|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
3-475 |
0e+00 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 612.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKE---TVSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAial 79
Cdd:COG0215 2 LKLYNTLTRKKEefvPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 80 sekepgkyADLKQALAAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGSVYYRISEKKD 159
Cdd:COG0215 79 --------AEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 160 YGKLSRIDLEKNKTGTRYNTDEYdKDDVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDL 239
Cdd:COG0215 151 YGKLSGRNLDDLRAGARVEVDEE-KRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 240 IFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAAHYSQKVNYTADAL 319
Cdd:COG0215 230 IFPHHENEIAQSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-YDPEVLRFFLLSAHYRSPLDFSEEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 320 HQAEAGVEKFYGLLARLDRLqkidAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNIDAKNDqlsSA 399
Cdd:COG0215 309 EEAEKALERLYNALRRLEEA----LGAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGED---KA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 400 DLEVIRQTLTYFDQVLGLIDLMPKAQVG--------DDLQQLLAERNAARAAKDFKRADALRDQLLAAGYKILDTKSGSH 471
Cdd:COG0215 382 ALAALAALLRALGGVLGLLLLEPEAWQGaaedelldALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTT 461
|
....
gi 504614693 472 LEKV 475
Cdd:COG0215 462 WRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-474 |
9.00e-155 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 447.60 E-value: 9.00e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKET---VSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIAL 79
Cdd:TIGR00435 1 LKLYNTLTRQKEEfepLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 80 SEKEPgkyadlkqalaAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQD-GSVYYRISEKK 158
Cdd:TIGR00435 81 GESVY-----------EVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 159 DYGKLSRIDLEKNKTGTRYNTDEYDKDdVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVD 238
Cdd:TIGR00435 150 DYGKLSKQDLDQLEAGARVDVDEAKRN-KLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 239 LIFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAAHYSQKVNYTADA 318
Cdd:TIGR00435 229 LIFPHHENEIAQSEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKN-YDPEILRYFLLSVHYRSPLDFSEEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 319 LHQAEAGVEKFYGLLARLDRLQKIDAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNidakndQLSS 398
Cdd:TIGR00435 308 LEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDEKEFEARFVEAMDDDLNTANALAVLFELAKSINLT------FVSK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 399 ADLEVIRQTLTYFDQVLGLIDLMP----KAQVGDDLQ---QLLAERNAARAAKDFKRADALRDQLLAAGYKILDTKSGSH 471
Cdd:TIGR00435 382 ADAALLIEHLIFLESRLGLLLGLPskpvQAGSNDDLGeieALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTT 461
|
...
gi 504614693 472 LEK 474
Cdd:TIGR00435 462 WRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
16-322 |
5.39e-120 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 353.21 E-value: 5.39e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 16 VSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIALSEKEpgkyadlkQALA 95
Cdd:pfam01406 5 LHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESF--------RQLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 96 AYtepYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYE-QDGSVYYRISEKKDYGKLSRIDLEKNKTG 174
Cdd:pfam01406 77 AR---FIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVsDNGDVYFDVSSFPDYGKLSGQNLEQLEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 175 TRYNTDEyDKDDVRDFVLWKAEgKEG-VHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDLIFPHHENEIAQSES 253
Cdd:pfam01406 154 ARGEVSE-GKRDPLDFALWKAS-KEGePSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504614693 254 GYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLaQGRRPEVIRYFLLAAHYSQKVNYTADALHQA 322
Cdd:pfam01406 232 AFDKQLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVL-KRYDPEILRYFLLSVHYRSPLDFSEELLEQA 299
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-475 |
7.99e-112 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 339.20 E-value: 7.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 1 MHIQLFNTLSKQKETVSSRE---VKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDV--------- 68
Cdd:PRK14536 1 MALRLYNTLGRQQEEFQPIEhghVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddads 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 69 -DDKTIKgaialSEKEPGKYAdlkQALAAYtepYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQD 147
Cdd:PRK14536 81 gEDKMVK-----SAQEHGKSV---LEIAAH---YTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 148 GSVYYRISEKKDYGKLSRIDLEKNKTGTRYNTDEyDKDDVRDFVLWKAEGKEGVH---WHSSHGDGRPGWHLECSAMIHE 224
Cdd:PRK14536 150 GNVYFDIRTFPSYGSLASAAVEDLQAGARIEHDT-NKRNPHDFVLWFTRSKFENHaltWDSPWGRGYPGWHIECSAMSMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 225 IFKGAIDIHTGGVDLIFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGRRPEVIRYFLL 304
Cdd:PRK14536 229 YLGEQCDIHIGGVDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKGFQPLDYRFFLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 305 AAHYSQKVNYTADALHQAEAGVEKFYGLLAR-LDRLQKIDAAADATLAATAKEAR------------EKFMAELADDLNT 371
Cdd:PRK14536 309 GGHYRSQLAFSWEALKTAKAARRSLVRRVARvVDAARATTGSVRGTLAECAAERVaesraseselllTDFRAALEDDFST 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 372 PRALAVVLEFIRAANTNIDAKNDQLSSAD----LEVIRQTLTYFDqvlgliDLMPKAQVGDDLQQLLAERNAARAAKDFK 447
Cdd:PRK14536 389 PKALSELQKLVKDTSVPPSLCLSVLQAMDtvlgLGLIQEATASLS------AQVPAGPSEEEIGQLIEARAHARQTKDFP 462
|
490 500
....*....|....*....|....*...
gi 504614693 448 RADALRDQLLAAGYKILDTKSGSHLEKV 475
Cdd:PRK14536 463 LADEIRDKLKAEGIELEDTHLGTIWKRV 490
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
4-315 |
3.96e-94 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 283.70 E-value: 3.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 4 QLFNTLSKQKETVSSR---EVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIALS 80
Cdd:cd00672 1 RLYNTLTRQKEEFVPLnpgLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 81 EKEpgkyadlkqalAAYTEPYTEAFFADLKTLNVCKFDFHPRAtdyipamldlvdrliaqgvayeqdgsvyyrisekkdy 160
Cdd:cd00672 81 LSW-----------KEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 161 gklsridleknktgtryntdeydkddvrdfvlwkaegkegvhwhsshgdgrpgWHLECSAMIHEIFKGAIDIHTGGVDLI 240
Cdd:cd00672 113 -----------------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLI 139
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504614693 241 FPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLaQGRRPEVIRYFLLAAHYSQKVNYT 315
Cdd:cd00672 140 FPHHENEIAQSEAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDAL-KKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
360-417 |
8.63e-10 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 54.50 E-value: 8.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504614693 360 KFMAELADDLNTPRALAVVLEFIRAANTNIDAKNDqlsSADLEVIRQTLTYFDQVLGL 417
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKATD---AEELAALAALLRALGGVLGL 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
3-475 |
0e+00 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 612.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKE---TVSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAial 79
Cdd:COG0215 2 LKLYNTLTRKKEefvPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 80 sekepgkyADLKQALAAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGSVYYRISEKKD 159
Cdd:COG0215 79 --------AEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 160 YGKLSRIDLEKNKTGTRYNTDEYdKDDVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDL 239
Cdd:COG0215 151 YGKLSGRNLDDLRAGARVEVDEE-KRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 240 IFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAAHYSQKVNYTADAL 319
Cdd:COG0215 230 IFPHHENEIAQSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKK-YDPEVLRFFLLSAHYRSPLDFSEEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 320 HQAEAGVEKFYGLLARLDRLqkidAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNIDAKNDqlsSA 399
Cdd:COG0215 309 EEAEKALERLYNALRRLEEA----LGAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGED---KA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 400 DLEVIRQTLTYFDQVLGLIDLMPKAQVG--------DDLQQLLAERNAARAAKDFKRADALRDQLLAAGYKILDTKSGSH 471
Cdd:COG0215 382 ALAALAALLRALGGVLGLLLLEPEAWQGaaedelldALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTT 461
|
....
gi 504614693 472 LEKV 475
Cdd:COG0215 462 WRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-474 |
9.00e-155 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 447.60 E-value: 9.00e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKET---VSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIAL 79
Cdd:TIGR00435 1 LKLYNTLTRQKEEfepLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 80 SEKEPgkyadlkqalaAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQD-GSVYYRISEKK 158
Cdd:TIGR00435 81 GESVY-----------EVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 159 DYGKLSRIDLEKNKTGTRYNTDEYDKDdVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVD 238
Cdd:TIGR00435 150 DYGKLSKQDLDQLEAGARVDVDEAKRN-KLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 239 LIFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAAHYSQKVNYTADA 318
Cdd:TIGR00435 229 LIFPHHENEIAQSEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKN-YDPEILRYFLLSVHYRSPLDFSEEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 319 LHQAEAGVEKFYGLLARLDRLQKIDAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNidakndQLSS 398
Cdd:TIGR00435 308 LEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDEKEFEARFVEAMDDDLNTANALAVLFELAKSINLT------FVSK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 399 ADLEVIRQTLTYFDQVLGLIDLMP----KAQVGDDLQ---QLLAERNAARAAKDFKRADALRDQLLAAGYKILDTKSGSH 471
Cdd:TIGR00435 382 ADAALLIEHLIFLESRLGLLLGLPskpvQAGSNDDLGeieALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTT 461
|
...
gi 504614693 472 LEK 474
Cdd:TIGR00435 462 WRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
16-322 |
5.39e-120 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 353.21 E-value: 5.39e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 16 VSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIALSEKEpgkyadlkQALA 95
Cdd:pfam01406 5 LHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESF--------RQLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 96 AYtepYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYE-QDGSVYYRISEKKDYGKLSRIDLEKNKTG 174
Cdd:pfam01406 77 AR---FIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVsDNGDVYFDVSSFPDYGKLSGQNLEQLEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 175 TRYNTDEyDKDDVRDFVLWKAEgKEG-VHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDLIFPHHENEIAQSES 253
Cdd:pfam01406 154 ARGEVSE-GKRDPLDFALWKAS-KEGePSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504614693 254 GYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLaQGRRPEVIRYFLLAAHYSQKVNYTADALHQA 322
Cdd:pfam01406 232 AFDKQLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVL-KRYDPEILRYFLLSVHYRSPLDFSEELLEQA 299
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-475 |
7.99e-112 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 339.20 E-value: 7.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 1 MHIQLFNTLSKQKETVSSRE---VKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDV--------- 68
Cdd:PRK14536 1 MALRLYNTLGRQQEEFQPIEhghVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddads 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 69 -DDKTIKgaialSEKEPGKYAdlkQALAAYtepYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQD 147
Cdd:PRK14536 81 gEDKMVK-----SAQEHGKSV---LEIAAH---YTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 148 GSVYYRISEKKDYGKLSRIDLEKNKTGTRYNTDEyDKDDVRDFVLWKAEGKEGVH---WHSSHGDGRPGWHLECSAMIHE 224
Cdd:PRK14536 150 GNVYFDIRTFPSYGSLASAAVEDLQAGARIEHDT-NKRNPHDFVLWFTRSKFENHaltWDSPWGRGYPGWHIECSAMSMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 225 IFKGAIDIHTGGVDLIFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGRRPEVIRYFLL 304
Cdd:PRK14536 229 YLGEQCDIHIGGVDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKGFQPLDYRFFLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 305 AAHYSQKVNYTADALHQAEAGVEKFYGLLAR-LDRLQKIDAAADATLAATAKEAR------------EKFMAELADDLNT 371
Cdd:PRK14536 309 GGHYRSQLAFSWEALKTAKAARRSLVRRVARvVDAARATTGSVRGTLAECAAERVaesraseselllTDFRAALEDDFST 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 372 PRALAVVLEFIRAANTNIDAKNDQLSSAD----LEVIRQTLTYFDqvlgliDLMPKAQVGDDLQQLLAERNAARAAKDFK 447
Cdd:PRK14536 389 PKALSELQKLVKDTSVPPSLCLSVLQAMDtvlgLGLIQEATASLS------AQVPAGPSEEEIGQLIEARAHARQTKDFP 462
|
490 500
....*....|....*....|....*...
gi 504614693 448 RADALRDQLLAAGYKILDTKSGSHLEKV 475
Cdd:PRK14536 463 LADEIRDKLKAEGIELEDTHLGTIWKRV 490
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
3-470 |
1.22e-101 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 317.74 E-value: 1.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKE---TVSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLR-LAGYQVQHAMNLTDVDDKTIKGAia 78
Cdd:PTZ00399 40 LKVNNSLTGGKVefvPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 79 lseKEPGKyaDLKQALAAYtepYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGSVYYRI---- 154
Cdd:PTZ00399 118 ---REEKL--SIFLELARK---WEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVeafr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 155 SEKKDYGKL---SRIDLEKNKTGT-RYNTDEYDKDDVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAI 230
Cdd:PTZ00399 190 KAGHVYPKLepeSVADEDRIAEGEgALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 231 DIHTGGVDLIFPHHENEIAQSESGYG-DGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAAHYS 309
Cdd:PTZ00399 270 DIHSGGIDLKFPHHDNELAQSEAYFDkHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSK-YTARQIRLLFLLHKWD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 310 QKVNYTADALHQAEAGVEKFYGLLARLD-RLQKIDAAADATLAATAKEAREKFM-------AELADDLNTPRALAVVLEF 381
Cdd:PTZ00399 349 KPMNYSDESMDEAIEKDKVFFNFFANVKiKLRESELTSPQKWTQHDFELNELFEetksavhAALLDNFDTPEALQALQKL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 382 IRAANTNIDAKNdQLSSADLEVIRQTLTYFDQVLGLID------LMPKAQVGDDLQQLLAE--------RNAARAAKD-- 445
Cdd:PTZ00399 429 ISATNTYLNSGE-QPSAPLLRSVAQYVTKILSIFGLVEgsdglgSQGQNSTSENFKPLLEAllrfrdevRDAAKAEMKli 507
|
490 500 510
....*....|....*....|....*....|....*
gi 504614693 446 ---------FKRADALRDQ-LLAAGYKILDTKSGS 470
Cdd:PTZ00399 508 sldkkkkqlLQLCDKLRDEwLPNLGIRIEDKPDGP 542
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
3-470 |
1.28e-94 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 296.84 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKETVSSR---EVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIAL 79
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKvegKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 80 SEkEPgkyadlkqalAAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGSVYYRISEKKD 159
Cdd:PLN02946 140 GE-DP----------ISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 160 YGKLSRIDLEKNKTGTRYNTDEYDKDDVrDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDL 239
Cdd:PLN02946 209 YGKLSGRKLEDNRAGERVAVDSRKKNPA-DFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 240 IFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLaQGRRPEVIRYFLLAAHYSQKVNYTadaL 319
Cdd:PLN02946 288 VFPHHENEIAQSCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVI-DLYHPLALRLFLLGTHYRSPINYS---D 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 320 HQAEAGVEKFYGLLARLDRLQKIDAAADATLAATA---------KEAREKFMAELADDLNTPRALAVVLEFIRAANTNID 390
Cdd:PLN02946 364 VQLESASERIFYIYQTLHDCEESLQQHDSTFEKDSvppdtlnciNKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLH 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 391 AKNDQLSSADLEVIRQTLTYFDQVLGLIDLMPkAQVGDDLQQL------------------LAERNAARAAKDFKRADAL 452
Cdd:PLN02946 444 TRKGKKQEKRLESLAALEKKIRDVLSVLGLMP-TSYSEALQQLrekalrraklteeqvlqkIEERTVARKNKEYEKSDAI 522
|
490
....*....|....*...
gi 504614693 453 RDQLLAAGYKILDTKSGS 470
Cdd:PLN02946 523 RKDLAAVGIALMDSPDGT 540
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
4-315 |
3.96e-94 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 283.70 E-value: 3.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 4 QLFNTLSKQKETVSSR---EVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIALS 80
Cdd:cd00672 1 RLYNTLTRQKEEFVPLnpgLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 81 EKEpgkyadlkqalAAYTEPYTEAFFADLKTLNVCKFDFHPRAtdyipamldlvdrliaqgvayeqdgsvyyrisekkdy 160
Cdd:cd00672 81 LSW-----------KEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 161 gklsridleknktgtryntdeydkddvrdfvlwkaegkegvhwhsshgdgrpgWHLECSAMIHEIFKGAIDIHTGGVDLI 240
Cdd:cd00672 113 -----------------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLI 139
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504614693 241 FPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLaQGRRPEVIRYFLLAAHYSQKVNYT 315
Cdd:cd00672 140 FPHHENEIAQSEAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDAL-KKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-474 |
2.43e-93 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 290.98 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 1 MHIQLFNTLSKQ-KETVSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDV----------D 69
Cdd:PRK14534 1 MLLKLYNTKTKDlSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 70 DKTIKGAialseKEPGkyadlkqaLAAY--TEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQD 147
Cdd:PRK14534 81 DKVVKAA-----RERG--------LTVYeiSRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 148 GSVYYRISEKKDYGKLSRIDL--EKNKTGTRYNTDEYDKDDVrDFVLWKAEGK---EGVHWHSSHGDGRPGWHLECSAMI 222
Cdd:PRK14534 148 GNVYFDTSCFKSYGQMAGINLndFKDMSVSRVEIDKSKRNKS-DFVLWFTNSKfkdQEMKWDSPWGFGYPSWHLECAAMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 223 HEIFKGAIDIHTGGVDLIFPHHENEIAQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGRRPEVIRYF 302
Cdd:PRK14534 227 LEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGFSPLDFRYF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 303 LLAAHYSQKVNYTADALHQAEAGVEK-------FYGLLARLDrLQKIDAAADATLAATAKEAREKFMAELADDLNTPRAL 375
Cdd:PRK14534 307 CLTAHYRTQLKFTFNNLKACKIARENmlnkltyFYSSLDQFD-LNLLNKDLENIEFSLEKEYYDSFLEKIAFDLNIPQGL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 376 AVVLEFIraantnidaKNDQLSSadleVIRQTLTY-FDQVLGL---IDLMPKAQ-----VGDDLQQLLAERNAARAAKDF 446
Cdd:PRK14534 386 ALLWDII---------KDDNLSF----LSKLRLAFkFDEVLSLglrEEILREIEnhrivIDDNMKSLIEERRLAKCEKDF 452
|
490 500
....*....|....*....|....*...
gi 504614693 447 KRADALRDQLLAAGYKILDTKSGSHLEK 474
Cdd:PRK14534 453 KRADEIREYFASKGFVLIDTEEGTKVKR 480
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
5-469 |
7.04e-82 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 267.35 E-value: 7.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 5 LFNTLSKQKET---VSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAialse 81
Cdd:PRK14535 230 IYNTLTRQKEPfapIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARA----- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 82 kepgkyADLKQALAAYTEPYTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAY-EQDGSVYYRISEKKDY 160
Cdd:PRK14535 305 ------AENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAY 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 161 GKLSRIDLEKNKTGTRYNTDEYDKDDVrDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAIDIHTGGVDLI 240
Cdd:PRK14535 379 GQLSGKSLDDLRAGERVEVDGFKRDPL-DFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 241 FPHHENEIAQSESGYGD----------------GFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLL 304
Cdd:PRK14535 458 FPHHENEIAQSVGATGHtcghhhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQ-YDPEVVRFFIL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 305 AAHYSQKVNYTADALHQAEAGVEKFYGLLarldrlqKIDAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRA 384
Cdd:PRK14535 537 RAHYRSPLNYSDAHLDDAKGALTRLYTTL-------KNTPAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 385 ANTNIDAkndQLSSAdlevirqtLTYFDQVLGLIDLMPKA--QVG--------DDLQQLLAERNAARAAKDFKRADALRD 454
Cdd:PRK14535 610 VNKTNDA---QLAGC--------LKALGGIIGLLQRDPTEflQGGaasdglsnEEIEDLIARRKQARADKNWAESDRIRD 678
|
490
....*....|....*
gi 504614693 455 qLLAAGYKILDTKSG 469
Cdd:PRK14535 679 -LLNEHKIILEDNAG 692
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
3-394 |
1.57e-63 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 211.51 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 3 IQLFNTLSKQKETVS-SREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDktikgaiALSE 81
Cdd:TIGR03447 18 LRLFDTADGQVRPVEpGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDD-------PLFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 82 KEPGKYADLkQALAAYTepyTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGS----VYYRISEK 157
Cdd:TIGR03447 91 RAERDGVDW-RELGTSQ---IDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPeypdVYFSIDAT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 158 KDYGKLSRID------LEKNKTGtryNTDEYDKDDVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGAID 231
Cdd:TIGR03447 167 EQFGYESGYDratmleLFAERGG---DPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 232 IHTGGVDLIFPHHENEIAQSESGYGDG-FVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGRRPEVIRYFLLAAHYSQ 310
Cdd:TIGR03447 244 IQGGGSDLIFPHHEFSAAHAEAATGVRrMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAGVDPAAIRLGLLAGHYRQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 311 KVNYTADALHQAEAgvekfygllarldRLQKIDAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNID 390
Cdd:TIGR03447 324 DRDWTDAVLAEAEA-------------RLARWRAALALPDAPDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGG 390
|
....
gi 504614693 391 AKND 394
Cdd:TIGR03447 391 SDTE 394
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
13-387 |
8.59e-61 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 203.62 E-value: 8.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 13 KETVSSREVKIYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIA-------LSEKEpg 85
Cdd:PRK12418 2 RPVAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARdgvdwrdLAERE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 86 kyadlkqalaaytepyTEAFFADLKTLNVCKFDFHPRATDYIPAMLDLVDRLIAQGVAYEQDGS----VYYRISEKKDYG 161
Cdd:PRK12418 80 ----------------IALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEeypdVYFSVDATPQFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 162 KLSRIDLEK------------NKTGtryntdeydKDDVRDFVLWKAEGKEGVHWHSSHGDGRPGWHLECSAMIHEIFKGA 229
Cdd:PRK12418 144 YESGYDRATmlelfaerggdpDRPG---------KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 230 IDIHTGGVDLIFPHHENEIAQSESGYGDG-FVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGRRPEVIRYFLLAAHY 308
Cdd:PRK12418 215 FDIQGGGSDLIFPHHEFSAAHAEAATGERrFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAGVDPAAIRLALLAGHY 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504614693 309 SQKVNYTADALHQAEAgvekfygllarldRLQKIDAAADATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANT 387
Cdd:PRK12418 295 RADREWTDAVLAEAEA-------------RLARWRAAAALPAGPDAADVVARVRAALADDLDTPGALAAVDGWATDALE 360
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
317-469 |
8.07e-18 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.
Pssm-ID: 153417 [Multi-domain] Cd Length: 156 Bit Score: 80.30 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 317 DALHQAEAGVEKFYGLLARLDRlqkidaaaDATLAATAKEAREKFMAELADDLNTPRALAVVLEFIRAANTNidAKNDQL 396
Cdd:cd07963 2 DNLEDARAALERLYTALRGVPP--------TTVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRL--KKEDIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 397 SSADLEvirQTLTYFDQVLGLIDLMPKA--QVGDDL--------QQLLAERNAARAAKDFKRADALRDQLLAAGYKILDT 466
Cdd:cd07963 72 KAAALA---ALLKALGGVLGLLQQDPEAflQGGTGEgglsvaeiEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDS 148
|
...
gi 504614693 467 KSG 469
Cdd:cd07963 149 PEG 151
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
360-417 |
8.63e-10 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 54.50 E-value: 8.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504614693 360 KFMAELADDLNTPRALAVVLEFIRAANTNIDAKNDqlsSADLEVIRQTLTYFDQVLGL 417
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKATD---AEELAALAALLRALGGVLGL 55
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
360-417 |
9.16e-09 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 51.82 E-value: 9.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504614693 360 KFMAELADDLNTPRALAVVLEFIRAANTNIDAKNdqlsSADLEVIRQTLTYFDQVLGL 417
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTND----AEAAAALAALLRELGDVLGL 54
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
23-125 |
2.79e-08 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 52.48 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 23 IYSCGPTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHAMNLTDVDDKTIKGAIALSEKEPgkyADLKQALAAYTEPY- 101
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAK---AFVERWIERIKEDVe 77
|
90 100
....*....|....*....|....*.
gi 504614693 102 --TEAFFADLKtLNVCKFDFHPRATD 125
Cdd:cd00802 78 ymFLQAADFLL-LYETECDIHLGGSD 102
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
261-392 |
1.45e-07 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 53.96 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 261 KHWVHcEHLLVDNKKMSKSAGNFYTLRDLLAQ-GrrPEVIRYFLLA-AHYSQKVNYTADAL---HQAE-AG--------- 325
Cdd:COG0143 314 KVFAH-GFLTVEGEKMSKSRGNVIDPDDLLDRyG--PDALRYYLLReVPFGQDGDFSWEDFvarVNSDlANdlgnlasrt 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504614693 326 ---VEKFY-GLLARLDRLQKIDAAADATLAATAKEAREKFmaelaDDLNTPRALAVVLEFIRAANTNIDAK 392
Cdd:COG0143 391 lsmIHKYFdGKVPEPGELTEADEELLAEAEAALEEVAEAM-----EAFEFRKALEEIMALARAANKYIDET 456
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
35-306 |
2.37e-05 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 46.37 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 35 HIGNFRSYLFADVLNRTLRLAGYQVQHamnLTDVDD---KTIKGAIALSeKEPGKYADLkqalaaytepYTEAFFADLKT 111
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLF---VTGTDEhgtKIEQKAEEEG-VTPQELCDK----------YHEIFKDLFKW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 112 LNVcKFDFHPRATD--YIPAMLDLVDRLIAQGVAYEQDGSVYYRIS------EKKD----YGKLSRID------LEKNKT 173
Cdd:cd00814 82 LNI-SFDYFIRTTSprHKEIVQEFFKKLYENGYIYEGEYEGLYCVScerflpEWREeehyFFRLSKFQdrllewLEKNPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 174 G---------TRYNTDE--YDKDDVRDFVLW-----KAEGKEGVHWH-------SSHG-----DGRPGWHL-ECSAMIHE 224
Cdd:cd00814 161 FiwpenarneVLSWLKEglKDLSITRDLFDWgipvpLDPGKVIYVWFdaligyiSATGyyneeWGNSWWWKdGWPELVHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 225 IFKgaiDI---HTggvdLIFPhheneiaQSESGYGDGFVKHWVHCEHLLVDNKKMSKSAGNFYTLRDLLAQGrRPEVIRY 301
Cdd:cd00814 241 IGK---DIirfHA----IYWP-------AMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRY 305
|
....*
gi 504614693 302 FLLAA 306
Cdd:cd00814 306 YLLRE 310
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
35-304 |
6.02e-05 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 45.53 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 35 HIGNFRSYLFADVLNRTLRLAGYQVQ---HamnltdVDD--KTIkGAIALSekepgkYADLKQALAAYTEpytEAFFADL 109
Cdd:PRK01611 127 HVGHLRSAVIGDALARILEFAGYDVTreyY------VNDagTQI-GMLIAS------LELLWRKAVDISL---DEIKEDL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 110 KTLNVcKFD--FHPRATDYIPAMLDLVDRLIAQGVAY-EQDGSVYYRisekkdygklsridleknktgtrynTDEYDKDD 186
Cdd:PRK01611 191 DRLGV-HFDvwFSESELYYNGKVDEVVEDLKEKGLLYvESDGALWVR-------------------------LTEFGDDK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 187 vrDFVLWKAegkegvhwhsshgDGRP-------GWHLECsamiHEIFKGAIDIHtgGVDlifphHENEIAQSES-----G 254
Cdd:PRK01611 245 --DRVLIKS-------------DGTYtyftrdiAYHLYK----FERFDRVIYVV--GAD-----HHGHFKRLKAalkalG 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504614693 255 YGDGFVKHwvhCEHLLV------DNKKMSKSAGNFYTLRDLL--AQGRRPEVI--------------RYFLL 304
Cdd:PRK01611 299 YDPDALEV---LLHQMVglvrggEGVKMSTRAGNVVTLDDLLdeAVGRARELIeekeiaeavgidavRYFDL 367
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
268-288 |
5.38e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 42.75 E-value: 5.38e-04
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
28-152 |
6.39e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 41.89 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 28 PTVYNYAHIGNFRSYLFADVLNRTLRLAGYQVQHamnLTDVDDKTIKgaIALSEKEPGKYAdlkqalAAYTEPYTEAFFA 107
Cdd:pfam09334 8 PYANGPPHLGHLYSYIPADIFARYLRLRGYDVLF---VCGTDEHGTP--IELKAEKEGITP------EELVDRYHEIHRE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 504614693 108 DLKTLNVcKFDFHPRATD--YIPAMLDLVDRLIAQGVAYEQDGSVYY 152
Cdd:pfam09334 77 DFKKFNI-SFDDYGRTTSerHHELVQEFFLKLYENGYIYEKEIEQFY 122
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
268-390 |
7.60e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 42.09 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 268 HLLVDNKKMSKSAGNF---YTLRDllAQGRrpEVIRYFLL-AAHYSQKVNYTADALHQ---------------------- 321
Cdd:PRK12267 292 WWLMKDGKMSKSKGNVvdpEELVD--RYGL--DALRYYLLrEVPFGSDGDFSPEALVErinsdlandlgnllnrtvamin 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504614693 322 --------AEAGVEKFYGLLARLdrlqkidaaadatlaatAKEAREKFMaELADDLNTPRALAVVLEFIRAANTNID 390
Cdd:PRK12267 368 kyfdgeipAPGNVTEFDEELIAL-----------------AEETLKNYE-ELMEELQFSRALEEVWKLISRANKYID 426
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
274-305 |
1.89e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 40.57 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|..
gi 504614693 274 KKMSKSAGNFYTLRDLLAQGrRPEVIRYFLLA 305
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYA-PPESLRLFMFA 309
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
35-290 |
2.75e-03 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 40.13 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 35 HIGNFRSYLFADVLNRTLRLAGYQV-----------QHAM------------------NLTDVDDKTIKGAIALSEKEPg 85
Cdd:COG0018 132 HVGHLRGAVIGDALARILEAAGYDVtrenyindagtQIGKlalslerygeeeiepeskPDGYLGDLYVKFHKEYEEDPE- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 86 kYADLKQALAAYTEPYTE---------------AFFADLKTLNVcKFD--FHPRATDYIPAMLDLVDRLIAQGVAYEQDG 148
Cdd:COG0018 211 -LEDIARELLAKLEPGDEealelwkkavdwsleEIKEDLKRLGV-EFDvwFSESSLYDSGAVEEVVEELKEKGLLYESDG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504614693 149 SVYYRISEkkdYGKLS-RIDLEKNKTGTrYNTdeydkddvRD--FVLWKAEgkegvhwhsshgdgRPGwhlecsamihei 225
Cdd:COG0018 289 ALWVRLTE---FGDDKdRVLVKSDGTYT-YFT--------TDiaYHLYKFE--------------RYG------------ 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504614693 226 FKGAIDI----HTGGVDLIFphhenEIAQsESGYGDGFvkhwvHCEHLLV------DNKKMSKSAGNFYTLRDLL 290
Cdd:COG0018 331 FDRVIYVvgadQHGHFKRLF-----AALK-ALGYDPAK-----DLEHLLFgmvnlrDGEKMSTRAGTVVTLDDLL 394
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
270-336 |
2.91e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 40.24 E-value: 2.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504614693 270 LVDNKKMSKSAGNFYTLRDLLAQ-GrrPEVIRYFLL-AAHYSQKVNYTADALHQAEAGVEKFYGLLARL 336
Cdd:PRK12300 572 LLEGKKMSKSKGNVIPLRKAIEEyG--ADVVRLYLTsSAELLQDADWREKEVESVRRQLERFYELAKEL 638
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
268-306 |
3.89e-03 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 39.15 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504614693 268 HLLVDNKKMSKSAGNFYTLRDLLAQ-GrrPEVIRYFLLAA 306
Cdd:cd00812 268 MVLLEGEKMSKSKGNVVTPDEAIKKyG--ADAARLYILFA 305
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
267-306 |
6.16e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 38.81 E-value: 6.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504614693 267 EHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFLLAA 306
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARN 354
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
264-312 |
6.81e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 38.98 E-value: 6.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 504614693 264 VHcEHLLVDNKKMSKSAGNFYTLRDLLAQgRRPEVIRYFlLAAHYSQKV 312
Cdd:PRK00133 319 AH-GFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYY-LAAKLPETI 364
|
|
| |
