|
Name |
Accession |
Description |
Interval |
E-value |
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
33-501 |
0e+00 |
|
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 776.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 33 HGEKMTEFSEWFHNILEEAEIIDQrYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDELAKEAIHVK 111
Cdd:TIGR00408 1 MASKMQDFSEWYHQILEKAEIIDY-YPVKGCYVWLPYGFKIWKNIQKILRNILDEiGHEEVYFPMLIPESELAKEKDHIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 112 GFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREITtFKEAHT 191
Cdd:TIGR00408 80 GFEPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFT-WQEAHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 192 IHATASEAEEQVERAVEIYKEFF-NSLGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFEIK 270
Cdd:TIGR00408 159 AHATAEEAEEQVLRALDIYKEFIeNSLAIPYFVGRKPEWEKFAGAEYTWAFETIMPDGRTLQIATSHNLGQNFAKTFEIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 271 FETPEGDHEYVHQTCYGLSDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAA-EEVMEACRELRSRLEAAGFRV 349
Cdd:TIGR00408 239 FETPTGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPIIFKKKEnEKVMEAAREVRSRLKKAGFRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 350 HLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMES 429
Cdd:TIGR00408 319 HIDDRDNRPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWERFEQ 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1NJ2_A 430 EIREAETLEEASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGS--GTCINCGREAPYRAYLARTY 501
Cdd:TIGR00408 399 KIVIVETLEEIKQALNEKRGVVLVPWCGEEECEEDLKEKVQVTILCIPEDGDvlQLCIFCGRKAPDYVLIARTY 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
39-299 |
1.48e-154 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 440.49 E-value: 1.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 39 EFSEWFHNILEEAEIIDqRYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDELAKEAIHVKGFEDEV 117
Cdd:cd00778 1 DFSEWYTEVITKAELID-YGPVKGCMVFRPYGYAIWENIQKILDKEIKEtGHENVYFPLLIPESELEKEKEHIEGFAPEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 118 YWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREItTFKEAHTIHATAS 197
Cdd:cd00778 80 AWVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREF-LWQEGHTAHATEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 198 EAEEQVERAVEIYKEFFNS-LGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEG 276
Cdd:cd00778 159 EAEEEVLQILDLYKEFYEDlLAIPVVKGRKTEWEKFAGADYTYTIEAMMPDGRALQSGTSHNLGQNFSKAFDIKYQDKDG 238
|
250 260
....*....|....*....|...
1NJ2_A 277 DHEYVHQTCYGLSDRVIASVIAI 299
Cdd:cd00778 239 QKEYVHQTSWGISTRLIGAIIMI 261
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
39-412 |
6.92e-87 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 277.81 E-value: 6.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 39 EFSEWFHNILEEAEIIdqRYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEdELAKEAIHVKGFEDEV 117
Cdd:COG0442 17 DAEVWSHQLMLRAGLI--RKLASGIYTYLPLGYRVLEKIEAIVREEMKRtGAQEVLMPLLQPA-ELWEESGRWEGFGPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 118 YWVTHgglsKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREittF--KEAHTIHAT 195
Cdd:COG0442 94 ARVTD----RLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTRE---FlmKDAYSFHAT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 196 ASEAEEQVERAVEIYKEFFNSLGIPYLI-------------------------------------------TRRPPWDKF 232
Cdd:COG0442 167 EEELDEEYQKMLDAYERIFERLGLPVRAveadsgaiggseshefmvladsgedtivycdacdyaaniekaeALAPPAERA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 233 PGSEYTVAFDT--------------------------------------------------------------------- 243
Cdd:COG0442 247 EPTKELEAVATpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaal 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 244 ----------------------------------------------------------------------LMPDGKTLQI 253
Cdd:COG0442 327 gavpgflgpvglgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggLLQDGRGIEV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 254 GTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGLSD-RVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKaaEEVM 332
Cdd:COG0442 407 GHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVtRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD--EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 333 EACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELM 412
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKELL 564
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
316-411 |
1.30e-25 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 100.35 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 316 QVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGE 395
Cdd:pfam03129 1 QVVVIPL--GEKAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGE 78
|
90
....*....|....*.
