|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
85-466 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 672.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 85 VDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGP 164
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 165 SSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGms 244
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVG-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 245 SGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 324
Cdd:PLN02486 161 GAFYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 325 PRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLT 404
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47419914 405 FFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKL 466
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
154-471 |
8.65e-131 |
|
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: 381.29 E-value: 8.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 154 KPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQdVFNVPLVIQMTDDEKYLWKDlTLDQAYSYAVEN-AKDIIACGFDINKT 232
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 233 FIFSDLDYMGmssgFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAIQAAPSFSNSFPqifrdrtdiqcLI 307
Cdd:TIGR00233 78 FIFLQSDYPE----HYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 308 PCAIDQDPYFRMTRDVAPRIG------YPKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKTKVNKHAFSGG 380
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNkkfknfFPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 381 RDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEF 460
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
330
....*....|..
gi 47419914 461 MTP-RKLSFDFQ 471
Cdd:TIGR00233 303 LEPgAKKARETA 314
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
157-441 |
8.33e-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: 341.49 E-value: 8.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 157 YLYTGRGPSSeAMHVGHLIP-FIFTKWLQDVfNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIF 235
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 236 SDLDYMGmssgFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAIQAAPSFSNSFpqifrdrtdiqCLIPC 309
Cdd:cd00806 79 FQSDVPE----HYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 310 AIDQDPYFRMTRDVAPRIG------YPKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGR 381
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNklygeiFPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 382 DtieEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPL 441
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
159-459 |
6.81e-24 |
|
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: 102.05 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 159 YTGRGPSSEaMHVGHLIPFIFtKW--LQDvfNVPLVIQMTDDEKylwkdLTLDQ----AYSYAVENAKDIIACGFDINKT 232
Cdd:COG0180 7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTPQdpeeLRENTREVAADYLAAGLDPEKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 233 FIF--SDLD-------YMGMSSGF--------YKNvvKIQKHVTFNQVKGIFGftdsdcigkisFPAIQAApsfsnsfpq 295
Cdd:COG0180 78 TIFvqSDVPehaelawLLSCLTPLgelermpqFKD--KSAKNGKENVNAGLLT-----------YPVLMAA--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 296 ifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRI------GYPKPALLHSTFFPALQG--AQTKMSASDpNSSIFL 361
Cdd:COG0180 136 ------DI--LLykadlvPVGEDQKQHLELTRDIARRFnhrygeVFPEPEALIPEEGARIPGldGRKKMSKSY-GNTINL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 362 TDTAKQIKTKVNKhAFSggrDTIEEHRQFGGNCDVDVSFMYLTFFLeDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPL 441
Cdd:COG0180 207 LDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGIGYGDLKKALAEAVVEF 281
|
330 340
....*....|....*....|....
gi 47419914 442 IAEHQARRKEVT------DEIVKE 459
Cdd:COG0180 282 LAPIRERRAELLadpaelDEILAE 305
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
151-439 |
5.11e-21 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 93.11 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 151 ENKKPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDDEKYLwKDLTLDQAYSYAVENAKDIIAC 225
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhAIIGDPSKS-PERKLLSRETVLENAIKAQLAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 226 GFDINKTFIF--SD----LDYMGMSSGFyKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAApsfsnsfpQIFRD 299
Cdd:pfam00579 79 GLDPEKAEIVnnSDwlehLELAWLLRDL-GKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY--------DILLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 300 RTDIQcliPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKTKVNKhAF 377
