLGNAI 205
                         90
                 ....*....|....*.
gi 524688481 225 GVDEAPEMMFGKMMSA 240
Cdd:PRK12282 206 YLSDDADTIKKKVMSM 221
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
198-231 4.49e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 41.86  E-value: 4.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 524688481 198 PQIAMT----MPlleGLDGvRKMSKSYGNYVGVDEAPE 231
Cdd:PRK12283 247 PQALLTeaskMP---GLDG-QKMSKSYGNTIGLREDPE 280
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
15-240 1.18e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 40.62  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  15 ERLKLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTAtigdpsgRSVTRppLSREQVLENAETYT 94
Cdd:PRK12285  59 EAYRNGKPFAVYTGFMPSGP-MHIGHKMVFDELKWHQEFGANVYIPIADDEA-------YAARG--LSWEETREWAYEYI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481  95 KQAFKI-LDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKevrlheMQYPIMQGWD------SV 167
Cdd:PRK12285 129 LDLIALgFDPDKTEIYFQSE--NIKVYDLAFELAKKVNFSELKAIYGFTGETNIGH------IFYPATQAADilhpqlEE 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688481 168 EIRSDVELGGTDQLFNILVGRD----LQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGN-YVGVDEAPEMMFGKMMSA 240
Cdd:PRK12285 201 GPKPTLVPVGIDQDPHIRLTRDiaerLHGGYGFIKPSSTYHKFMPGLTG-GKMSSSKPEsAIYLTDDPETVKKKIMKA 277
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
180-222 5.47e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 38.45  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 524688481 180 QLFNILVGRDLQkeegMLP--QIAMTMPLLEGLDGvRKMSKSYGN 222
Cdd:PRK12284 170 QRFNHLYGGEFF----VLPeaVIEESVATLPGLDG-RKMSKSYDN 209
 
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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