1NJ2_A 396 KVTADLQGIEETLREL 411
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
41-398 |
1.94e-23 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 102.63 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 41 SEWFHNILEE----AEIIDQRYPVK---------GMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDeLAKE 106
Cdd:PRK12325 4 SRYFLPTLKEnpkeAEIVSHRLMLRagmirqqaaGIYSWLPLGLKVLKKIENIVREEQNRaGAIEILMPTIQPAD-LWRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 107 AIHVKGFEDEVYWVT--HgglsklQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETkhtRP---LIRVR 181
Cdd:PRK12325 83 SGRYDAYGKEMLRIKdrH------DREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEI---RPrfgVMRGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 182 E---------------------------ITTFKE-------------------AHTIHATASEAEEQVeraveIY-KEFF 214
Cdd:PRK12325 154 EflmkdaysfdldeegarhsynrmfvayLRTFARlglkaipmradtgpiggdlSHEFIILAETGESTV-----FYdKDFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 215 NSLGIPYLITRRPPWDKFPGSEYT------------VAFDTLMPD----GKTLQIGTVHNLGQTFARTFEIKFETPEGDH 278
Cdd:PRK12325 229 DLLVPGEDIDFDVADLQPIVDEWTslyaateemhdeAAFAAVPEErrlsARGIEVGHIFYFGTKYSEPMNAKVQGPDGKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 279 EYVHQTCYGLS-DRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIR 357
Cdd:PRK12325 309 VPVHMGSYGIGvSRLVAAIIEASHDDKGIIWPESVAPFKVGIINL--KQGDEACDAACEKLYAALSAAGIDVLYDDTDER 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
1NJ2_A 358 AGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVT 398
Cdd:PRK12325 387 PGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREE 427
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
437-501 |
5.35e-17 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 75.30 E-value: 5.35e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1NJ2_A 437 LEEASRIVDEKrGIISFMWCGEEECGMDVEEKVRVDILGI---QEEGSGTCINCGREAPYRAYLARTY 501
Cdd:smart00946 1 LEEFKKALEEG-KFVLAPWCGDEECEEKIKEETGATIRCIpfdQDEEPGKCVVCGKPAKKWVLFARSY 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| proS_fam_I |
TIGR00408 |
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
33-501 |
0e+00 |
|
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 776.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 33 HGEKMTEFSEWFHNILEEAEIIDQrYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDELAKEAIHVK 111
Cdd:TIGR00408 1 MASKMQDFSEWYHQILEKAEIIDY-YPVKGCYVWLPYGFKIWKNIQKILRNILDEiGHEEVYFPMLIPESELAKEKDHIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 112 GFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREITtFKEAHT 191
Cdd:TIGR00408 80 GFEPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFT-WQEAHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 192 IHATASEAEEQVERAVEIYKEFF-NSLGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFEIK 270
Cdd:TIGR00408 159 AHATAEEAEEQVLRALDIYKEFIeNSLAIPYFVGRKPEWEKFAGAEYTWAFETIMPDGRTLQIATSHNLGQNFAKTFEIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 271 FETPEGDHEYVHQTCYGLSDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAA-EEVMEACRELRSRLEAAGFRV 349
Cdd:TIGR00408 239 FETPTGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIPIIFKKKEnEKVMEAAREVRSRLKKAGFRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 350 HLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMES 429
Cdd:TIGR00408 319 HIDDRDNRPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWERFEQ 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1NJ2_A 430 EIREAETLEEASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGS--GTCINCGREAPYRAYLARTY 501
Cdd:TIGR00408 399 KIVIVETLEEIKQALNEKRGVVLVPWCGEEECEEDLKEKVQVTILCIPEDGDvlQLCIFCGRKAPDYVLIARTY 472
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
39-299 |
1.48e-154 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 440.49 E-value: 1.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 39 EFSEWFHNILEEAEIIDqRYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDELAKEAIHVKGFEDEV 117
Cdd:cd00778 1 DFSEWYTEVITKAELID-YGPVKGCMVFRPYGYAIWENIQKILDKEIKEtGHENVYFPLLIPESELEKEKEHIEGFAPEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 118 YWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREItTFKEAHTIHATAS 197
Cdd:cd00778 80 AWVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREF-LWQEGHTAHATEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 198 EAEEQVERAVEIYKEFFNS-LGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEG 276
Cdd:cd00778 159 EAEEEVLQILDLYKEFYEDlLAIPVVKGRKTEWEKFAGADYTYTIEAMMPDGRALQSGTSHNLGQNFSKAFDIKYQDKDG 238
|
250 260
....*....|....*....|...