Cdd:pfam00579 150 KADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYKKIQK-AY 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47419914 378 SGGRDtiEEHRQFGGNCDVDVS-FMYLTFFLEDDDK--LEQIRKDYTSGAMLTGELKKALIEVLQ 439
Cdd:pfam00579 226 TDPDR--EVRKDLKLFTFLSNEeIEILEAELGKSPYreAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
12-61 |
6.97e-21 |
|
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: 85.36 E-value: 6.97e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 47419914 12 LFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKAD 61
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
12-64 |
1.18e-20 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 84.85 E-value: 1.18e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 47419914 12 LFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPP 64
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
13-68 |
2.66e-18 |
|
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: 78.54 E-value: 2.66e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 47419914 13 FNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPA 68
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
8-68 |
1.40e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 50.90 E-value: 1.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47419914 8 SLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSyKAAAGEDYKADCPPGNPA 68
Cdd:PLN02734 8 ALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGGDG 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
85-466 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 672.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 85 VDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGP 164
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 165 SSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGms 244
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVG-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 245 SGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 324
Cdd:PLN02486 161 GAFYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 325 PRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLT 404
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47419914 405 FFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKL 466
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
81-460 |
1.70e-142 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 412.72 E-value: 1.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 81 EEDF-VDPWTVQTSsakgIDYDKLIVRFGSSKIDKELINrIERatgqrPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLY 159
Cdd:PRK12285 1 EDEFmVTPWEVSGI----VDYDKLFEEFGIEPFTEVLPE-LPE-----PHPLMRRGIIFGHRDYDKILEAYRNGKPFAVY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 160 TGRGPSSEaMHVGHLIPFIFTKWLQDvFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLD 239
Cdd:PRK12285 71 TGFMPSGP-MHIGHKMVFDELKWHQE-FGANVYIPIADDEAYAARGLSWEETREWAYEYILDLIALGFDPDKTEIYFQSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 240 YMGMssgfYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFsnsFPQIFRDRTdiQCLIPCAIDQDPYFRM 319
Cdd:PRK12285 149 NIKV----YDLAFELAKKVNFSELKAIYGFTGETNIGHIFYPATQAADIL---HPQLEEGPK--PTLVPVGIDQDPHIRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 320 TRDVAPRI----GYPKPALLHSTFFPALQGaqTKMSASDPNSSIFLTDTAKQIKTKVnKHAFSGGRDTIEEHRQFGGNCD 395
Cdd:PRK12285 220 TRDIAERLhggyGFIKPSSTYHKFMPGLTG--GKMSSSKPESAIYLTDDPETVKKKI-MKALTGGRATLEEQRKLGGEPD 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47419914 396 VDVSFMYLTFFLEDDDK-LEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVtDEIVKEF 460
Cdd:PRK12285 297 ECVVYELLLYHLEEDDKeLKEIYEECRSGELLCGECKKEAAEKIAEFLKEHQEKREEA-REILEKY 361
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
154-471 |
8.65e-131 |
|
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: 381.29 E-value: 8.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 154 KPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQdVFNVPLVIQMTDDEKYLWKDlTLDQAYSYAVEN-AKDIIACGFDINKT 232
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 233 FIFSDLDYMGmssgFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAIQAAPSFSNSFPqifrdrtdiqcLI 307
Cdd:TIGR00233 78 FIFLQSDYPE----HYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 308 PCAIDQDPYFRMTRDVAPRIG------YPKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKTKVNKHAFSGG 380
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNkkfknfFPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 381 RDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEF 460
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
330
....*....|..
