|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
90-471 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 672.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 90 VDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELVNRIERATGQKPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 169
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 170 SSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKKTFIFSDLDYMGMS 249
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 250 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDSIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 329
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 330 PRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLT 409
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57090365 410 FFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKL 471
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
159-476 |
8.54e-128 |
|
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: 373.97 E-value: 8.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 159 KPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQdVFNVPLVIQMTDDEKYLWKDlTLDQAYGYAVEN-AKDIIACGFDIKKT 237
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 238 FIFSDLDYmgmsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----SIGKISFPAIQAAPSFSNSFPqifrdrtdiqcLI 312
Cdd:TIGR00233 78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 313 PCAIDQDPYFRMTRDVAPRIG------YPKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKTKVNKHAFSGG 385
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNkkfknfFPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 386 RDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVTDEIVKEF 465
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
330
....*....|..
gi 57090365 466 MTP-RKLSYDFQ 476
Cdd:TIGR00233 303 LEPgAKKARETA 314
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
162-446 |
4.31e-115 |
|
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: 339.94 E-value: 4.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 162 YLYTGRGPSSeAMHVGHLIP-FIFTKWLQDVfNVPLVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKKTFIF 240
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 241 SDLDYmgmsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDSIGKISFPAIQAAPSFSNSFpqifrdrtdiqCLIPC 314
Cdd:cd00806 79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 315 AIDQDPYFRMTRDVAPRIG------YPKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGR 386
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNklygeiFPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 387 DtieEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPL 446
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
222-464 |
1.44e-23 |
|
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: 100.89 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 222 ENAKDIIACGFDIKKTFIF--SDLD-------YMGMSPGF--------YKNvvKIQKHVtfnqvkgifgfTDSDSIGKIS 284
Cdd:COG0180 62 EVAADYLAAGLDPEKSTIFvqSDVPehaelawLLSCLTPLgelermpqFKD--KSAKNG-----------KENVNAGLLT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 285 FPAIQAApsfsnsfpqifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRI------GYPKPALLHSTFFPALQG-- 350
Cdd:COG0180 129 YPVLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFnhrygeVFPEPEALIPEEGARIPGld 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 351 AQTKMSASDpNSSIFLTDTAKQIKTKVNKhAFSggrDTIEEHRQFGGNCDVDVSFMYLTFFLeDDDKLEQIRKDYTSGDM 430
Cdd:COG0180 192 GRKKMSKSY-GNTINLLDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 57090365 431 LTGELKKTLIEVLQPLIAEHQARRKEVT------DEIVKE 464
Cdd:COG0180 266 GYGDLKKALAEAVVEFLAPIRERRAELLadpaelDEILAE 305
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
17-69 |
5.72e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 88.71 E-value: 5.72e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 57090365 17 LFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKADCPP 69
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
17-66 |
7.94e-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: 7.94e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 57090365 17 LFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKAD 66
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
156-444 |
3.79e-20 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 90.41 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 156 ENKKPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDDEKYLwKDLTLDQAYGYAVENAKDIIAC 230