1NJ2_A 277 DHEYVHQTCYGLSDRVIASVIAI 299
Cdd:cd00778 239 QKEYVHQTSWGISTRLIGAIIMI 261
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
305-501 |
8.69e-89 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 270.32 E-value: 8.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 305 GLCLPPDVAAHQVVIVPIIFKKA-AEEVMEACRELRSRLEAAGFRVHLDDRDI-RAGRKYYEWEMRGVPLRVEIGPRDLE 382
Cdd:cd00862 1 GLVLPPRVAPIQVVIVPIGIKDEkREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 383 KGAAVISRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMESeIREAETLEEASRIVDEKrGIISFMWCGEEECG 462
Cdd:cd00862 81 KNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEK-GIVLAPWCGEEECE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1NJ2_A 463 MDVEEKVRVDILGIQ-----EEGSGTCINCGREAPYRAYLARTY 501
Cdd:cd00862 159 EEIKEETAATILCIPfdeakLEEGGKCVVCGRPAKAYARFAKSY 202
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
39-412 |
6.92e-87 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 277.81 E-value: 6.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 39 EFSEWFHNILEEAEIIdqRYPVKGMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEdELAKEAIHVKGFEDEV 117
Cdd:COG0442 17 DAEVWSHQLMLRAGLI--RKLASGIYTYLPLGYRVLEKIEAIVREEMKRtGAQEVLMPLLQPA-ELWEESGRWEGFGPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 118 YWVTHgglsKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREittF--KEAHTIHAT 195
Cdd:COG0442 94 ARVTD----RLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRTRE---FlmKDAYSFHAT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 196 ASEAEEQVERAVEIYKEFFNSLGIPYLI-------------------------------------------TRRPPWDKF 232
Cdd:COG0442 167 EEELDEEYQKMLDAYERIFERLGLPVRAveadsgaiggseshefmvladsgedtivycdacdyaaniekaeALAPPAERA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 233 PGSEYTVAFDT--------------------------------------------------------------------- 243
Cdd:COG0442 247 EPTKELEAVATpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllgaselelateeeieaal 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 244 ----------------------------------------------------------------------LMPDGKTLQI 253
Cdd:COG0442 327 gavpgflgpvglgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpcpdcggLLQDGRGIEV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 254 GTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGLSD-RVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKaaEEVM 332
Cdd:COG0442 407 GHIFKLGTKYSKAMDATFLDENGKEQPVWMGCYGIGVtRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKD--EAVL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 333 EACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELM 412
Cdd:COG0442 485 EAAEELYAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETVKELL 564
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
39-297 |
1.73e-54 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 183.72 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 39 EFSEWFHNILEEAEIIDQrYPVKGMHVWMPHGFMIRKNTLKIL-RRILDRDHEEVLFPLLVPEDELAKEAIHVKGFEDEV 117
Cdd:cd00772 1 DASEKSLEHIGKAELADQ-GPGRGIINFLPLAKAILDKIENVLdKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 118 YWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREItTFKEAHTIHATAS 197
Cdd:cd00772 80 AVFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREF-IMKDGHSAHADAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 198 EAEEQVERAVEIYKEFFNSLG-IPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLGQTFARTFE--IKFETP 274
Cdd:cd00772 159 EADEEFLNMLSAYAEIARDLAaIDFIEGEADEGAKFAGASKSREFEALMEDGKAKQAETGHIFGEGFARAFDlkAKFLDK 238
|
250 260
....*....|....*....|....
