NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1859508457|ref|WP_175187434|]
View 

tyrosine--tRNA ligase [Prosthecochloris ethylica]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 9-402 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: 519.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   9 QLDLITRNTVEVISEEELKKKLEkssltGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDP 88
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  89 SGKSKTRPQLSAEEARRNGETYFEQASKILDPS--RTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAR 165
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 166 EPISLHEFLYPLAQGMDSVHL----KNDIELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAI 241
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 242 SFSD---TPQDMYGRTLSIPDDLIETYFRLLVPHPetpahlfMEIIRQ---------NPREAKRTLAREIVSLYHSRTEA 309
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLP-------LEEIEEleaevaegpNPREAKKRLAEEITALVHGEEAA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 310 VKAEEHFDRVFVQKKAPEDIPEFSFDSP--SMPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLGKEAR 387
Cdd:COG0162   311 EAAEEAFEALFGKGELPDDLPEVELSAAegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLLH 390

                         410
                  ....*....|....*....
gi 1859508457 388 ----IIKSGKRKFFKVTRK 402
Cdd:COG0162   391 ggylVLRVGKKKFALVKLK 409
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 9-402 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: 519.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   9 QLDLITRNTVEVISEEELKKKLEkssltGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDP 88
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  89 SGKSKTRPQLSAEEARRNGETYFEQASKILDPS--RTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAR 165
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 166 EPISLHEFLYPLAQGMDSVHL----KNDIELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAI 241
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 242 SFSD---TPQDMYGRTLSIPDDLIETYFRLLVPHPetpahlfMEIIRQ---------NPREAKRTLAREIVSLYHSRTEA 309
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLP-------LEEIEEleaevaegpNPREAKKRLAEEITALVHGEEAA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 310 VKAEEHFDRVFVQKKAPEDIPEFSFDSP--SMPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLGKEAR 387
Cdd:COG0162   311 EAAEEAFEALFGKGELPDDLPEVELSAAegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLLH 390

                         410
                  ....*....|....*....
gi 1859508457 388 ----IIKSGKRKFFKVTRK 402
Cdd:COG0162   391 ggylVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 36-402 8.64e-153

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 437.80  E-value: 8.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  36 TGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSGKSKTRPQLSAEEARRNGETYFEQAS 115
Cdd:PRK13354   30 EGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 116 KILDPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKN----DI 190
Cdd:PRK13354  110 KLFDFEKTEIVNNSDWLSKLNLIDFLRdYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVHLNRkedvDL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 191 ELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAISFSD---TPQDMYGRTLSIPDDLIETYFR 267
Cdd:PRK13354  190 QIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADG-TKMGKSAGGAIWLDPektSPYEFYQFWMNIDDRDVVKYLK 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 268 LLVP-HPEtpahlfmEIIR--------QNPREAKRTLAREIVSLYHSRTEAVKAEEHFDRVFVQKKAPE-DIPEFSFDSP 337
Cdd:PRK13354  269 LFTDlSPD-------EIDEleaqletePNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLkDIPTFEVSAE 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859508457 338 SMPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVT----LGKEARIIKSGKRKFFKVTRK 402
Cdd:PRK13354  342 TKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINpedaFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 8-379 4.77e-132

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: 384.06  E-value: 4.77e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   8 EQLDLITRNTVEVISEEELKKKLEKSsltGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGD 87
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKLL---ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  88 PSGKSKTRPQLSAEEARRNGETYFEQASKILDPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQarE 166
Cdd:TIGR00234  80 PTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRlLGKIFTVNRMLRRDAFSSRFE--E 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 167 PISLHEFLYPLAQGMDSVHLKNDIELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAISFSDT 246
Cdd:TIGR00234 158 NISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 247 PQDMYGRTLSIPDDLIETYFRLLVPHPETPAHLFMEIIRQNPREAKRTLAREIVSLYHSRTEAVKAEEHFDRVFVQKKAP 326
Cdd:TIGR00234 237 KYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1859508457 327 EDIPEFSFDSPSMP--LVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHE 379
Cdd:TIGR00234 317 DEVPIFRPEKFGGPitLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPI 371
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 40-302 3.68e-105

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: 311.46  E-value: 3.68e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  40 LKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSGKSKTRPQLSAEEARRNGETYFEQASKILD 119
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 120 ---PSRTTICYNSEWLGSMNFSDVIRLSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKNDIELGGTD 196
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 197 QKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAI--SFSDTPQDMYGRTLSIPDDLIETYFRLLVPHPE 274
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1859508457 275 TPAHLFME--IIRQNPREAKRTLAREIVSL 302
Cdd:cd00805   240 EEIEELEEehAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
39-320 1.30e-84