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhAIIGDPSKS-PERKLLSRETVLENAIKAQLAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 231 GFDIKKTFIF--SD-LDYMGMSPGFYK--NVVKIQKHVTFNQVKGIFGFTDSDSIGKISFPAIQAApsfsnsfpQIFRDR 305
Cdd:pfam00579 79 GLDPEKAEIVnnSDwLEHLELAWLLRDlgKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY--------DILLLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 306 TDIQcliPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKTKVNKhAFS 383
Cdd:pfam00579 151 ADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYKKIQK-AYT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57090365 384 GGRDtiEEHRQFGGNCDVDVS-FMYLTFFLEDDDK--LEQIRKDYTSGDMLTGELKKTLIEVLQ 444
Cdd:pfam00579 227 DPDR--EVRKDLKLFTFLSNEeIEILEAELGKSPYreAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
18-73 |
1.14e-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: 79.69 E-value: 1.14e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 57090365 18 FNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKADCPPARPA 73
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
16-65 |
6.58e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 52.05 E-value: 6.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 57090365 16 ELFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSyKATVGEEYKA 65
Cdd:PLN02734 11 EKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQA 59
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
90-471 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 672.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 90 VDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELVNRIERATGQKPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 169
Cdd:PLN02486 3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 170 SSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKKTFIFSDLDYMGMS 249
Cdd:PLN02486 83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 250 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDSIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 329
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 330 PRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLT 409
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57090365 410 FFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKL 471
Cdd:PLN02486 321 FFLEDDAELERIKKEYGSGRMLTGEVKKRLIEVLTEIVERHQRARAAVTDEMVDAFMAVRPL 382
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
86-465 |
2.69e-142 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 412.34 E-value: 2.69e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 86 EEDF-VDPWTVQTSsakgIDYDKLIVRFGSSKIDKELVNrIERatgqkPHRFLRRGIFFSHRDMNQILDAYENKKPFYLY 164
Cdd:PRK12285 1 EDEFmVTPWEVSGI----VDYDKLFEEFGIEPFTEVLPE-LPE-----PHPLMRRGIIFGHRDYDKILEAYRNGKPFAVY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 165 TGRGPSSEaMHVGHLIPFIFTKWLQDvFNVPLVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKKTFIFSDLD 244
Cdd:PRK12285 71 TGFMPSGP-MHIGHKMVFDELKWHQE-FGANVYIPIADDEAYAARGLSWEETREWAYEYILDLIALGFDPDKTEIYFQSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 245 YMGMspgfYKNVVKIQKHVTFNQVKGIFGFTDSDSIGKISFPAIQAAPSFsnsFPQIFRDRTdiQCLIPCAIDQDPYFRM 324
Cdd:PRK12285 149 NIKV----YDLAFELAKKVNFSELKAIYGFTGETNIGHIFYPATQAADIL---HPQLEEGPK--PTLVPVGIDQDPHIRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 325 TRDVAPRI----GYPKPALLHSTFFPALQGaqTKMSASDPNSSIFLTDTAKQIKTKVnKHAFSGGRDTIEEHRQFGGNCD 400
Cdd:PRK12285 220 TRDIAERLhggyGFIKPSSTYHKFMPGLTG--GKMSSSKPESAIYLTDDPETVKKKI-MKALTGGRATLEEQRKLGGEPD 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57090365 401 VDVSFMYLTFFLEDDDK-LEQIRKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVtDEIVKEF 465
Cdd:PRK12285 297 ECVVYELLLYHLEEDDKeLKEIYEECRSGELLCGECKKEAAEKIAEFLKEHQEKREEA-REILEKY 361
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
159-476 |
8.54e-128 |
|
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: 373.97 E-value: 8.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 159 KPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQdVFNVPLVIQMTDDEKYLWKDlTLDQAYGYAVEN-AKDIIACGFDIKKT 237
Cdd:TIGR00233 1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 238 FIFSDLDYmgmsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----SIGKISFPAIQAAPSFSNSFPqifrdrtdiqcLI 312
Cdd:TIGR00233 78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 313 PCAIDQDPYFRMTRDVAPRIG------YPKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKTKVNKHAFSGG 385
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNkkfknfFPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 386 RDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVTDEIVKEF 465
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVLQEFLKEIQERRAEIAEEILDKI 302
|
330
....*....|..
