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Conserved domains on  [gi|503286911|ref|WP_013521572|]
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tyrosine--tRNA ligase [Taylorella equigenitalis]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11415010)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 14-406 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: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  14 QMDIVRRGTDEILVESEFLEKLQkshdsGTPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDP 93
Cdd:COG0162    4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  94 SGRNATRPPLTKEQIEVNAQTYYDQASKVLDPS--KTVISYNSKWCDALGARGLI-ELASKYTVARIMERDDFTKRFKGG 170
Cdd:COG0162   79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 171 IPISMHEILYPLMQGYDSVAL----KSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYI 246
Cdd:COG0162  159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 247 GITE---TPDSMFGKIMSISDSLMWNYYELISSKSLDEIKKLKQDVEDGINPRNIKVALAQEIITRFHNSQAAEKALADF 323
Cdd:COG0162  238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 324 ELRFRDGQIPEDIPEVTLPGPE--MGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSG------TYVVQ 395
Cdd:COG0162  318 EALFGKGELPDDLPEVELSAAEggIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGdllhggYLVLR 397

                        410
                 ....*....|.
gi 503286911 396 IGKRKFARITI 406
Cdd:COG0162  398 VGKKKFALVKL 408
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 14-406 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: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  14 QMDIVRRGTDEILVESEFLEKLQkshdsGTPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDP 93
Cdd:COG0162    4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  94 SGRNATRPPLTKEQIEVNAQTYYDQASKVLDPS--KTVISYNSKWCDALGARGLI-ELASKYTVARIMERDDFTKRFKGG 170
Cdd:COG0162   79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 171 IPISMHEILYPLMQGYDSVAL----KSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYI 246
Cdd:COG0162  159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 247 GITE---TPDSMFGKIMSISDSLMWNYYELISSKSLDEIKKLKQDVEDGINPRNIKVALAQEIITRFHNSQAAEKALADF 323
Cdd:COG0162  238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 324 ELRFRDGQIPEDIPEVTLPGPE--MGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSG------TYVVQ 395
Cdd:COG0162  318 EALFGKGELPDDLPEVELSAAEggIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGdllhggYLVLR 397

                        410
                 ....*....|.
gi 503286911 396 IGKRKFARITI 406
Cdd:COG0162  398 VGKKKFALVKL 408
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 23-406 1.89e-150

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 432.02  E-value: 1.89e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  23 DEILVESEFLEKLQKSHDSGTPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSGRNATRPP 102
Cdd:PRK13354  12 RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 103 LTKEQIEVNAQTYYDQASKVLDPSKTVISYNSKWCDALGARGLI-ELASKYTVARIMERDDFTKRFKGGIPISMHEILYP 181
Cdd:PRK13354  92 LTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 182 LMQGYDSVAL----KSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGVeKMSKSKNNYIGITE---TPDS 254
Cdd:PRK13354 172 LLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPektSPYE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 255 MFGKIMSISDSLMWNYYELISSKSLDEIKKLKQDVEDGINPRNIKVALAQEIITRFHNSQAAEKALADFELRFRDGQIPE 334
Cdd:PRK13354 251 FYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPL 330

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503286911 335 -DIPEVTLPGPEMGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSGT------YVVQIGKRKFARITI 406
Cdd:PRK13354 331 kDIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDafdgkfVILRRGKKKFFLVKL 409
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 10-388 3.56e-131

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: 381.75  E-value: 3.56e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   10 EVARQMDIVRRGTDEILVE-SEFLEKLQKShdsgtPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTA 88
Cdd:TIGR00234   1 MNNILLLLTKRGLEVQTPEeEKDLLKLLER-----PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   89 TIGDPSGRNATRPPLTKEQIEVNAQTYYDQASKVLDPSKTVISYNSKWCDALGARGLIELASK-YTVARIMERDDFTKRF 167
Cdd:TIGR00234  76 LIGDPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  168 KGGipISMHEILYPLMQGYDSVALKSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYIG 247
Cdd:TIGR00234 156 EEN--ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVS 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  248 ITETPDSMFGKIMSISDSLMWNYYELISSKSLDEIKKLKQdvEDGINPRNIKVALAQEIITRFHNSQAAEKALADFELRF 327
Cdd:TIGR00234 233 LDEGKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIF 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503286911  328 RDGQIPEDIPEVTLP--GPEMGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILK 388
Cdd:TIGR00234 311 SGGLNPDEVPIFRPEkfGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRK 373
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 45-309 1.35e-102

