|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
89-470 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 677.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 89 VDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 168
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 169 SSEAMHLGHLVPFIFTKWLQDVFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLEYMGQS 248
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 249 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 328
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 329 PRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGSDTVEEHRQFGGNCEVDVSFMYLT 408
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62460630 409 FFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEFMAPRQL 470
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
158-467 |
1.64e-124 |
|
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: 365.50 E-value: 1.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 158 KPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQdVFDVPLVIQMSDDEKYLWKDlTLEQAYSYTVEN-AKDIIACGFDVNKT 236
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 237 FIFSDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAVQAAPSFSNSFPkifrdrtdiqcLI 311
Cdd:TIGR00233 78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 312 PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKSKVNKHAFSGG 384
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNKkfknffPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 385 SDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEF 464
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
...
gi 62460630 465 MAP 467
Cdd:TIGR00233 303 LEP 305
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
161-445 |
2.75e-116 |
|
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
Pssm-ID: 173903 [Multi-domain] Cd Length: 280 Bit Score: 342.64 E-value: 2.75e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 161 YLYTGRGPSSeAMHLGHLVP-FIFTKWLQDVfDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIF 239
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 240 SDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAVQAAPSFSNSFpkifrdrtdiqCLIPC 313
Cdd:cd00806 79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 314 AIDQDPYFRMTRDVAPRIGH------PKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGS 385
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNKlygeifPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 386 DtveEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPL 445
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
163-455 |
1.37e-25 |
|
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: 106.67 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 163 YTGRGPSSEaMHLGHLVPFIFtKW--LQDvfDVPLVIQMSDDEKylwkdLTL----EQAYSYTVENAKDIIACGFDVNKT 236
Cdd:COG0180 7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTpqdpEELRENTREVAADYLAAGLDPEKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 237 FIF--SD-------------------LEYMGQspgfYKNvvKIQKHVTFNQVKGIFGFtdsdcigkisfPAVQAApsfsn 295
Cdd:COG0180 78 TIFvqSDvpehaelawllscltplgeLERMPQ----FKD--KSAKNGKENVNAGLLTY-----------PVLMAA----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 296 sfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQG--AQTKMSASDpNS 361
Cdd:COG0180 136 ----------DI--LLykadlvPVGEDQKQHLELTRDIARRFNHrygevfPEPEALIPEEGARIPGldGRKKMSKSY-GN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 362 SIFLTDTAKQIKSKVNKhAFsggSDTVEEHRQFGGNCEVDVSFMYLTFFLeDDDSLEQIRKDYTSGAMLTGELKKTLIDV 441
Cdd:COG0180 203 TINLLDDPKEIRKKIKS-AV---TDSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGIGYGDLKKALAEA 277
|
330
....*....|....
gi 62460630 442 LQPLIAEHQARRKA 455
Cdd:COG0180 278 VVEFLAPIRERRAE 291
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
16-65 |
3.90e-22 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 89.22 E-value: 3.90e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62460630 16 LFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAG 65
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
16-68 |
9.43e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.94 E-value: 9.43e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62460630 16 LFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAGCPP 68
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
155-443 |
2.19e-20 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 91.18 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 155 ENKKPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQDVFDVPLVI----------QMSDDEKylwkdlTLEQAYSYTVENAK 224
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhaiigdPSKSPER------KLLSRETVLENAIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 225 DIIACGFDVNKTFIF--------SDLEYMGQSPGfykNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAApsfsns 296
Cdd:pfam00579 74 AQLACGLDPEKAEIVnnsdwlehLELAWLLRDLG---KHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 297 fpKIFRDRTDIQcliPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKS 374
Cdd:pfam00579 145 --DILLLKADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62460630 375 KVNKhAFSgGSDtVEEHRQFGGNCEVDVS-FMYLTFFLEDDD--SLEQIRKDYTSGAMLTGELKKTLIDVLQ 443
Cdd:pfam00579 220 KIQK-AYT-DPD-REVRKDLKLFTFLSNEeIEILEAELGKSPyrEAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
17-71 |
4.82e-20 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 83.55 E-value: 4.82e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62460630 17 FNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAGCPPGNS 71