gi 57090365 466 MTP-RKLSYDFQ 476
Cdd:TIGR00233 303 LEPgAKKARETA 314
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
162-446 |
4.31e-115 |
|
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: 339.94 E-value: 4.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 162 YLYTGRGPSSeAMHVGHLIP-FIFTKWLQDVfNVPLVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKKTFIF 240
Cdd:cd00806 1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 241 SDLDYmgmsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDSIGKISFPAIQAAPSFSNSFpqifrdrtdiqCLIPC 314
Cdd:cd00806 79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 315 AIDQDPYFRMTRDVAPRIG------YPKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGR 386
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNklygeiFPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 387 DtieEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGDMLTGELKKTLIEVLQPL 446
Cdd:cd00806 224 T---EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF 280
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
222-464 |
1.44e-23 |
|
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: 100.89 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 222 ENAKDIIACGFDIKKTFIF--SDLD-------YMGMSPGF--------YKNvvKIQKHVtfnqvkgifgfTDSDSIGKIS 284
Cdd:COG0180 62 EVAADYLAAGLDPEKSTIFvqSDVPehaelawLLSCLTPLgelermpqFKD--KSAKNG-----------KENVNAGLLT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 285 FPAIQAApsfsnsfpqifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRI------GYPKPALLHSTFFPALQG-- 350
Cdd:COG0180 129 YPVLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFnhrygeVFPEPEALIPEEGARIPGld 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 351 AQTKMSASDpNSSIFLTDTAKQIKTKVNKhAFSggrDTIEEHRQFGGNCDVDVSFMYLTFFLeDDDKLEQIRKDYTSGDM 430
Cdd:COG0180 192 GRKKMSKSY-GNTINLLDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEAEYRAGGI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 57090365 431 LTGELKKTLIEVLQPLIAEHQARRKEVT------DEIVKE 464
Cdd:COG0180 266 GYGDLKKALAEAVVEFLAPIRERRAELLadpaelDEILAE 305
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
164-446 |
1.35e-22 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 98.40 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 164 YTGRGPSSEaMHVGHLIpfiftkW------LQDV-FNVplVIQMTDDEKYLWKDLTLDQAYGYAVENAKDIIACGFDIKK 236
Cdd:PRK08560 34 YIGFEPSGK-IHLGHLL------TmnkladLQKAgFKV--TVLLADWHAYLNDKGDLEEIRKVAEYNKKVFEALGLDPDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 237 T-FIF-----SDLDYMGmspgfykNVVKIQKHVTFNQVK---GIFGFTDSDS-IGKISFPAIQAApsfsnsfpQIFRDRT 306
Cdd:PRK08560 105 TeFVLgsefqLDKEYWL-------LVLKLAKNTTLARARrsmTIMGRRMEEPdVSKLVYPLMQVA--------DIFYLDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 307 DIqclipcA---IDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNK---- 379
Cdd:PRK08560 170 DI------AvggMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGIKMSKSKPGSAIFVHDSPEEIRRKIKKaycp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 380 ---------------HAFSG-GRDTIEEHRQFGGNcdvdvsfmyLTFfleddDKLEQIRKDYTSGDMLTGELKKT----L 439
Cdd:PRK08560 244 pgevegnpvleiakyHIFPRyDPFVIERPEKYGGD---------LEY-----ESYEELERDYAEGKLHPMDLKNAvaeyL 309
|
....*..
gi 57090365 440 IEVLQPL 446
Cdd:PRK08560 310 IEILEPV 316
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
17-69 |
5.72e-22 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 88.71 E-value: 5.72e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 57090365 17 LFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKADCPP 69
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
17-66 |
7.94e-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: 7.94e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 57090365 17 LFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKAD 66
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
156-444 |
3.79e-20 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 90.41 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 156 ENKKPFYLYTGRGPSSeAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDDEKYLwKDLTLDQAYGYAVENAKDIIAC 230
Cdd:pfam00579 1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhAIIGDPSKS-PERKLLSRETVLENAIKAQLAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 231 GFDIKKTFIF--SD-LDYMGMSPGFYK--NVVKIQKHVTFNQVKGIFGFTDSDSIGKISFPAIQAApsfsnsfpQIFRDR 305
Cdd:pfam00579 79 GLDPEKAEIVnnSDwLEHLELAWLLRDlgKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY--------DILLLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 306 TDIQcliPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKTKVNKhAFS 383
Cdd:pfam00579 151 ADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYKKIQK-AYT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57090365 384 GGRDtiEEHRQFGGNCDVDVS-FMYLTFFLEDDDK--LEQIRKDYTSGDMLTGELKKTLIEVLQ 444
Cdd:pfam00579 227 DPDR--EVRKDLKLFTFLSNEeIEILEAELGKSPYreAEELLAREVTGLVHGGDLKKAAAEAVN 288
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
18-73 |
1.14e-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: 79.69 E-value: 1.14e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 57090365 18 FNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKATVGEEYKADCPPARPA 73
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
224-456 |
3.86e-16 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 79.13 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 224 AKDIIACGFDIKKTFIF-----SDLDYMGMspgFYKNVV-------------KIQKHvtfnqvkgifGFTDSDSIGKISF 285
Cdd:PRK12282 64 ALDYLAVGIDPAKSTIFiqsqiPELAELTM---YYMNLVtvarlernptvktEIAQK----------GFGRSIPAGFLTY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 286 PAIQAApsfsnsfpqifrdrtDIQC----LIPCAIDQDPYFRMTRDVAPRIGY---------PKPALLHSTFFPALQGaQ 352
Cdd:PRK12282 131 PVSQAA---------------DITAfkatLVPVGDDQLPMIEQTREIVRRFNSlygtdvlvePEALLPEAGRLPGLDG-K 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 353 TKMSASDPNSsIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNcdvdVSFMYLTFFLEDDDKLEQIRKDYTSGDMLT 432
Cdd:PRK12282 195 AKMSKSLGNA-IYLSDDADTIKKKVMSMYTDPNHIRVEDPGKVEGN----VVFTYLDAFDPDKAEVAELKAHYQRGGLGD 269
|
250 260
....*....|....*....|....