1NJ2_A 275 EGDHEYVHQTCYGLS-DRVIASVI 297
Cdd:cd00772 239 DGKEKFFEMGCWGIGiSRFIGAII 262
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
82-297 |
2.49e-26 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 107.09 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 82 RRILDRDHEEVLFPLLVPEDELAKEaIHVKGFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFY 161
Cdd:cd00670 14 DRMAEYGYQEILFPFLAPTVLFFKG-GHLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEILSYRALPLRLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 162 QVVNTFRYETKHTRPLIRVREITTFkEAHTIHaTASEAEEQVERAVEIYKEFFNSLGIPYLI--------TRRPPWDKFP 233
Cdd:cd00670 93 QIGPCFRHEPSGRRGLMRVREFRQV-EYVVFG-EPEEAEEERREWLELAEEIARELGLPVRVvvaddpffGRGGKRGLDA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1NJ2_A 234 GSEYTVAFDTLMPD-GKTLQIGTVH--NLGQTFARTFEIkfetPEGDHEYVHQTC--YGLSDRVIASVI 297
Cdd:cd00670 171 GRETVVEFELLLPLpGRAKETAVGSanVHLDHFGASFKI----DEDGGGRAHTGCggAGGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
316-411 |
1.30e-25 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 100.35 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 316 QVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGE 395
Cdd:pfam03129 1 QVVVIPL--GEKAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGE 78
|
90
....*....|....*.
1NJ2_A 396 KVTADLQGIEETLREL 411
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
126-300 |
2.28e-25 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 102.49 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 126 SKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKH-TRPLIRVREITTfKEAHTIHaTASEAEEQVE 204
Cdd:pfam00587 5 DENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGdTRGLIRVRQFHQ-DDAHIFH-APGQSPDELE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 205 RAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYTVAFDTLMPD-GKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQ 283
Cdd:pfam00587 83 DYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSlGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYM 162
|
170
....*....|....*....
1NJ2_A 284 TCYGL--SDRVIASVIAIH 300
Cdd:pfam00587 163 IHRAGlgVERFLAAILENN 181
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
41-398 |
1.94e-23 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 102.63 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 41 SEWFHNILEE----AEIIDQRYPVK---------GMHVWMPHGFMIRKNTLKILRRILDR-DHEEVLFPLLVPEDeLAKE 106
Cdd:PRK12325 4 SRYFLPTLKEnpkeAEIVSHRLMLRagmirqqaaGIYSWLPLGLKVLKKIENIVREEQNRaGAIEILMPTIQPAD-LWRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 107 AIHVKGFEDEVYWVT--HgglsklQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETkhtRP---LIRVR 181
Cdd:PRK12325 83 SGRYDAYGKEMLRIKdrH------DREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEI---RPrfgVMRGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 182 E---------------------------ITTFKE-------------------AHTIHATASEAEEQVeraveIY-KEFF 214
Cdd:PRK12325 154 EflmkdaysfdldeegarhsynrmfvayLRTFARlglkaipmradtgpiggdlSHEFIILAETGESTV-----FYdKDFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 215 NSLGIPYLITRRPPWDKFPGSEYT------------VAFDTLMPD----GKTLQIGTVHNLGQTFARTFEIKFETPEGDH 278
Cdd:PRK12325 229 DLLVPGEDIDFDVADLQPIVDEWTslyaateemhdeAAFAAVPEErrlsARGIEVGHIFYFGTKYSEPMNAKVQGPDGKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 279 EYVHQTCYGLS-DRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIR 357
Cdd:PRK12325 309 VPVHMGSYGIGvSRLVAAIIEASHDDKGIIWPESVAPFKVGIINL--KQGDEACDAACEKLYAALSAAGIDVLYDDTDER 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