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
15-75 |
1.85e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 53.60 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62460630 15 ELFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNyKTAMGEEYKAGCPPGNSTAGS 75
Cdd:PLN02734 11 EKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGGDGAAS 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
89-470 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 677.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 89 VDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 168
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 169 SSEAMHLGHLVPFIFTKWLQDVFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLEYMGQS 248
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 249 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 328
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 329 PRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGSDTVEEHRQFGGNCEVDVSFMYLT 408
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62460630 409 FFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEFMAPRQL 470
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
85-464 |
3.44e-137 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 399.24 E-value: 3.44e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 85 SEDF-VDPWTVRTSsakgIDYDKLIVQFGSSKIDKELINrIERatgqrPHRFLRRGIFFSHRDMNQILDAYENKKPFYLY 163
Cdd:PRK12285 1 EDEFmVTPWEVSGI----VDYDKLFEEFGIEPFTEVLPE-LPE-----PHPLMRRGIIFGHRDYDKILEAYRNGKPFAVY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 164 TGRGPSSEaMHLGHLVPFIFTKWLQDvFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLE 243
Cdd:PRK12285 71 TGFMPSGP-MHIGHKMVFDELKWHQE-FGANVYIPIADDEAYAARGLSWEETREWAYEYILDLIALGFDPDKTEIYFQSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 244 YMgqspGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFsnsFPKIFRDRTdiQCLIPCAIDQDPYFRM 323
Cdd:PRK12285 149 NI----KVYDLAFELAKKVNFSELKAIYGFTGETNIGHIFYPATQAADIL---HPQLEEGPK--PTLVPVGIDQDPHIRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 324 TRDVAPRI----GHPKPALLHSTFFPALQGaqTKMSASDPNSSIFLTDTAKQIKSKVnKHAFSGGSDTVEEHRQFGGNCE 399
Cdd:PRK12285 220 TRDIAERLhggyGFIKPSSTYHKFMPGLTG--GKMSSSKPESAIYLTDDPETVKKKI-MKALTGGRATLEEQRKLGGEPD 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62460630 400 VDVSFMYLTFFLEDDDS-LEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVtEETVKEF 464
Cdd:PRK12285 297 ECVVYELLLYHLEEDDKeLKEIYEECRSGELLCGECKKEAAEKIAEFLKEHQEKREEA-REILEKY 361
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
158-467 |
1.64e-124 |
|
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: 365.50 E-value: 1.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 158 KPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQdVFDVPLVIQMSDDEKYLWKDlTLEQAYSYTVEN-AKDIIACGFDVNKT 236
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 237 FIFSDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAVQAAPSFSNSFPkifrdrtdiqcLI 311
Cdd:TIGR00233 78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 312 PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKSKVNKHAFSGG 384
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNKkfknffPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 385 SDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEF 464
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
...
gi 62460630 465 MAP 467
Cdd:TIGR00233 303 LEP 305
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
161-445 |
2.75e-116 |
|
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
Pssm-ID: 173903 [Multi-domain] Cd Length: 280 Bit Score: 342.64 E-value: 2.75e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 161 YLYTGRGPSSeAMHLGHLVP-FIFTKWLQDVfDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIF 239
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 240 SDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAVQAAPSFSNSFpkifrdrtdiqCLIPC 313
Cdd:cd00806 79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 314 AIDQDPYFRMTRDVAPRIGH------PKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGS 385
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNKlygeifPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 386 DtveEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPL 445
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
163-455 |
1.37e-25 |
|
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: 106.67 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 163 YTGRGPSSEaMHLGHLVPFIFtKW--LQDvfDVPLVIQMSDDEKylwkdLTL----EQAYSYTVENAKDIIACGFDVNKT 236
Cdd:COG0180 7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTpqdpEELRENTREVAADYLAAGLDPEKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 237 FIF--SD-------------------LEYMGQspgfYKNvvKIQKHVTFNQVKGIFGFtdsdcigkisfPAVQAApsfsn 295
Cdd:COG0180 78 TIFvqSDvpehaelawllscltplgeLERMPQ----FKD--KSAKNGKENVNAGLLTY-----------PVLMAA----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 296 sfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQG--AQTKMSASDpNS 361
Cdd:COG0180 136 ----------DI--LLykadlvPVGEDQKQHLELTRDIARRFNHrygevfPEPEALIPEEGARIPGldGRKKMSKSY-GN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 362 SIFLTDTAKQIKSKVNKhAFsggSDTVEEHRQFGGNCEVDVSFMYLTFFLeDDDSLEQIRKDYTSGAMLTGELKKTLIDV 441
Cdd:COG0180 203 TINLLDDPKEIRKKIKS-AV---TDSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGIGYGDLKKALAEA 277
|
330
....*....|....