gi 57090365 433 GELKKTLIEVLQPLIAEHQARRKE 456
Cdd:PRK12282 270 VKCKRYLEEVLQELLAPIRERRAE 293
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
18-57 |
2.80e-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: 2.80e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 57090365 18 FNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSYKA 57
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKE 40
|
|
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
224-464 |
2.29e-12 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 67.81 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 224 AKDIIACGFDIKKTFIF--SDLD-------YMGMSPGF--------YKNvvKIQKHvtfnqvkgifgfTDSDSIGKISFP 286
Cdd:PRK00927 62 AADYLACGIDPEKSTIFvqSHVPehaelawILNCITPLgelermtqFKD--KSAKQ------------KENVSAGLFTYP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 287 AIQAApsfsnsfpqifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGYpkpalLHSTFFPA------------- 347
Cdd:PRK00927 128 VLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFNN-----LYGEVFPVpeplipkvgarvm 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 348 -LQGAQTKMSASDPN--SSIFLTDTAKQIKTKVNKhAFSggrDTIEEHR-QFGGNCDVDVS--FMYLTFFLedDDKLEQI 421
Cdd:PRK00927 186 gLDGPTKKMSKSDPNdnNTINLLDDPKTIAKKIKK-AVT---DSERLREiRYDLPNKPEVSnlLTIYSALS--GESIEEL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 57090365 422 RKDYTSGDMLTGELKKTLIEVLQPLIAEHQARRKEVT------DEIVKE 464
Cdd:PRK00927 260 EAEYEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLadpaylDEILAE 308
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
252-448 |
7.96e-11 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 63.56 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 252 FYKNVVKIQKHVTFNQVK---GIFGFTDSD--SIGKISFPAIQAApsfsnsfpQIFRDRTDIQCLipcAIDQDPYFRMTR 326
Cdd:PTZ00126 160 YWLRVMDIARSFNITRIKrcsQIMGRSEGDeqPCAQILYPCMQCA--------DIFYLKADICQL---GMDQRKVNMLAR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 327 DVA--PRIGYpKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVnKHAFS-----GGRDTIE--EHRQFGg 397
Cdd:PTZ00126 229 EYCdkKKIKK-KPIILSHHMLPGLLEGQEKMSKSDPNSAIFMEDSEEDVNRKI-KKAYCppgviEGNPILAyfKSIVFP- 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 398 ncdvdvsfMYLTFFLEDDDK---------LEQIRKDYTSGDMLTGELKKTLIEVLQPLIA 448
Cdd:PTZ00126 306 --------AFNSFTVLRKEKnggdvtyttYEELEKDYLSGALHPGDLKPALAKYLNLMLQ 357
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
163-443 |
2.97e-09 |
|
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: 57.62 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 163 LYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDD---EKYLWKDLTLDQaygyaVENAKDIIAcgFDI 234
Cdd:cd00805 3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLigdatAMIGDpsgKSEERKLLDLEL-----IRENAKYYK--KQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 235 KKTFIFSDLD----------YMGMSpgfYKNVVKIQKHVTFNQ------VKGIFGFTDSDSIGKISFPAIQAAPSFsnsf 298
Cdd:cd00805 76 KAILDFIPPEkakfvnnsdwLLSLY---TLDFLRLGKHFTVNRmlrrdaVKVRLEEEEGISFSEFIYPLLQAYDFV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 299 pQIFRDrtdIQClipCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAqtKMSASDPNSS-IFLTDTAKQIKTKV 377
Cdd:cd00805 149 -YLDVD---LQL---GGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG--KMSKSEGNAIwDPVLDSPYDVYQKI 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57090365 378 NKhAFsggrdtieehrqfggncDVDV-SFM-YLTFFleDDDKLEQIRKDYTSGdMLTGELKKTLIEVL 443