1NJ2_A 358 AGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVT 398
Cdd:PRK12325 387 PGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREE 427
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
246-411 |
4.15e-23 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 102.47 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 246 PDGK-TLQ------IGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGL--SdRVIASVIAIHGDESGLCLPPDVAAHQ 316
Cdd:PRK09194 392 PDGGgTLKiargieVGHIFQLGTKYSEAMNATVLDENGKAQPLIMGCYGIgvS-RLVAAAIEQNHDEKGIIWPKAIAPFD 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 317 VVIVPIIFKKaaEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEK 396
Cdd:PRK09194 471 VHIVPVNMKD--EEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEK 548
|
170
....*....|....*
1NJ2_A 397 VTADLQGIEETLREL 411
Cdd:PRK09194 549 EEVPVDELVEFLKAL 563
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
316-409 |
6.29e-21 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 87.07 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 316 QVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGE 395
Cdd:cd00738 3 DVAIVPL--TDPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
1NJ2_A 396 KVTADLQGIEETLR 409
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
62-409 |
1.53e-19 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 91.62 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 62 GMHVWMPHGFMIRKNTLKILRR-ILDRDHEEVLFPLLVpEDELAKEAIHVKGFEDEVYWVTHGGlsklQRKLALRPTSET 140
Cdd:TIGR00418 191 GLPFWLPKGATIRNLLEDFVRQkQIKYGYMEVETPIMY-DLELWEISGHWDNYKERMFPFTELD----NREFMLKPMNCP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 141 VMYPMFALWVRSHTDLPMRFYQVVNTFRYETK-HTRPLIRVREITTfKEAHTIhATASEAEEQVERAV----EIYKEFFN 215
Cdd:TIGR00418 266 GHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSgELHGLMRVRGFTQ-DDAHIF-CTEDQIKEEFKNQFrliqKVYSDFGF 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 216 SLGIPYLITRRPP--------WDK------------------------FPGSEYTVAF-DTLmpdGKTLQIGTVHnLGQT 262
Cdd:TIGR00418 344 SFDKYELSTRDPEdfigedelWEKaeaaleealkelgvpyeidpgrgaFYGPKIDFAFkDAL---GREWQCATVQ-LDFE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 263 FARTFEIKFETPEGDHEY---VHQTCYGLSDRVIASVIaihgDESGLCLPPDVAAHQVVIVPIifkkaAEEVMEACRELR 339
Cdd:TIGR00418 420 LPERFDLTYVDEDNEEKRpvmIHRAILGSIERFIAILL----EKYAGNFPLWLAPVQVVVIPV-----NERHLDYAKKVA 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 340 SRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLR 409
Cdd:TIGR00418 491 QKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEKLR 560
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
437-501 |
5.57e-18 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 77.94 E-value: 5.57e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1NJ2_A 437 LEEASRIVDEKrGIISFMWCGEEECGMDVEEKVRVDILGI---QEEGSGTCINCGREAPYRAYLARTY 501
Cdd:pfam09180 1 WEEFKEALEEK-GFVLAPWCGDEECEDKIKEETGATSRCIpfdQEEEGGKCIVCGKPAKKWVLFARSY 67
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
50-297 |
6.09e-18 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 83.39 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 50 EAEIIDQRYPVK---------GMHVWMPHGFMIRKNTLKILRRILDRDH-EEVLFPLLVPEdELAKEAIHVKGFEDEVYW 119
Cdd:cd00779 1 DAEIISHKLLLRagfirqtssGLYSWLPLGLRVLKKIENIIREEMNKIGaQEILMPILQPA-ELWKESGRWDAYGPELLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 120 VThgglSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYEtkhTRP---LIRVREItTFKEAHTIHATA 196
Cdd:cd00779 80 LK----DRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDE---IRPrfgLMRGREF-LMKDAYSFDIDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 197 SEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDkFPGS---EYTVAFDTLMPdgKTLQIGTVHNLGQTFARTFEIKFET 273
Cdd:cd00779 152 ESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGA-IGGSlshEFHVLSPLKIT--KGIEVGHIFQLGTKYSKALGATFLD 228
|
250 260
....*....|....*....|....*
1NJ2_A 274 PEGDHEYVHQTCYGLS-DRVIASVI 297
Cdd:cd00779 229 ENGKPKPLEMGCYGIGvSRLLAAII 253
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
73-289 |
2.41e-17 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 80.62 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 73 IRKNTLKILRRIL-DRDHEEVLFPLLVPEDELAKEAIHVKgfedevywVTHGGLSKLQRKLALRPTSETVMYPMFALWVR 151
Cdd:cd00768 1 IRSKIEQKLRRFMaELGFQEVETPIVEREPLLEKAGHEPK--------DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 152 shtDLPMRFYQVVNTFRYETKHtRPLIRVREITTfKEAHTIHATASEAEEqVERAVEIYKEFFNSLGIPYLITRR-PPWD 230
Cdd:cd00768 73 ---KLPLRLAEIGPAFRNEGGR-RGLRRVREFTQ-LEGEVFGEDGEEASE-FEELIELTEELLRALGIKLDIVFVeKTPG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1NJ2_A 231 KFPGSEYTVAFD--TLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGLS 289
Cdd:cd00768 147 EFSPGGAGPGFEieVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGFGLG 207
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
437-501 |
5.35e-17 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 75.30 E-value: 5.35e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1NJ2_A 437 LEEASRIVDEKrGIISFMWCGEEECGMDVEEKVRVDILGI---QEEGSGTCINCGREAPYRAYLARTY 501
Cdd:smart00946 1 LEEFKKALEEG-KFVLAPWCGDEECEEKIKEETGATIRCIpfdQDEEPGKCVVCGKPAKKWVLFARSY 67
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
36-414 |
2.45e-14 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 75.55 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 36 KMTEFSEWFHnILEEAEIIDQRYPVK------------GMHVWMPHGFMIRKNTLKILRRI-LDRDHEEVLFPLLVPEdE 102
Cdd:PRK12444 228 SQKELEEYLH-FVEEAAKRNHRKLGKelelfmfseeapGMPFYLPKGQIIRNELEAFLREIqKEYNYQEVRTPFMMNQ-E 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 103 LAKEAIHVKGFEDEVYW--VTHgglsklqRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYE-TKHTRPLIR 179
Cdd:PRK12444 306 LWERSGHWDHYKDNMYFseVDN-------KSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEfSGALNGLLR 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 180 VReitTF--KEAHtIHATASEAEEQVERAVEIYKEFFNSLGIPYLI--TRRPP--------WDKFPGSEYTVAFDTLMP- 246
Cdd:PRK12444 379 VR---TFcqDDAH-LFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVelSTRPEdsmgddelWEQAEASLENVLQSLNYKy 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 247 -----DG----------------KTLQIGTVhnlgqtfartfEIKFETPEG-DHEYV------------HQTCYGLSDRV 292
Cdd:PRK12444 455 rlnegDGafygpkidfhikdalnRSHQCGTI-----------QLDFQMPEKfDLNYIdeknekrrpvviHRAVLGSLDRF 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 293 IASVIaihgDESGLCLPPDVAAHQVVIVPIifkkaAEEV-MEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVP 371
Cdd:PRK12444 524 LAILI----EHFGGAFPAWLAPVQVKVIPV-----SNAVhVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIP 594
|
410 420 430 440
....*....|....*....|....*....|....*....|...
1NJ2_A 372 LRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELMKD 414
Cdd:PRK12444 595 YVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIKN 637
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
316-411 |
6.66e-12 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 61.45 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 316 QVVIVPIifKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGE 395
Cdd:cd00861 3 DVVIIPM--NMKDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|....*.
1NJ2_A 396 KVTADlqgIEETLREL 411
Cdd:cd00861 81 KEEIS---IDELLEFL 93
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
250-417 |
1.61e-10 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 63.35 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 250 TLQIgTVHNlgqtfARTFEIKFETPEGDHEY---VHQTCYGLSDRVIASV---IAIHGDESGL-CLPPDVAAHQVVIVPI 322
Cdd:PRK03991 434 TVQI-DVEN-----AERFGIKYVDENGEEKYpiiLHCSPTGSIERVIYALlekAAKEEEEGKVpMLPTWLSPTQVRVIPV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 323 ifkkaAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVtadlq 402
Cdd:PRK03991 508 -----SERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKV----- 577
|
170
....*....|....*
1NJ2_A 403 giEETLRELMKDILE 417
Cdd:PRK03991 578 --EMTLEELIERIKE 590
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
315-395 |
2.12e-09 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 54.43 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 315 HQVVIVPIifkkaAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTG 394
Cdd:cd00860 2 VQVVVIPV-----TDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
.
1NJ2_A 395 E 395
Cdd:cd00860 77 D 77
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
62-410 |
2.36e-09 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 59.66 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 62 GMHVWMPHGFMIRkNTLK--ILRRILDRDHEEVLFPLLVpedelakeaihvkgfeDEVYWVTHGGLSKLQ---------- 129
Cdd:COG0441 262 GLPFWHPKGAIIR-RELEdyIREKHRKAGYQEVKTPHIL----------------DRELWETSGHWDHYRenmfptesdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 130 RKLALRPtsetvMY-PM----FALWVRSHTDLPMRFYQVVNTFRYEtkhtrP------LIRVREITTfKEAHtIHATASE 198
Cdd:COG0441 325 EEYALKP-----MNcPGhiliYKSGLRSYRDLPLRLAEFGTVHRYE-----PsgalhgLMRVRGFTQ-DDAH-IFCTPDQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 199 AEEQVERAVEIYKEFFNSLGIP----YLITRRppwDKFPGS--------------------EYTV-----AF-------- 241
Cdd:COG0441 393 IEDEIKKVIDLVLEVYKDFGFEdyyvKLSTRP---EKRIGSdeiwdkaeaalrealeelglEYVInpgegAFygpkidfq 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 242 --DTLmpdGKTLQIGTVH---NLGQTFartfeikfetpegDHEYV------------HQTCYGLSDRVIASVIAIH-GDe 303
Cdd:COG0441 470 lkDAI---GREWQCGTIQldfNLPERF-------------DLTYVgedgekhrpvmiHRAILGSIERFIGILIEHYaGA- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 304 sglcLPPDVAAHQVVIVPIifkkaAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEK 383
Cdd:COG0441 533 ----FPLWLAPVQVVVLPI-----SDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVEN 603
|
410 420
....*....|....*....|....*..
1NJ2_A 384 GAAVISRRDTGEKVTADLQGIEETLRE 410
Cdd:COG0441 604 GTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
31-312 |
3.71e-09 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 57.95 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 31 RYHGEKmTEFSEW---FHNILEEAEIIDQR----------YPVKGMHVWMPHG---FMIRKNTlkilrrilDRDHEEVLF 94
Cdd:cd00770 6 RRWGEP-RVFDFKpkdHVELGEKLDILDFErgakvsgsrfYYLKGDGALLERAlinFALDFLT--------KRGFTPVIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 95 PLLVPEDELAKeAIHVKGFEDEVYWVTHGGLsklqrklALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYET--- 171
Cdd:cd00770 77 PFLVRKEVMEG-TGQLPKFDEQLYKVEGEDL-------YLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAgsa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 172 -KHTRPLIRVREITtfKEAHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYTVAFDTLMP-DGK 249
Cdd:cd00770 149 gRDTRGLFRVHQFE--KVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPgQGK 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1NJ2_A 250 TLQIGTVHNLGQTFARTFEIKF-ETPEGDHEYVHQ-TCYGL-SDRVIASVIAIHGDESGLCLPPDV 312
Cdd:cd00770 227 YREISSCSNCTDFQARRLNIRYrDKKDGKKQYVHTlNGTALaTPRTIVAILENYQTEDGSVVIPEV 292
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
306-413 |
3.77e-07 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 48.71 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 306 LCLPPDVAAHQVVIVPIIFKkaaEEVMEACRELRSRLEAAGFRVHLDDRD-IraGRKYyeweMR----GVPLRVEIGPRD 380
Cdd:cd00858 18 LRLPPALAPIKVAVLPLVKR---DELVEIAKEISEELRELGFSVKYDDSGsI--GRRY----ARqdeiGTPFCVTVDFDT 88
|
90 100 110
....*....|....*....|....*....|...
1NJ2_A 381 LEKGAAVISRRDTGEKVTADLQGIEETLRELMK 413
Cdd:cd00858 89 LEDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
62-236 |
1.24e-05 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 47.16 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 62 GMHVWMPHGFMIRKNTLKILRRIL-DRDHEEVLFPLLVPEDELAKEAiHVKGFEDEVYWVTHGGlsklqRKLALRPtset 140
Cdd:cd00771 21 GLPFWLPKGAIIRNELEDFLRELQrKRGYQEVETPIIYNKELWETSG-HWDHYRENMFPFEEED-----EEYGLKP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 141 vM-----YPMFALWVRSHTDLPMRFYQVVNTFRYETK---HTrpLIRVREITTFkEAHTIhATASEAEEQVERAVEIYKE 212
Cdd:cd00771 91 -MncpghCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSgalHG--LTRVRGFTQD-DAHIF-CTPDQIKEEIKGVLDLIKE 165
|
170 180
....*....|....*....|....*...
1NJ2_A 213 FFNSLGI----PYLITRRppwDKFPGSE 236
Cdd:cd00771 166 VYSDFGFfdykVELSTRP---EKFIGSD 190
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
20-395 |
8.72e-05 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 45.27 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 20 HMQKPIKKDPNRYHGEKMTEFSewfhnILEEAEiidqrypvKGMHVWMPHGFMIRKNTLKILRRILDRDHEEVLFPLLVP 99
Cdd:PLN02837 209 HFKEEAKRRDHRRLGQDLDLFS-----IQDDAG--------GGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 100 EDELAKEAIHVKGFEDEVYwvthgGLSKLQRKL-ALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHT-RPL 177
Cdd:PLN02837 276 KADLWKTSGHLDFYKENMY-----DQMDIEDELyQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSlHGL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 178 IRVREITTfKEAHtIHATASEAEEQVERAVEIYKEFFNSLGIPYL---ITRRPP--------WDKF----------PGSE 236
Cdd:PLN02837 351 FRVRGFTQ-DDAH-IFCLEDQIKDEIRGVLDLTEEILKQFGFSKYeinLSTRPEksvgsddiWEKAttalrdalddKGWE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 237 YTV-----AF-----DTLMPD--GKTLQIGTVH---NLGQTFARTFeIKFETPEGDHEYVHQTCYGLSDRVIASVIAIHG 301
Cdd:PLN02837 429 YKVdegggAFygpkiDLKIEDalGRKWQCSTIQvdfNLPERFDITY-VDSNSEKKRPIMIHRAILGSLERFFGVLIEHYA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NJ2_A 302 DESGLCLPPDvaahQVVIVPIifkkaAEEVMEACRELRSRLEAAGFRVHLDDRDiRAGRKYYEWEMRGVPLRVEIGPRDL 381
Cdd:PLN02837 508 GDFPLWLAPV----QARVLPV-----TDNELEYCKEVVAKLKAKGIRAEVCHGE-RLPKLIRNAETQKIPLMAVVGPKEV 577
|
410
....*....|....
1NJ2_A 382 EKGAAVISRRDTGE 395
Cdd:PLN02837 578 ETRTLTVRSRHGGE 591
|
|
| TIR_2 |
pfam13676 |
TIR domain; This is a family of Toll-like receptors. |
336-370 |
5.29e-03 |
|
TIR domain; This is a family of Toll-like receptors.
Pssm-ID: 463954 [Multi-domain] Cd Length: 118 Bit Score: 36.91 E-value: 5.29e-03
10 20 30
....*....|....*....|....*....|....*
1NJ2_A 336 RELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGV 370
Cdd:pfam13676 14 EWLADALEAAGYRVWLDRWDIRPGDDWVEEIEEAI 48
|
|
| |