gi 47419914 461 MTP-RKLSFDFQ 471
Cdd:TIGR00233 303 LEPgAKKARETA 314
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
157-441 |
8.33e-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: 341.49 E-value: 8.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 157 YLYTGRGPSSeAMHVGHLIP-FIFTKWLQDVfNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIF 235
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 236 SDLDYMGmssgFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAIQAAPSFSNSFpqifrdrtdiqCLIPC 309
Cdd:cd00806 79 FQSDVPE----HYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 310 AIDQDPYFRMTRDVAPRIG------YPKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGR 381
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNklygeiFPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 382 DtieEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPL 441
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
159-459 |
6.81e-24 |
|
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: 102.05 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 159 YTGRGPSSEaMHVGHLIPFIFtKW--LQDvfNVPLVIQMTDDEKylwkdLTLDQ----AYSYAVENAKDIIACGFDINKT 232
Cdd:COG0180 7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTPQdpeeLRENTREVAADYLAAGLDPEKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 233 FIF--SDLD-------YMGMSSGF--------YKNvvKIQKHVTFNQVKGIFGftdsdcigkisFPAIQAApsfsnsfpq 295
Cdd:COG0180 78 TIFvqSDVPehaelawLLSCLTPLgelermpqFKD--KSAKNGKENVNAGLLT-----------YPVLMAA--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 296 ifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRI------GYPKPALLHSTFFPALQG--AQTKMSASDpNSSIFL 361
Cdd:COG0180 136 ------DI--LLykadlvPVGEDQKQHLELTRDIARRFnhrygeVFPEPEALIPEEGARIPGldGRKKMSKSY-GNTINL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 362 TDTAKQIKTKVNKhAFSggrDTIEEHRQFGGNCDVDVSFMYLTFFLeDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPL 441
Cdd:COG0180 207 LDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGIGYGDLKKALAEAVVEF 281
|
330 340
....*....|....*....|....
gi 47419914 442 IAEHQARRKEVT------DEIVKE 459
Cdd:COG0180 282 LAPIRERRAELLadpaelDEILAE 305
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
159-441 |
1.01e-22 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 98.40 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 159 YTGRGPSSEaMHVGHLIpfiftkW------LQDV-FNVplVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINK 231
Cdd:PRK08560 34 YIGFEPSGK-IHLGHLL------TmnkladLQKAgFKV--TVLLADWHAYLNDKGDLEEIRKVAEYNKKVFEALGLDPDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 232 T-FIF-----SDLDYMGmssgfykNVVKIQKHVTFNQVK---GIFG--FTDSDcIGKISFPAIQAApsfsnsfpQIFRDR 300
Cdd:PRK08560 105 TeFVLgsefqLDKEYWL-------LVLKLAKNTTLARARrsmTIMGrrMEEPD-VSKLVYPLMQVA--------DIFYLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 301 TDIqclipcA---IDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNK--- 374
Cdd:PRK08560 169 VDI------AvggMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGIKMSKSKPGSAIFVHDSPEEIRRKIKKayc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 375 ----------------HAFSG-GRDTIEEHRQFGGNcdvdvsfmyLTFfleddDKLEQIRKDYTSGAMLTGELKKA---- 433
Cdd:PRK08560 243 ppgevegnpvleiakyHIFPRyDPFVIERPEKYGGD---------LEY-----ESYEELERDYAEGKLHPMDLKNAvaey 308
|
....*...
gi 47419914 434 LIEVLQPL 441
Cdd:PRK08560 309 LIEILEPV 316
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
151-439 |
5.11e-21 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 93.11 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 151 ENKKPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDDEKYLwKDLTLDQAYSYAVENAKDIIAC 225
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhAIIGDPSKS-PERKLLSRETVLENAIKAQLAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 226 GFDINKTFIF--SD----LDYMGMSSGFyKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAApsfsnsfpQIFRD 299
Cdd:pfam00579 79 GLDPEKAEIVnnSDwlehLELAWLLRDL-GKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY--------DILLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 300 RTDIQcliPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKTKVNKhAF 377
Cdd:pfam00579 150 KADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYKKIQK-AY 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47419914 378 SGGRDtiEEHRQFGGNCDVDVS-FMYLTFFLEDDDK--LEQIRKDYTSGAMLTGELKKALIEVLQ 439
Cdd:pfam00579 226 TDPDR--EVRKDLKLFTFLSNEeIEILEAELGKSPYreAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
12-61 |
6.97e-21 |
|
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: 85.36 E-value: 6.97e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 47419914 12 LFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKAD 61
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
12-64 |
1.18e-20 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 84.85 E-value: 1.18e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 47419914 12 LFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPP 64
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
13-68 |
2.66e-18 |
|
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: 78.54 E-value: 2.66e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 47419914 13 FNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPA 68
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
219-451 |
2.16e-16 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 79.90 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 219 AKDIIACGFDINKTFIF-----SDLDYMGMssgFYKNVV-------------KIQKHvtfnqvkgifGFTDSDCIGKISF 280
Cdd:PRK12282 64 ALDYLAVGIDPAKSTIFiqsqiPELAELTM---YYMNLVtvarlernptvktEIAQK----------GFGRSIPAGFLTY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 281 PAIQAApsfsnsfpqifrdrtDIQC----LIPCAIDQDPYFRMTRDVAPRIGY---------PKPALLHSTFFPALQGaQ 347
Cdd:PRK12282 131 PVSQAA---------------DITAfkatLVPVGDDQLPMIEQTREIVRRFNSlygtdvlvePEALLPEAGRLPGLDG-K 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 348 TKMSASDPNSsIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNcdvdVSFMYLTFFLEDDDKLEQIRKDYTSGAMLT 427
Cdd:PRK12282 195 AKMSKSLGNA-IYLSDDADTIKKKVMSMYTDPNHIRVEDPGKVEGN----VVFTYLDAFDPDKAEVAELKAHYQRGGLGD 269
|
250 260
....*....|....*....|....