gi 62460630 442 LQPLIAEHQARRKA 455
Cdd:COG0180 278 VVEFLAPIRERRAE 291
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
163-445 |
9.77e-24 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 101.48 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 163 YTGRGPSSEaMHLGHLVpfiftkW------LQDV-FDVplVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNK 235
Cdd:PRK08560 34 YIGFEPSGK-IHLGHLL------TmnkladLQKAgFKV--TVLLADWHAYLNDKGDLEEIRKVAEYNKKVFEALGLDPDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 236 T-FIF-----SDLEYMGqspgfykNVVKIQKHVTFNQVK---GIFG--FTDSDcIGKISFPAVQAApsfsnsfpKIFRDR 304
Cdd:PRK08560 105 TeFVLgsefqLDKEYWL-------LVLKLAKNTTLARARrsmTIMGrrMEEPD-VSKLVYPLMQVA--------DIFYLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 305 TDIqclipcA---IDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNK--- 378
Cdd:PRK08560 169 VDI------AvggMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGIKMSKSKPGSAIFVHDSPEEIRRKIKKayc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 379 ----------------HAFSG-GSDTVEEHRQFGGNCEVdvsfmyltffleddDSLEQIRKDYTSGAMLTGELKKT---- 437
Cdd:PRK08560 243 ppgevegnpvleiakyHIFPRyDPFVIERPEKYGGDLEY--------------ESYEELERDYAEGKLHPMDLKNAvaey 308
|
....*...
gi 62460630 438 LIDVLQPL 445
Cdd:PRK08560 309 LIEILEPV 316
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
16-65 |
3.90e-22 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 89.22 E-value: 3.90e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62460630 16 LFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAG 65
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
16-68 |
9.43e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.94 E-value: 9.43e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62460630 16 LFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAGCPP 68
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
155-443 |
2.19e-20 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 91.18 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 155 ENKKPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQDVFDVPLVI----------QMSDDEKylwkdlTLEQAYSYTVENAK 224
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhaiigdPSKSPER------KLLSRETVLENAIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 225 DIIACGFDVNKTFIF--------SDLEYMGQSPGfykNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAApsfsns 296
Cdd:pfam00579 74 AQLACGLDPEKAEIVnnsdwlehLELAWLLRDLG---KHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 297 fpKIFRDRTDIQcliPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKS 374
Cdd:pfam00579 145 --DILLLKADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62460630 375 KVNKhAFSgGSDtVEEHRQFGGNCEVDVS-FMYLTFFLEDDD--SLEQIRKDYTSGAMLTGELKKTLIDVLQ 443
Cdd:pfam00579 220 KIQK-AYT-DPD-REVRKDLKLFTFLSNEeIEILEAELGKSPyrEAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
17-71 |
4.82e-20 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 83.55 E-value: 4.82e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62460630 17 FNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMGEEYKAGCPPGNS 71
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
157-454 |
2.70e-16 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 79.90 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 157 KKPFYLyTGRGPSSeAMHLGHLV--------------PFIF---TKWLQDVFDVPlviqmsddekylwkdltlEQAYSYT 219
Cdd:PRK12282 1 TKPIIL-TGDRPTG-KLHLGHYVgslknrvalqneheQFVLiadQQALTDNAKNP------------------EKIRRNI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 220 VENAKDIIACGFDVNKTFIFSdleymgQS--PG------FYKNVV-------------KIQKHvtfnqvkgifGFTDSDC 278
Cdd:PRK12282 61 LEVALDYLAVGIDPAKSTIFI------QSqiPElaeltmYYMNLVtvarlernptvktEIAQK----------GFGRSIP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 279 IGKISFPAVQAApsfsnsfpkifrdrtDIQC----LIPCAIDQDPYFRMTRDVAPRIGH---------PKPALLHSTFFP 345
Cdd:PRK12282 125 AGFLTYPVSQAA---------------DITAfkatLVPVGDDQLPMIEQTREIVRRFNSlygtdvlvePEALLPEAGRLP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 346 ALQGaQTKMSASDPNSsIFLTDTAKQIKSKVNKHAFSGGSDTVEEHRQFGGNcevdVSFMYLTFFLEDDDSLEQIRKDYT 425
Cdd:PRK12282 190 GLDG-KAKMSKSLGNA-IYLSDDADTIKKKVMSMYTDPNHIRVEDPGKVEGN----VVFTYLDAFDPDKAEVAELKAHYQ 263
|
330 340
....*....|....*....|....*....