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 259.52  E-value: 1.30e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  39 PLKVKLGADPSRPdLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSgKSKTRPQLSAEEARRNgeTYFEQASKIL 118
Cdd:pfam00579   5 PLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQLACGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 119 DPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKNDIELGGTDQ 197
Cdd:pfam00579  81 DPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 198 KFNLLVGRDLQREY---DIDPQVCITMPLLVGTFGEEKMSKSLGN-AISFSD---TPQDMYGRTLSIPDDLIETYFRLLV 270
Cdd:pfam00579 161 WGNIELGRDLARRFnkkIFKKPVGLTNPLLTGLDGGKKMSKSAGNsAIFLDDdpeSVYKKIQKAYTDPDREVRKDLKLFT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1859508457 271 PHPETPAHLFMEIIRQNP-REAKRTLAREIVSLYHSRTEAVKAEEHFDRVF 320
Cdd:pfam00579 241 FLSNEEIEILEAELGKSPyREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
S4 smart00363
S4 RNA-binding domain;
344-383 4.11e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 4.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1859508457  344 LLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLG 383
Cdd:smart00363   6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPG 45
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 9-402 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: 519.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   9 QLDLITRNTVEVISEEELKKKLEkssltGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDP 88
Cdd:COG0162     4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  89 SGKSKTRPQLSAEEARRNGETYFEQASKILDPS--RTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAR 165
Cdd:COG0162    79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 166 EPISLHEFLYPLAQGMDSVHL----KNDIELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAI 241
Cdd:COG0162   159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 242 SFSD---TPQDMYGRTLSIPDDLIETYFRLLVPHPetpahlfMEIIRQ---------NPREAKRTLAREIVSLYHSRTEA 309
Cdd:COG0162   238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLP-------LEEIEEleaevaegpNPREAKKRLAEEITALVHGEEAA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 310 VKAEEHFDRVFVQKKAPEDIPEFSFDSP--SMPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLGKEAR 387
Cdd:COG0162   311 EAAEEAFEALFGKGELPDDLPEVELSAAegGIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLLH 390

                         410
                  ....*....|....*....
gi 1859508457 388 ----IIKSGKRKFFKVTRK 402
Cdd:COG0162   391 ggylVLRVGKKKFALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 36-402 8.64e-153

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 437.80  E-value: 8.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  36 TGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSGKSKTRPQLSAEEARRNGETYFEQAS 115
Cdd:PRK13354   30 EGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 116 KILDPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKN----DI 190
Cdd:PRK13354  110 KLFDFEKTEIVNNSDWLSKLNLIDFLRdYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVHLNRkedvDL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 191 ELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAISFSD---TPQDMYGRTLSIPDDLIETYFR 267
Cdd:PRK13354  190 QIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADG-TKMGKSAGGAIWLDPektSPYEFYQFWMNIDDRDVVKYLK 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 268 LLVP-HPEtpahlfmEIIR--------QNPREAKRTLAREIVSLYHSRTEAVKAEEHFDRVFVQKKAPE-DIPEFSFDSP 337
Cdd:PRK13354  269 LFTDlSPD-------EIDEleaqletePNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLkDIPTFEVSAE 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859508457 338 SMPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVT----LGKEARIIKSGKRKFFKVTRK 402
Cdd:PRK13354  342 TKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINpedaFDGKFVILRRGKKKFFLVKLK 410
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 8-379 4.77e-132

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: 384.06  E-value: 4.77e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   8 EQLDLITRNTVEVISEEELKKKLEKSsltGQPLKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGD 87
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKLL---ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  88 PSGKSKTRPQLSAEEARRNGETYFEQASKILDPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQarE 166
Cdd:TIGR00234  80 PTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRlLGKIFTVNRMLRRDAFSSRFE--E 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 167 PISLHEFLYPLAQGMDSVHLKNDIELGGTDQKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAISFSDT 246
Cdd:TIGR00234 158 NISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDEG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 247 PQDMYGRTLSIPDDLIETYFRLLVPHPETPAHLFMEIIRQNPREAKRTLAREIVSLYHSRTEAVKAEEHFDRVFVQKKAP 326
Cdd:TIGR00234 237 KYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1859508457 327 EDIPEFSFDSPSMP--LVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHE 379
Cdd:TIGR00234 317 DEVPIFRPEKFGGPitLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPI 371
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 40-302 3.68e-105