gi 47419914 428 GELKKALIEVLQPLIAEHQARRKE 451
Cdd:PRK12282 270 VKCKRYLEEVLQELLAPIRERRAE 293
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
13-53 |
2.62e-14 |
|
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: 66.79 E-value: 2.62e-14
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 47419914 13 FNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAA 53
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEA 41
|
|
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
219-459 |
1.60e-13 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 71.27 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 219 AKDIIACGFDINKTFIF--SDLD-------YMGMSSGF--------YKNvvKIQKHvtfnqvkgifgfTDSDCIGKISFP 281
Cdd:PRK00927 62 AADYLACGIDPEKSTIFvqSHVPehaelawILNCITPLgelermtqFKD--KSAKQ------------KENVSAGLFTYP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 282 AIQAApsfsnsfpqifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGYpkpalLHSTFFPA------------- 342
Cdd:PRK00927 128 VLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFNN-----LYGEVFPVpeplipkvgarvm 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 343 -LQGAQTKMSASDPN--SSIFLTDTAKQIKTKVNKhAFSggrDTIEEHR-QFGGNCDVDVS--FMYLTFFLedDDKLEQI 416
Cdd:PRK00927 186 gLDGPTKKMSKSDPNdnNTINLLDDPKTIAKKIKK-AVT---DSERLREiRYDLPNKPEVSnlLTIYSALS--GESIEEL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 47419914 417 RKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVT------DEIVKE 459
Cdd:PRK00927 260 EAEYEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLadpaylDEILAE 308
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
224-443 |
1.16e-11 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 66.25 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 224 ACGFDI-NKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVK---GIFGFTDSD--CIGKISFPAIQAApsfsnsfpQIF 297
Cdd:PTZ00126 136 AAGMDMdNVRFLWASEEINKNPNDYWLRVMDIARSFNITRIKrcsQIMGRSEGDeqPCAQILYPCMQCA--------DIF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 298 RDRTDIQCLipcAIDQDPYFRMTRDVA--PRIGYpKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVnKH 375
Cdd:PTZ00126 208 YLKADICQL---GMDQRKVNMLAREYCdkKKIKK-KPIILSHHMLPGLLEGQEKMSKSDPNSAIFMEDSEEDVNRKI-KK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 376 AFS-----GGRDTIE--EHRQFGgncdvdvsfMYLTFFLEDDDK---------LEQIRKDYTSGAMLTGELKKALIEVLQ 439
Cdd:PTZ00126 283 AYCppgviEGNPILAyfKSIVFP---------AFNSFTVLRKEKnggdvtyttYEELEKDYLSGALHPGDLKPALAKYLN 353
|
....