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: 304.91  E-value: 1.35e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  45 LRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSGRNATRPPLTKEQIEVNAQTYYDQASKVLD 124
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 125 ---PSKTVISYNSKWCDALGARGLIELASKYTVARIMERDDFTKRFKGGIPISMHEILYPLMQGYDSVALKSDMELGGTD 201
Cdd:cd00805   81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 202 QKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYI--GITETPDSMFGKIMSISDSLMWNYYELISSKSL 279
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 503286911 280 DEIKKLKQDVEDGINPRNIKVALAQEIITR 309
Cdd:cd00805  240 EEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
41-327 2.10e-86

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 264.52  E-value: 2.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   41 SGTPLRIKLGLDPTAPdLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSgRNATRPPLTKEQIEVNAqtYYDQAS 120
Cdd:pfam00579   2 KNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  121 KVLDPSKTVISYNSKWCDALGARGLIE-LASKYTVARIMERDDFTKRFKGGIPISMHEILYPLMQGYDSVALKSDMELGG 199
Cdd:pfam00579  78 CGLDPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  200 TDQKFNLLVGRELQKEYGQ---PQQTVLTMPLLVGLDGVEKMSKSKNN----YIGITETPDSMFGKIMSISDSLMWNYYE 272
Cdd:pfam00579 158 SDQWGNIELGRDLARRFNKkifKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 503286911  273 LISSKSLDEIKKLKQDVEDGInPRNIKVALAQEIITRFHNSQAAEKALADFELRF 327
Cdd:pfam00579 238 LFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
S4 smart00363
S4 RNA-binding domain;
351-403 1.58e-04

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 39.50  E-value: 1.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 503286911   351 VLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSGTYV-VQIGKRKFAR 403
Cdd:smart00363   6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVIsVRGKELKRLK 59
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 14-406 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: 570.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  14 QMDIVRRGTDEILVESEFLEKLQkshdsGTPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDP 93
Cdd:COG0162    4 LLELIWRGLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  94 SGRNATRPPLTKEQIEVNAQTYYDQASKVLDPS--KTVISYNSKWCDALGARGLI-ELASKYTVARIMERDDFTKRFKGG 170
Cdd:COG0162   79 SGKSEERKLLTEEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 171 IPISMHEILYPLMQGYDSVAL----KSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYI 246
Cdd:COG0162  159 QGISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 247 GITE---TPDSMFGKIMSISDSLMWNYYELISSKSLDEIKKLKQDVEDGINPRNIKVALAQEIITRFHNSQAAEKALADF 323
Cdd:COG0162  238 WLDEektSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 324 ELRFRDGQIPEDIPEVTLPGPE--MGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSG------TYVVQ 395
Cdd:COG0162  318 EALFGKGELPDDLPEVELSAAEggIPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGdllhggYLVLR 397

                        410
                 ....*....|.
gi 503286911 396 IGKRKFARITI 406
Cdd:COG0162  398 VGKKKFALVKL 408
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 23-406 1.89e-150

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 432.02  E-value: 1.89e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  23 DEILVESEFLEKLQKSHDSGTPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSGRNATRPP 102
Cdd:PRK13354  12 RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 103 LTKEQIEVNAQTYYDQASKVLDPSKTVISYNSKWCDALGARGLI-ELASKYTVARIMERDDFTKRFKGGIPISMHEILYP 181
Cdd:PRK13354  92 LTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 182 LMQGYDSVAL----KSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGVeKMSKSKNNYIGITE---TPDS 254
Cdd:PRK13354 172 LLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPektSPYE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 255 MFGKIMSISDSLMWNYYELISSKSLDEIKKLKQDVEDGINPRNIKVALAQEIITRFHNSQAAEKALADFELRFRDGQIPE 334
Cdd:PRK13354 251 FYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPL 330

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503286911 335 -DIPEVTLPGPEMGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSGT------YVVQIGKRKFARITI 406
Cdd:PRK13354 331 kDIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDafdgkfVILRRGKKKFFLVKL 409
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 10-388 3.56e-131

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: 381.75  E-value: 3.56e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   10 EVARQMDIVRRGTDEILVE-SEFLEKLQKShdsgtPLRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTA 88
Cdd:TIGR00234   1 MNNILLLLTKRGLEVQTPEeEKDLLKLLER-----PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   89 TIGDPSGRNATRPPLTKEQIEVNAQTYYDQASKVLDPSKTVISYNSKWCDALGARGLIELASK-YTVARIMERDDFTKRF 167
Cdd:TIGR00234  76 LIGDPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  168 KGGipISMHEILYPLMQGYDSVALKSDMELGGTDQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYIG 247
Cdd:TIGR00234 156 EEN--ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVS 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  248 ITETPDSMFGKIMSISDSLMWNYYELISSKSLDEIKKLKQdvEDGINPRNIKVALAQEIITRFHNSQAAEKALADFELRF 327
Cdd:TIGR00234 233 LDEGKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIF 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503286911  328 RDGQIPEDIPEVTLP--GPEMGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILK 388
Cdd:TIGR00234 311 SGGLNPDEVPIFRPEkfGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRK 373
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 45-309 1.35e-102

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: 304.91  E-value: 1.35e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  45 LRIKLGLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSGRNATRPPLTKEQIEVNAQTYYDQASKVLD 124
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 125 ---PSKTVISYNSKWCDALGARGLIELASKYTVARIMERDDFTKRFKGGIPISMHEILYPLMQGYDSVALKSDMELGGTD 201
Cdd:cd00805   81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 202 QKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNNYI--GITETPDSMFGKIMSISDSLMWNYYELISSKSL 279
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 503286911 280 DEIKKLKQDVEDGINPRNIKVALAQEIITR 309
Cdd:cd00805  240 EEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
41-327 2.10e-86

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 264.52  E-value: 2.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   41 SGTPLRIKLGLDPTAPdLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSgRNATRPPLTKEQIEVNAqtYYDQAS 120
Cdd:pfam00579   2 KNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  121 KVLDPSKTVISYNSKWCDALGARGLIE-LASKYTVARIMERDDFTKRFKGGIPISMHEILYPLMQGYDSVALKSDMELGG 199
Cdd:pfam00579  78 CGLDPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  200 TDQKFNLLVGRELQKEYGQ---PQQTVLTMPLLVGLDGVEKMSKSKNN----YIGITETPDSMFGKIMSISDSLMWNYYE 272
Cdd:pfam00579 158 SDQWGNIELGRDLARRFNKkifKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 503286911  273 LISSKSLDEIKKLKQDVEDGInPRNIKVALAQEIITRFHNSQAAEKALADFELRF 327
Cdd:pfam00579 238 LFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 50-307 1.34e-38

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: 139.75  E-value: 1.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  50 GLDPTAPDLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPSGRNATRPPLTKEQIEVNAQTYYDQASKVL---DPS 126
Cdd:cd00395    5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGifeDPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 127 KTVISYNSKWCDALG-ARGLIELASKYTVARIMERDDFTKRFKGGipISMHEILYPLMQGYD----SVALKSDMELGGTD 201
Cdd:cd00395   85 QATLFNNSDWPGPLAhIQFLRDLGKHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPGGSD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 202 QKFNLLVGREL-QKEYGQPQQTVLTMPLLVGLDGvEKMSKSKNN---YIGITETPDSMFGKIMSISDSLMWNYYELISSK 277
Cdd:cd00395  163 QWGNITLGRELaRRFNGFTIAEGLTIPLVTKLDG-PKFGKSESGpkwLDTEKTSPYEFYQFWINAVDSDVINILKYFTFL 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 503286911 278 SLDEIKKLKQDVEDGINPRNIKVALAQEII 307
Cdd:cd00395  242 SKEEIERLEQEQYEAPGYRVAQKTLAEEVT 271
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 15-260 1.34e-22

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 97.63  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  15 MDIVRRGTDEILVESEFLEKLQkshdSGTPLRIKLGLDPTAPdLHLGHTVVLTKMRQLQDMGHEVIFLIGDFTATIGDPS 94
Cdd:PRK08560   5 LELITRNTEEVVTEEELRELLE----SKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLNDKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  95 grnatrpplTKEQIEVNAQTYYDQASKV-LDPSKTVISYNSK-------WCDalgargLIELASKYTVARIMERDDFTKR 166
Cdd:PRK08560  80 ---------DLEEIRKVAEYNKKVFEALgLDPDKTEFVLGSEfqldkeyWLL------VLKLAKNTTLARARRSMTIMGR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 167 FKGGIPISMheILYPLMQGYDSVALKSDMELGGTDQ-KFNLLVgRELQKEYGQPQQTVLTMPLLVGLDGVE-KMSKSK-N 243
Cdd:PRK08560 145 RMEEPDVSK--LVYPLMQVADIFYLDVDIAVGGMDQrKIHMLA-REVLPKLGYKKPVCIHTPLLTGLDGGGiKMSKSKpG 221

                        250
                 ....*....|....*..
gi 503286911 244 NYIGITETPDSMFGKIM 260
Cdd:PRK08560 222 SAIFVHDSPEEIRRKIK 238
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 53-261 7.18e-12

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 66.03  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  53 PTAPdLHLGHTVVLTKMR-QLQDmGHEVIFLIGDFTAtIGDpsgrNATRPPLTKEQI-EVNAqtyyDQASKVLDPSKTVI 130
Cdd:PRK12282  11 PTGK-LHLGHYVGSLKNRvALQN-EHEQFVLIADQQA-LTD----NAKNPEKIRRNIlEVAL----DYLAVGIDPAKSTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 131 SYNSkwcdALGArgLIELASKY----TVARiMERDDFTKR------FKGGIPISMheILYPLMQGYDSVALKSDMELGGT 200
Cdd:PRK12282  80 FIQS----QIPE--LAELTMYYmnlvTVAR-LERNPTVKTeiaqkgFGRSIPAGF--LTYPVSQAADITAFKATLVPVGD 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503286911 201 DQ------------KFNLLVGRELQKEygqPQQTVLTMPLLVGLDGVEKMSKSKNNYIGITETPDSMFGKIMS 261
Cdd:PRK12282 151 DQlpmieqtreivrRFNSLYGTDVLVE---PEALLPEAGRLPGLDGKAKMSKSLGNAIYLSDDADTIKKKVMS 220
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 202-294 5.40e-10

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: 60.06  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 202 QKFNLLvgrelqkeYGQpqqtVLTMP---------LLVGLDGVEKMSKSKNNYIGITETPDSMFGKIMSI-SDSL----- 266
Cdd:COG0180  163 RRFNHR--------YGE----VFPEPealipeegaRIPGLDGRKKMSKSYGNTINLLDDPKEIRKKIKSAvTDSErlryd 230

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 503286911 267 ---------MWNYYELISSK-SLDEIKK-----------LKQDVEDGIN 294
Cdd:COG0180  231 dpgkpevcnLFTIYSAFSGKeEVEELEAeyraggigygdLKKALAEAVV 279
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 44-262 2.40e-09

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: 58.11  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911   44 PLRIKLGLDPTAPdLHLGHTVVLTKMRQLQDMGHEVIFLIGD---FTATIGDPSGRNATRPPLTKEQIEVNaqtyydqas 120
Cdd:TIGR00233   2 KFRVLTGIQPSGK-MHLGHYLGAIQTKWLQQFGVELFICIADlhaITVKQTDPDALRKAREELAADYLAVG--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  121 kvLDPSKTVISYNSkwcDALGARGLIELASKYTVARIMER-DDFT-KRFKGGIPISMheILYPLMQGYDSVALKSDMELG 198
Cdd:TIGR00233  72 --LDPEKTFIFLQS---DYPEHYELAWLLSCQVTFGELKRmTQFKdKSQAENVPIGL--LSYPVLQAADILLYQADLVPV 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503286911  199 GTDQKFNLLVGREL----QKEYGQ----PQQTV-LTMPLLVGLDGVeKMSKSK-NNYIGITETPDSMFGKIMSI 262
Cdd:TIGR00233 145 GIDQDQHLELTRDLaerfNKKFKNffpkPESLIsKFFPRLMGLSGK-KMSKSDpNSAIFLTDTPKQIKKKIRKA 217
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 202-310 8.57e-06

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 47.39  E-value: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 202 QKFNLLvgrelqkeYGQpqqtVLTMP---------LLVGLDG-VEKMSKS---KNNYIGITETPDSMFGKIMSI-SDSL- 266
Cdd:PRK00927 160 RRFNNL--------YGE----VFPVPeplipkvgaRVMGLDGpTKKMSKSdpnDNNTINLLDDPKTIAKKIKKAvTDSEr 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503286911 267 ----------------MWNYYELISSKSLDEIKKL-----KQDVEdginprnIKVALAQEIITRF 310
Cdd:PRK00927 228 lreirydlpnkpevsnLLTIYSALSGESIEELEAEyeaggKGYGD-------FKKDLAEAVVEFL 285
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 346-400 8.57e-06

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: 43.39  E-value: 8.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503286911 346 MGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSGtYVVQIGKRK 400
Cdd:cd00165    1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPG-DVIEVDGKS 54
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 346-390 1.77e-05

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: 41.71  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 503286911  346 MGIVSVLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSG 390
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPG 45
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 146-306 1.79e-05

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 46.61  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 146 IELASKYTVAR------IMERDDFTKRfkggiPISmhEILYPLMQGYDSVALKSDMELGGTDQ-KFNLLvGRE---LQKE 215
Cdd:PTZ00126 165 MDIARSFNITRikrcsqIMGRSEGDEQ-----PCA--QILYPCMQCADIFYLKADICQLGMDQrKVNML-AREycdKKKI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 216 YGQPqqTVLTMPLLVGL-DGVEKMSKS-KNNYIGITETPDSMFGKIMS-------ISDSLMWNYYELISSKSLDEI---- 282
Cdd:PTZ00126 237 KKKP--IILSHHMLPGLlEGQEKMSKSdPNSAIFMEDSEEDVNRKIKKaycppgvIEGNPILAYFKSIVFPAFNSFtvlr 314

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 503286911 283 -------------KKLKQDVEDG-INPRNIKVALAQEI 306
Cdd:PTZ00126 315 keknggdvtyttyEELEKDYLSGaLHPGDLKPALAKYL 352
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 50-242 8.62e-05

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: 42.47  E-value: 8.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  50 GLDPTAPdLHLGHTVVLTKMRQLQ----DMGHEV--IFLIGDFTATIGDPSGRNATRPPLTKEQievnaqtyydqaskvl 123
Cdd:cd00802    5 GITPNGY-LHIGHLRTIVTFDFLAqayrKLGYKVrcIALIDDAGGLIGDPANKKGENAKAFVER---------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911 124 dpsktvisynskwcdalgarglielaskytvarimerddFTKRFKggipismHEILYPLMQGYDSVAL---KSDMELGGT 200
Cdd:cd00802   68 ---------------------------------------WIERIK-------EDVEYMFLQAADFLLLyetECDIHLGGS 101

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 503286911 201 DQKFNLLVGRELQKEYGQPQQTVLTMPLLVGLDGVEKMSKSK 242
Cdd:cd00802  102 DQLGHIELGLELLKKAGGPARPFGLTFGRVMGADGTKMSKSK 143
S4 smart00363
S4 RNA-binding domain;
351-403 1.58e-04

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 39.50  E-value: 1.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 503286911   351 VLRESGLAVSGSEASRNIVQGGVKVDGSKVEDKGLILKSGTYV-VQIGKRKFAR 403
Cdd:smart00363   6 FLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVIsVRGKELKRLK 59
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 17-241 1.98e-04

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 43.74  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  17 IVRRGTDEILVESEFLEKLQKSHDsgtpLRIKLGLDPTApDLHLGHTVV-LTKMRQLQDMGHEVIFLIGDFTATIGDPSG 95
Cdd:PTZ00348   9 LLRSVGEECIQESELRNLIEKKPL----IRCYDGFEPSG-RMHIAQGIFkAVNVNKCTQAGCEFVFWVADWFALMNDKVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503286911  96 RNATRPPLTKEQ-IEVNAQTYYDQASKVLDPSKTVIS--YNSKWcdalgaRGLIELASKYTVARIMERDDFTKRFKGgiP 172
Cdd:PTZ00348  84 GELEKIRIVGRYlIEVWKAAGMDMDKVLFLWSSEEITnhANTYW------RTVLDIGRQNTIARIKKCCTIMGKTEG--T 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503286911 173 ISMHEILYPLMQGYDSVALKSDM-ELGGTDQKFNLL-------VGRELQKeygqpqqTVLTMPLLVGL-DGVEKMSKS 241
Cdd:PTZ00348 156 LTAAQVLYPLMQCADIFFLKADIcQLGLDQRKVNMLareycdlIGRKLKP-------VILSHHMLAGLkQGQAKMSKS 226
LeuS COG0495
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ...
 226-269 4.61e-03

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


Pssm-ID: 440261 [Multi-domain]  Cd Length: 826  Bit Score: 39.26  E-value: 4.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503286911 226 MPLLVGLDGV-----EKMSKSKNNYIgiteTPDSMFGK---------IMSIS---DSLMWN 269
Cdd:COG0495  573 MVLEVGKDGVviggiEKMSKSKGNVV----DPDEIIEKygadtlrlfEMFAGppeRDLEWS 629
 
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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