Cdd:cd00805 220 RN-AF-----------------DPDVlEFLkLFTFL--DYEEIEELEEEHAEG-PLPRDAKKALAEEL 266
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
16-65 |
6.58e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 52.05 E-value: 6.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 57090365 16 ELFNSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLKMSyKATVGEEYKA 65
Cdd:PLN02734 11 EKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKELQA 59
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
229-382 |
1.68e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 50.67 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 229 ACGFDIKKT-FIFSDLDYMGMSPGFYKNVVKIQKHVTFNQVKG---IFGFTDSD-SIGKISFPAIQAApsfsnsfpQIFR 303
Cdd:PTZ00348 102 AAGMDMDKVlFLWSSEEITNHANTYWRTVLDIGRQNTIARIKKcctIMGKTEGTlTAAQVLYPLMQCA--------DIFF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 304 DRTDIQCLipcAIDQDPYFRMTRDVAPRIGYP-KPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVnKHAF 382
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 ... |
21-52 |
2.05e-06 |
|
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: 44.38 E-value: 2.05e-06
10 20 30
....*....|....*....|....*....|..
gi 57090365 21 IAAQGELVRSLKAGKASKDEIDSAVKLLLSLK 52
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 ... |
21-52 |
8.24e-06 |
|
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: 42.84 E-value: 8.24e-06
10 20 30
....*....|....*....|....*....|..
gi 57090365 21 IAAQGELVRSLKAGKASKDEIDSAVKLLLSLK 52
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLK 36
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
158-398 |
5.86e-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: 42.00 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 158 KKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVI-----QMTDD---EKYLWKDLTLDQAYGYAvENAKDIIA 229
Cdd:TIGR00234 29 ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLlgdftALIGDptgKSEVRKILTREEVQENA-ENIKKQIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 230 CGFDIKKTFI------FSDLDYMGMspgfyknVVKIQKHVTFNQVKGIFGFT---DSD-SIGKISFPAIQAapsfsnsfp 299
Cdd:TIGR00234 108 RFLDFEKAKFvynsewLLKLNYTDF-------IRLLGKIFTVNRMLRRDAFSsrfEENiSLHEFIYPLLQA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57090365 300 qifrdrTDIQCL-IPCAI---DQDPYFRMTRDVA----PRIGYPKPALLHSTFFPALQG--AQTKMSASDPNSS--IFLT 367
Cdd:TIGR00234 172 ------YDFVYLnVDLQLggsDQWFNIRKGRDLArenlPSLQFGLTVPLLTPADGEKMGksLGGAVSLDEGKYDfyQKVI 245
|
250 260 270
....*....|....*....|....*....|.
gi 57090365 368 DTAKQIKTKVNKHAFSGGRDTIEEHRQFGGN 398
Cdd:TIGR00234 246 NTPDELVKKYLKLFTFLGLEEIEQLVELKGP 276
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
139-190 |
3.24e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 39.88 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 57090365 139 RGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQD 190
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 ... |
13-52 |
4.63e-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: 35.15 E-value: 4.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 57090365 13 SPLELfnSIAAQGELVRSLKAGKASKDEIDSAVKLLLSLK 52
Cdd:cd00935 2 APLRA--AVKEQGDLVRKLKEEGAPDVDIKKAVAELKARK 39
|
|
| |