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: 311.46  E-value: 3.68e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  40 LKVKLGADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSGKSKTRPQLSAEEARRNGETYFEQASKILD 119
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 120 ---PSRTTICYNSEWLGSMNFSDVIRLSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKNDIELGGTD 196
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 197 QKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGeEKMSKSLGNAI--SFSDTPQDMYGRTLSIPDDLIETYFRLLVPHPE 274
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1859508457 275 TPAHLFME--IIRQNPREAKRTLAREIVSL 302
Cdd:cd00805   240 EEIEELEEehAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
39-320 1.30e-84

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 259.52  E-value: 1.30e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  39 PLKVKLGADPSRPdLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSgKSKTRPQLSAEEARRNgeTYFEQASKIL 118
Cdd:pfam00579   5 PLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQLACGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 119 DPSRTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRYQAREPISLHEFLYPLAQGMDSVHLKNDIELGGTDQ 197
Cdd:pfam00579  81 DPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 198 KFNLLVGRDLQREY---DIDPQVCITMPLLVGTFGEEKMSKSLGN-AISFSD---TPQDMYGRTLSIPDDLIETYFRLLV 270
Cdd:pfam00579 161 WGNIELGRDLARRFnkkIFKKPVGLTNPLLTGLDGGKKMSKSAGNsAIFLDDdpeSVYKKIQKAYTDPDREVRKDLKLFT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1859508457 271 PHPETPAHLFMEIIRQNP-REAKRTLAREIVSLYHSRTEAVKAEEHFDRVF 320
Cdd:pfam00579 241 FLSNEEIEILEAELGKSPyREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 45-302 1.71e-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: 126.26  E-value: 1.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  45 GADPSRPDLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMIGDPSGKSKTRPQLSAEEARRNGETYFEQASKIL---DPS 121
Cdd:cd00395     5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGifeDPT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 122 RTTICYNSEWLGSMNFSDVIR-LSSHYTVARMLERDDFERRyqAREPISLHEFLYPLAQGMDSVHLKN----DIELGGTD 196
Cdd:cd00395    85 QATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSR--SEEGISATEFTYPPLQAADFLLLNTtegcDIQPGGSD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 197 QKFNLLVGRDLQREYDIDPQVCITMPLLVGTFGEEKMSKSLGNAISF---SDTPQDMYGRTLSIPDDLIETYFRLLVPHP 273
Cdd:cd00395   163 QWGNITLGRELARRFNGFTIAEGLTIPLVTKLDGPKFGKSESGPKWLdteKTSPYEFYQFWINAVDSDVINILKYFTFLS 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1859508457 274 ETPAHLFMEIIRQNP--REAKRTLAREIVSL 302
Cdd:cd00395   243 KEEIERLEQEQYEAPgyRVAQKTLAEEVTKT 273
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 6-249 1.81e-27

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 111.11  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457   6 IQEQLDLITRNTVEVIseeeLKKKLEKSSLTGQPLKVKLGADPSRPdLHLGHSVVLRKLRDFQDLGHQAILIIGDFTAMI 85
Cdd:PRK08560    1 IEERLELITRNTEEVV----TEEELRELLESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  86 GDpsgKSktrpqlSAEEARRNGETYFEQASKI-LDPSRTTICYNSEW-LGSMNFSDVIRLSSHYTVARMlerddfeRR-- 161
Cdd:PRK08560   76 ND---KG------DLEEIRKVAEYNKKVFEALgLDPDKTEFVLGSEFqLDKEYWLLVLKLAKNTTLARA-------RRsm 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 162 ----YQAREPiSLHEFLYPLAQGMDSVHLKNDIELGGTDQ-KFNLLVgRDLQREYDIDPQVCITMPLLVGTFGEE-KMSK 235
Cdd:PRK08560  140 timgRRMEEP-DVSKLVYPLMQVADIFYLDVDIAVGGMDQrKIHMLA-REVLPKLGYKKPVCIHTPLLTGLDGGGiKMSK 217

                         250
                  ....*....|....*
gi 1859508457 236 S-LGNAISFSDTPQD 249
Cdd:PRK08560  218 SkPGSAIFVHDSPEE 232
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 53-250 4.34e-11