gi 62460630 426 SGAMLTGELKKTLIDVLQPLIAEHQARRK 454
Cdd:PRK12282 264 RGGLGDVKCKRYLEEVLQELLAPIRERRA 292
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
17-57 |
3.15e-15 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 69.49 E-value: 3.15e-15
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 62460630 17 FNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTA 57
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEA 41
|
|
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
218-454 |
3.21e-13 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 70.50 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 218 YTVENAKDIIACGFDVNKTFIF--SD-------------------LEYMGQspgfYKNvvKIQKHvtfnqvkgifgfTDS 276
Cdd:PRK00927 57 NTRELAADYLACGIDPEKSTIFvqSHvpehaelawilncitplgeLERMTQ----FKD--KSAKQ------------KEN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 277 DCIGKISFPAVQAApsfsnsfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGHpkpalLHSTFFPA---- 346
Cdd:PRK00927 119 VSAGLFTYPVLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFNN-----LYGEVFPVpepl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 347 ----------LQGAQTKMSASDPN--SSIFLTDTAKQIKSKVNKhAFSgGSDTVEEHRqFG--GNCEVDVSFMYLTFFLe 412
Cdd:PRK00927 177 ipkvgarvmgLDGPTKKMSKSDPNdnNTINLLDDPKTIAKKIKK-AVT-DSERLREIR-YDlpNKPEVSNLLTIYSALS- 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 62460630 413 dDDSLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRK 454
Cdd:PRK00927 253 -GESIEELEAEYEAGGKGYGDFKKDLAEAVVEFLAPIRERYE 293
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
228-468 |
1.94e-12 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 68.56 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 228 ACGFDV-NKTFIFSDLEYMGQSPGFYKNVVKIQKHVTFNQVK---GIFGFTDSD--CIGKISFPAVQAApsfsnsfpKIF 301
Cdd:PTZ00126 136 AAGMDMdNVRFLWASEEINKNPNDYWLRVMDIARSFNITRIKrcsQIMGRSEGDeqPCAQILYPCMQCA--------DIF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 302 RDRTDIQCLipcAIDQDPYFRMTRDVA--PRIGHpKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVnKH 379
Cdd:PTZ00126 208 YLKADICQL---GMDQRKVNMLAREYCdkKKIKK-KPIILSHHMLPGLLEGQEKMSKSDPNSAIFMEDSEEDVNRKI-KK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 380 AF---------------------SGGSDTVEEHRQFGGncevDVSFmyltffleddDSLEQIRKDYTSGAMLTGELKKTL 438
Cdd:PTZ00126 283 AYcppgviegnpilayfksivfpAFNSFTVLRKEKNGG----DVTY----------TTYEELEKDYLSGALHPGDLKPAL 348
|
250 260 270
....*....|....*....|....*....|....*.
gi 62460630 439 IDVLQPLIA------EHQARRKAVTEEtVKEFMAPR 468
Cdd:PTZ00126 349 AKYLNLMLQpvrdhfQNNPEAKSLLSE-VKSYKVTK 383
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
15-75 |
1.85e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 53.60 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62460630 15 ELFNSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNyKTAMGEEYKAGCPPGNSTAGS 75
Cdd:PLN02734 11 EKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGGDGAAS 70
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
162-438 |
2.72e-07 |
|
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: 51.84 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 162 LYTGRGPSSEAMHLGHLVPFIFTKWLQDV-FDVPLVI----QMSDD---EKYLWKDLTLEQ------AYSYTVENAKDII 227
Cdd:cd00805 3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAgHEVIVLIgdatAMIGDpsgKSEERKLLDLELirenakYYKKQLKAILDFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 228 acgfDVNKTFIFSDLEYmgQSPGFYKNVVKIQKHVTFNQ------VKGIFGFTDSDCIGKISFPAVQAapsfsnsfpkif 301
Cdd:cd00805 83 ----PPEKAKFVNNSDW--LLSLYTLDFLRLGKHFTVNRmlrrdaVKVRLEEEEGISFSEFIYPLLQA------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 302 rdrTDIQCLIPCA----IDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAqtKMSASDPNSS-IFLTDTAKQIKSKV 376
Cdd:cd00805 145 ---YDFVYLDVDLqlggSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG--KMSKSEGNAIwDPVLDSPYDVYQKI 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62460630 377 NKhAFsggsdtveehrqfggnCEVDVSFM-YLTFFleDDDSLEQIRKDYTSGaMLTGELKKTL 438
Cdd:cd00805 220 RN-AF----------------DPDVLEFLkLFTFL--DYEEIEELEEEHAEG-PLPRDAKKAL 262
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
228-381 |
3.34e-07 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 52.98 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 228 ACGFDVNKT-FIFSDLEYMGQSPGFYKNVVKIQKHVTFNQVKG---IFGFTDSDCIG-KISFPAVQAApsfsnsfpKIFR 302
Cdd:PTZ00348 102 AAGMDMDKVlFLWSSEEITNHANTYWRTVLDIGRQNTIARIKKcctIMGKTEGTLTAaQVLYPLMQCA--------DIFF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 303 DRTDIQCLipcAIDQDPYFRMTRDVAPRIGHP-KPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVnKHAF 381
Cdd:PTZ00348 174 LKADICQL---GLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKI-RQAY 249
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
20-59 |
3.25e-05 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 40.92 E-value: 3.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 62460630 20 IAAQGELVRSLKAGNAPKDEIESAVKMLLSLKMNYKTAMG 59
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
157-397 |
7.36e-05 |
|
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: 45.08 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 157 KKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQDV-FDVPLVI-----------QMSDDEKYLWKDLTLEQAYSYtvenaK 224
Cdd:TIGR00234 29 ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAgHEVIVLLgdftaligdptGKSEVRKILTREEVQENAENI-----K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 225 DIIACGFDVNKTFIFSDLEYMGqSPGFYKNVVKIQKHVTFNQ-----------VKGIFgftdsdcIGKISFPAVQAapsf 293
Cdd:TIGR00234 104 KQIARFLDFEKAKFVYNSEWLL-KLNYTDFIRLLGKIFTVNRmlrrdafssrfEENIS-------LHEFIYPLLQA---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460630 294 snsfpkifrdrTDIQCL-IPCAI---DQDPYFRMTRDVAPRIGhpkPALLHSTFFPALQGA-QTKMSAS-------DPNS 361
Cdd:TIGR00234 172 -----------YDFVYLnVDLQLggsDQWFNIRKGRDLARENL---PSLQFGLTVPLLTPAdGEKMGKSlggavslDEGK 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 62460630 362 S---IFLTDTAKQIKSKVNKHAFSGGSDTVEEHRQFGGN 397
Cdd:TIGR00234 238 YdfyQKVINTPDELVKKYLKLFTFLGLEEIEQLVELKGP 276
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
20-51 |
2.01e-04 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 38.99 E-value: 2.01e-04
10 20 30
....*....|....*....|....*....|..
gi 62460630 20 IAAQGELVRSLKAGNAPKDEIESAVKMLLSLK 51
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELK 38
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
138-189 |
1.74e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 40.65 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62460630 138 RGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQD 189
Cdd:PRK13354 12 RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQD 63
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
12-51 |
4.14e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 35.54 E-value: 4.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 62460630 12 SPLELfnSIAAQGELVRSLKAGNAPKDEIESAVKMLLSLK 51
Cdd:cd00935 2 APLRA--AVKEQGDLVRKLKEEGAPDVDIKKAVAELKARK 39
|
|
| |