gi 47419914 440 PLIA 443
Cdd:PTZ00126 354 LMLQ 357
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
158-438 |
1.41e-08 |
|
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: 55.69 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 158 LYTGRGPSSEAMHVGHLIPFIFTKWLQDV-FNVPLVI----QMTDD---EKYLWKDLTLDQAysyaVENAKDI------I 223
Cdd:cd00805 3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAgHEVIVLIgdatAMIGDpsgKSEERKLLDLELI----RENAKYYkkqlkaI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 224 ACGFDINKTFIFSDLDYMGmsSGFYKNVVKIQKHVTFNQ------VKGIFGFTDSDCIGKISFPAIQAAPSFsnsfpQIF 297
Cdd:cd00805 79 LDFIPPEKAKFVNNSDWLL--SLYTLDFLRLGKHFTVNRmlrrdaVKVRLEEEEGISFSEFIYPLLQAYDFV-----YLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 298 RDrtdIQClipCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAqtKMSASDPNSS-IFLTDTAKQIKTKVNKhA 376
Cdd:cd00805 152 VD---LQL---GGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG--KMSKSEGNAIwDPVLDSPYDVYQKIRN-A 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47419914 377 FsggrdtieehrqfggncDVDV-SFM-YLTFFleDDDKLEQIRKDYTSGaMLTGELKKALIEVL 438
Cdd:cd00805 223 F-----------------DPDVlEFLkLFTFL--DYEEIEELEEEHAEG-PLPRDAKKALAEEL 266
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
8-68 |
1.40e-06 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 50.90 E-value: 1.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47419914 8 SLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSyKAAAGEDYKADCPPGNPA 68
Cdd:PLN02734 8 ALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQAAVGAGGDG 67
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
224-377 |
1.45e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 50.67 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 224 ACGFDINKT-FIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKG---IFGFTDSDCIG-KISFPAIQAApsfsnsfpQIFR 298
Cdd:PTZ00348 102 AAGMDMDKVlFLWSSEEITNHANTYWRTVLDIGRQNTIARIKKcctIMGKTEGTLTAaQVLYPLMQCA--------DIFF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 299 DRTDIQCLipcAIDQDPYFRMTRDVAPRIGYP-KPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVnKHAF 377
Cdd:PTZ00348 174 LKADICQL---GLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKI-RQAY 249
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
16-47 |
1.00e-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: 39.76 E-value: 1.00e-04
10 20 30
....*....|....*....|....*....|..
gi 47419914 16 IATQGELVRSLKAGNASKDEIDSAVKMLVSLK 47
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELK 38
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
16-55 |
1.19e-04 |
|
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: 39.38 E-value: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 47419914 16 IATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAG 55
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
153-393 |
4.97e-04 |
|
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: 42.38 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 153 KKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDD---EKYLWKDLTLDQAYSYAvENAKDIIA 224
Cdd:TIGR00234 29 ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLlgdftALIGDptgKSEVRKILTREEVQENA-ENIKKQIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 225 CGFDINKTFI------FSDLDYMGMssgfyknVVKIQKHVTFNQVKGIFGFTDSdcigkisfpaIQAAPSFSNSFPQIFR 298
Cdd:TIGR00234 108 RFLDFEKAKFvynsewLLKLNYTDF-------IRLLGKIFTVNRMLRRDAFSSR----------FEENISLHEFIYPLLQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47419914 299 DrTDIQCL-IPCAI---DQDPYFRMTRDVA----PRIGYPKPALLHSTFFPALQG--AQTKMSASDPNSS--IFLTDTAK 366
Cdd:TIGR00234 171 A-YDFVYLnVDLQLggsDQWFNIRKGRDLArenlPSLQFGLTVPLLTPADGEKMGksLGGAVSLDEGKYDfyQKVINTPD 249
|
250 260
....*....|....*....|....*..
gi 47419914 367 QIKTKVNKHAFSGGRDTIEEHRQFGGN 393
Cdd:TIGR00234 250 ELVKKYLKLFTFLGLEEIEQLVELKGP 276
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
134-185 |
6.03e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 38.73 E-value: 6.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 47419914 134 RGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQD 185
Cdd:PRK13354 12 RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQD 63
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