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 63.72  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  53 LHLGHSV-VLRKLRDFQDLGHQAILIiGDFTAM---IGDPsgksktrpqlsaEEARRN-GETYFEQASKILDPSRTTICY 127
Cdd:PRK12282   15 LHLGHYVgSLKNRVALQNEHEQFVLI-ADQQALtdnAKNP------------EKIRRNiLEVALDYLAVGIDPAKSTIFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 128 NSEwlgsmnFSDVIRLSSHY----TVARMlerddfERRYQAREPISLHEF---------LYPLAQGMDSVHLKNDIELGG 194
Cdd:PRK12282   82 QSQ------IPELAELTMYYmnlvTVARL------ERNPTVKTEIAQKGFgrsipagflTYPVSQAADITAFKATLVPVG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859508457 195 TDQ------------KFNLLVGRDLQREydidPQVCIT-MPLLVGTFGEEKMSKSLGNAISFSDTPQDM 250
Cdd:PRK12282  150 DDQlpmieqtreivrRFNSLYGTDVLVE----PEALLPeAGRLPGLDGKAKMSKSLGNAIYLSDDADTI 214
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 53-250 1.67e-05

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: 46.55  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  53 LHLGHSVVLRKLRDFQDLGHQAILIIGD---FTAMIGDPSGKSKTRPQLSAeearrngeTYFEQAskiLDPSRTTICYNS 129
Cdd:TIGR00233  15 MHLGHYLGAIQTKWLQQFGVELFICIADlhaITVKQTDPDALRKAREELAA--------DYLAVG---LDPEKTFIFLQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 130 EWlgsMNFSD-VIRLSSHYTVARMlerddfERRYQ-----AREPISLHEFLYPLAQGMDSVHLKNDIELGGTDQKFNLLV 203
Cdd:TIGR00233  84 DY---PEHYElAWLLSCQVTFGEL------KRMTQfkdksQAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLEL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508457 204 GRDLQREYDID-------PQVCIT--MPLLVGTFGeEKMSKSLGN-AISFSDTPQDM 250
Cdd:TIGR00233 155 TRDLAERFNKKfknffpkPESLISkfFPRLMGLSG-KKMSKSDPNsAIFLTDTPKQI 210
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 50-247 5.04e-05

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: 45.04  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457  50 RP--DLHLGHSV-VLRKLRDFQDlGHQAILIIGDFTAMigdpsgkskTRPQlSAEEARRNgeTYfEQASKIL----DPSR 122
Cdd:COG0180    11 QPtgRLHLGNYLgALKNWVELQD-EYECFFFIADLHAL---------TTPQ-DPEELREN--TR-EVAADYLaaglDPEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 123 TTICYNSE--------WLgsmnfsdvirLSSHYTVARmLER-----DdfERRYQAREPISLHEFLYP-------LAQGMD 182
Cdd:COG0180    77 STIFVQSDvpehaelaWL----------LSCLTPLGE-LERmpqfkD--KSAKNGKENVNAGLLTYPvlmaadiLLYKAD 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508457 183 SV--------HLK--NDIElggtdQKFNLLVGrdlqrEYDIDPQVCIT--MPLLVGTFGEEKMSKSLGNAISFSDTP 247
Cdd:COG0180   144 LVpvgedqkqHLEltRDIA-----RRFNHRYG-----EVFPEPEALIPeeGARIPGLDGRKKMSKSYGNTINLLDDP 210
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 339-399 6.02e-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: 40.70  E-value: 6.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859508457 339 MPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLG--------KEARIIKSGKRKFFKV 399
Cdd:cd00165     1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGdvievdgkSIEEDIVYEDKKLLVV 69
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 128-249 9.39e-05

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 44.30  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508457 128 NSEWLGSMNfsdvirLSSHYTVARM------LERDDFERRYQArepislhEFLYPLAQGMDSVHLKNDIELGGTDQ-KFN 200
Cdd:PTZ00126  158 NDYWLRVMD------IARSFNITRIkrcsqiMGRSEGDEQPCA-------QILYPCMQCADIFYLKADICQLGMDQrKVN 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1859508457 201 LLVgrdlqREY----DIDPQVCI----TMPLLVGtfGEEKMSKSLGN-AISFSDTPQD 249
Cdd:PTZ00126  225 MLA-----REYcdkkKIKKKPIIlshhMLPGLLE--GQEKMSKSDPNsAIFMEDSEED 275
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 339-383 5.79e-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: 37.47  E-value: 5.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1859508457 339 MPLVDLLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLG 383
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPG 45
S4 smart00363
S4 RNA-binding domain;
344-383 4.11e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 4.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1859508457  344 LLIELNAVKSKSEARRLIQQNAVQIDDEKIGSIEHEVTLG 383
Cdd:smart00363   6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPG 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH