|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
47-457 |
1.50e-175 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 506.49 E-value: 1.50e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 47 DLFMTDP-LSPGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFkveTTDEEKEE 125
Cdd:COG0441 251 DLFHFQEeVGPGLPFWHPKGAIIRRELEDYIREKHR-KAGYQEVKTPHILDRELWETSGHWDHYRENMF---PTESDGEE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 126 YGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLIDI 205
Cdd:COG0441 327 YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 206 VYnKIFPFvkggsgaeSNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKT 285
Cdd:COG0441 407 VY-KDFGF--------EDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 286 HQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKnvqQLDM 365
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDK---HADY 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 366 CTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRksfEKL 445
Cdd:COG0441 555 AKEVAKKLRAA--------------GIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGG---DLG 617
|
410
....*....|..
gi 6322654 446 TMSqiWEKFIEL 457
Cdd:COG0441 618 TMS--LDEFIAR 627
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
44-347 |
3.84e-169 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 477.43 E-value: 3.84e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 44 QRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVEttdEEK 123
Cdd:cd00771 8 ELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQR-KRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE---EED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 124 EEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLI 203
Cdd:cd00771 84 EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 204 DIVYNKIFPFvkggsgaesNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLR 283
Cdd:cd00771 164 KEVYSDFGFF---------DYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322654 284 KTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNP 347
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
41-462 |
3.25e-166 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 484.27 E-value: 3.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 41 MVSQRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKlQQKFKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETtd 120
Cdd:PLN02908 296 LLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR-EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEI-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 121 eEKEEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSL 200
Cdd:PLN02908 373 -EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 201 KLIDIVYnKIFPFvkggsgaesNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTD 280
Cdd:PLN02908 452 DFLDYVY-EVFGF---------TYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSD 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 281 HLRKTHQVATIQLDFQLPERFDLKFKDQDNSYK-RPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKN 359
Cdd:PLN02908 522 ALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKS 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 360 VqqlDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNR 439
Cdd:PLN02908 602 Q---DYAEEVRAQLHAA--------------GFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNV 664
|
410 420
....*....|....*....|...
gi 6322654 440 KSFEKlTMSQIWEKFIELEKNYK 462
Cdd:PLN02908 665 VHGEK-KIEELLTEFKEERAEFK 686
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
45-456 |
6.11e-150 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 438.68 E-value: 6.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 45 RQDLFMTDPLS-PGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFkvETTDEEK 123
Cdd:TIGR00418 178 ELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQI-KYGYMEVETPIMYDLELWEISGHWDNYKERMF--PFTELDN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 124 EEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLI 203
Cdd:TIGR00418 255 REFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 204 DIVYNKiFPFvkggsgaeSNYFINFSTR-PDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHL 282
Cdd:TIGR00418 335 QKVYSD-FGF--------SFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDFAFKDAL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 283 RKTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKnvqQ 362
Cdd:TIGR00418 406 GREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNER---H 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 363 LDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKsf 442
Cdd:TIGR00418 483 LDYAKKVAQKLKKA--------------GIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQK-- 546
|
410
....*....|....
gi 6322654 443 eKLTMSqiWEKFIE 456
Cdd:TIGR00418 547 -LEKMS--LDEFLE 557
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
114-337 |
1.07e-60 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 196.09 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 114 FKVEttDEEKEEYGLKPMNCPGHCLIFGKK-DRSYNeLPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQV 192
Cdd:pfam00587 1 YKVE--DENGDELALKPTNEPGHTLLFREEgLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 193 KSEIFNSLKLIDIVYNKIFPFVkggsgaesnyfinfstrpdhfigdlkvwnhaeQVLKEIleesgkpwklNPGDGAFYGP 272
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEV--------------------------------RVVRLS----------NSDGSAFYGP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322654 273 KLDIMVTDH-LRKTHQVATIQLD-FQLPERFDLKFKDQDNSYKRPIMIHRATFGsIERFMALLIDSN 337
Cdd:pfam00587 116 KLDFEVVFPsLGKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
47-457 |
1.50e-175 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 506.49 E-value: 1.50e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 47 DLFMTDP-LSPGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFkveTTDEEKEE 125
Cdd:COG0441 251 DLFHFQEeVGPGLPFWHPKGAIIRRELEDYIREKHR-KAGYQEVKTPHILDRELWETSGHWDHYRENMF---PTESDGEE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 126 YGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLIDI 205
Cdd:COG0441 327 YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 206 VYnKIFPFvkggsgaeSNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKT 285
Cdd:COG0441 407 VY-KDFGF--------EDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 286 HQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKnvqQLDM 365
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDK---HADY 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 366 CTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRksfEKL 445
Cdd:COG0441 555 AKEVAKKLRAA--------------GIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGG---DLG 617
|
410
....*....|..
gi 6322654 446 TMSqiWEKFIEL 457
Cdd:COG0441 618 TMS--LDEFIAR 627
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
44-347 |
3.84e-169 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 477.43 E-value: 3.84e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 44 QRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVEttdEEK 123
Cdd:cd00771 8 ELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQR-KRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE---EED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 124 EEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLI 203
Cdd:cd00771 84 EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 204 DIVYNKIFPFvkggsgaesNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLR 283
Cdd:cd00771 164 KEVYSDFGFF---------DYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322654 284 KTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNP 347
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
41-462 |
3.25e-166 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 484.27 E-value: 3.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 41 MVSQRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKlQQKFKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETtd 120
Cdd:PLN02908 296 LLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR-EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEI-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 121 eEKEEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSL 200
Cdd:PLN02908 373 -EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 201 KLIDIVYnKIFPFvkggsgaesNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTD 280
Cdd:PLN02908 452 DFLDYVY-EVFGF---------TYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSD 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 281 HLRKTHQVATIQLDFQLPERFDLKFKDQDNSYK-RPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKN 359
Cdd:PLN02908 522 ALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKS 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 360 VqqlDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNR 439
Cdd:PLN02908 602 Q---DYAEEVRAQLHAA--------------GFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNV 664
|
410 420
....*....|....*....|...
gi 6322654 440 KSFEKlTMSQIWEKFIELEKNYK 462
Cdd:PLN02908 665 VHGEK-KIEELLTEFKEERAEFK 686
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
45-456 |
6.11e-150 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 438.68 E-value: 6.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 45 RQDLFMTDPLS-PGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFkvETTDEEK 123
Cdd:TIGR00418 178 ELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQI-KYGYMEVETPIMYDLELWEISGHWDNYKERMF--PFTELDN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 124 EEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLI 203
Cdd:TIGR00418 255 REFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 204 DIVYNKiFPFvkggsgaeSNYFINFSTR-PDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHL 282
Cdd:TIGR00418 335 QKVYSD-FGF--------SFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDFAFKDAL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 283 RKTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKnvqQ 362
Cdd:TIGR00418 406 GREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNER---H 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 363 LDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKsf 442
Cdd:TIGR00418 483 LDYAKKVAQKLKKA--------------GIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQK-- 546
|
410
....*....|....
gi 6322654 443 eKLTMSqiWEKFIE 456
Cdd:TIGR00418 547 -LEKMS--LDEFLE 557
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
47-462 |
3.13e-122 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 370.23 E-value: 3.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 47 DLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQkFKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETTDEEkeeY 126
Cdd:PRK12444 255 ELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQ-KEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFSEVDNKS---F 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 127 GLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLIDIV 206
Cdd:PRK12444 331 ALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 207 YnKIFPFvkggsgaesNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKTH 286
Cdd:PRK12444 411 Y-KTFGF---------EYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSH 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 287 QVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNtkNVQQLDMC 366
Cdd:PRK12444 481 QCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVS--NAVHVQYA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 367 TALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKSfEKLT 446
Cdd:PRK12444 559 DEVADKLAQA--------------GIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS-EVIE 623
|
410
....*....|....*.
gi 6322654 447 MSQIWEKFIELEKNYK 462
Cdd:PRK12444 624 LDMFVESIKEEIKNRK 639
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
42-438 |
4.62e-90 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 286.02 E-value: 4.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 42 VSQRQDLF-MTDPLSPGSMFFLPNGAKIFNKLIEFMKlQQKFKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFkvETTD 120
Cdd:PLN02837 222 LGQDLDLFsIQDDAGGGLVFWHPKGAIVRHIIEDSWK-KMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMY--DQMD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 121 EEKEEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSL 200
Cdd:PLN02837 299 IEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVL 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 201 KLIDIVYNKiFPFVKggsgaesnYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTD 280
Cdd:PLN02837 379 DLTEEILKQ-FGFSK--------YEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIED 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 281 HLRKTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVnTKNv 360
Cdd:PLN02837 450 ALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPV-TDN- 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322654 361 qQLDMCTALQKKLR-NELEADdmepvplndwhfnvdlDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDN 438
Cdd:PLN02837 528 -ELEYCKEVVAKLKaKGIRAE----------------VCHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHG 589
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
114-337 |
1.07e-60 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 196.09 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 114 FKVEttDEEKEEYGLKPMNCPGHCLIFGKK-DRSYNeLPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQV 192
Cdd:pfam00587 1 YKVE--DENGDELALKPTNEPGHTLLFREEgLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 193 KSEIFNSLKLIDIVYNKIFPFVkggsgaesnyfinfstrpdhfigdlkvwnhaeQVLKEIleesgkpwklNPGDGAFYGP 272
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEV--------------------------------RVVRLS----------NSDGSAFYGP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322654 273 KLDIMVTDH-LRKTHQVATIQLD-FQLPERFDLKFKDQDNSYKRPIMIHRATFGsIERFMALLIDSN 337
Cdd:pfam00587 116 KLDFEVVFPsLGKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
52-457 |
9.36e-38 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 145.40 E-value: 9.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 52 DPLS-PGSMFFLPNGaKIFNKLIEFMKLQQKFKFGFNEVVTPLIYK---KTLWEksgHWENYADDMFKVETtdeEKEEYG 127
Cdd:PRK03991 212 EPASdVGHMRYYPKG-RLIRDLLEDYVYNLVVELGAMPVETPIMYDlshPAIRE---HADKFGERQYRVKS---DKKDLM 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 128 LKPMNCPGHCLIfgKKDR--SYNELPLR---FSDFSplHRNEASGALSGLTRLRKFHQDDGHIFCTP-SQVKSEIFNSLK 201
Cdd:PRK03991 285 LRFAACFGQFLM--LKDMtiSYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 202 LIdivynkifpfVKGGSGAESNY--FINFsTRpdhfigdlKVWNHAEQVLKEILEESGKPWKLNPGDGAFY--GPKLDIM 277
Cdd:PRK03991 361 MI----------LETGEDLGRDYevAIRF-TE--------DFYEENKDWIVELVKREGKPVLLEILPERKHywVLKVEFA 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 278 VTDHLRKTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFM-ALL----IDSNEG---RWPFWLNPYQ 349
Cdd:PRK03991 422 FIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIyALLekaaKEEEEGkvpMLPTWLSPTQ 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 350 AVIIPVNTKNvqqLDMCTALQKKLRNELeaddmepvplndwhFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQ 429
Cdd:PRK03991 502 VRVIPVSERH---LDYAEEVADKLEAAG--------------IRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESG 564
|
410 420
....*....|....*....|....*...
gi 6322654 430 KYNIRERdnRKSfEKLTMSQiwEKFIEL 457
Cdd:PRK03991 565 KLTVTIR--EES-EKVEMTL--EELIER 587
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
65-334 |
1.40e-26 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 107.09 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 65 GAKIFNKLIEFMKLQQKFKfGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETTDEEK--EEYGLKPMNCPGHCLIFGK 142
Cdd:cd00670 1 GTALWRALERFLDDRMAEY-GYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELrdTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 143 KDRSYNELPLRFSDFSPLHRNEASGAlSGLTRLRKFHQDDGHIFCTPSQVKsEIFNslKLIDIVYnkifpfvKGGSGAES 222
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAE-EERR--EWLELAE-------EIARELGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 223 NYFINFSTRPDHFIGDlkvwnhaeqvlkeileesgkpwklNPGDGAFYGPKLDI-MVTDHLRKTHQVATIQLDFQLPERF 301
Cdd:cd00670 149 PVRVVVADDPFFGRGG------------------------KRGLDAGRETVVEFeLLLPLPGRAKETAVGSANVHLDHFG 204
|
250 260 270
....*....|....*....|....*....|...
gi 6322654 302 DLKFKDQDNSYKRPIMIHRatFGSIERFMALLI 334
Cdd:cd00670 205 ASFKIDEDGGGRAHTGCGG--AGGEERLVLALL 235
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
347-459 |
4.55e-24 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 95.65 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 347 PYQAVIIPVNTKnvqQLDMCTALQKKLRNELeaddmepvplndwhFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEV 426
Cdd:cd00860 1 PVQVVVIPVTDE---HLDYAKEVAKKLSDAG--------------IRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEV 63
|
90 100 110
....*....|....*....|....*....|...
gi 6322654 427 QLQKYNIRERDNRKSfEKLTMsqiwEKFIELEK 459
Cdd:cd00860 64 ETGTVSVRTRDGGDL-GSMSL----DEFIEKLK 91
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
67-329 |
3.43e-19 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 85.63 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 67 KIFNKLIEFMKlqqkfKFGFNEVVTPLIYKKTLWEKSGHWENYAddmfkVETTDEEKEEYGLKPMNCPGHCLIFGKKDRS 146
Cdd:cd00768 4 KIEQKLRRFMA-----ELGFQEVETPIVEREPLLEKAGHEPKDL-----LPVGAENEEDLYLRPTLEPGLVRLFVSHIRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 147 yneLPLRFSDFSPLHRNEASGAlsGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLIdivynkifpfvkggsgaesnyfi 226
Cdd:cd00768 74 ---LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELT----------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 227 nfstrpdhfigdLKVWNHAEQVLKEILEEsgKPWKlnPGDGAFYGPKLDIMVTDHLRKTHQVATIQLDFQLPER-FDLKF 305
Cdd:cd00768 126 ------------EELLRALGIKLDIVFVE--KTPG--EFSPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYF 189
|
250 260
....*....|....*....|....
gi 6322654 306 KDQDNSYKRPIMIHRAtfGSIERF 329
Cdd:cd00768 190 LDEALEYRYPPTIGFG--LGLERL 211
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
349-457 |
3.77e-17 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 76.47 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 349 QAVIIPVNTKNVQQLDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQL 428
Cdd:pfam03129 1 QVVVIPLGEKAEELEEYAQKLAEELRAA--------------GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE 66
|
90 100
....*....|....*....|....*....
gi 6322654 429 QKYNIRERDNRKSfEKLTMSQIWEKFIEL 457
Cdd:pfam03129 67 GTVTVRRRDTGEQ-ETVSLDELVEKLKEL 94
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
50-443 |
1.03e-11 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 66.72 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 50 MTDPLSPGSMFFLPNGAKIFNKLI----EFMKlqqkfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVetTDEEKEE 125
Cdd:COG0442 31 LIRKLASGIYTYLPLGYRVLEKIEaivrEEMK-----RTGAQEVLMPLLQPAELWEESGRWEGFGPELARV--TDRLERE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 126 YGLkpmnCPGH----CLIFGKKDRSYNELPLRF----SDFsplhRNEASgALSGLTRLRKFHQDDGHIF-CTPSQVKSEi 196
Cdd:COG0442 104 FCL----GPTHeeviTDLVRNEIKSYRDLPLLLyqiqTKF----RDEIR-PRFGLLRTREFLMKDAYSFhATEEELDEE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 197 fnSLKLIDiVYNKIF-----PFVK--------GGSGAE------------------SNYFIN------------------ 227
Cdd:COG0442 174 --YQKMLD-AYERIFerlglPVRAveadsgaiGGSESHefmvladsgedtivycdaCDYAANiekaealappaeraeptk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 228 ----FST-------------------------------------RPDHFIGDLKVWNHAEQVLKEIL--EESGKPWKLNP 264
Cdd:COG0442 251 eleaVATpgaktieevaeflgvpaektvktlvykadgelvavlvRGDHELNEIKLENLLGASELELAteEEIEAALGAVP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 265 GdgaFYGP-KLDIMVT-DH-----------------------------------LRKTH------------------QVA 289
Cdd:COG0442 331 G---FLGPvGLGVPYIaDRsvagmsnfvcganeddyhytnvnwgrdfpvdevadLRNVVegdpcpdcggllqdgrgiEVG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 290 TIqldFQL----PERFDLKFKDQDNSYKRPIMihrATFG-SIERFMALLIDSN---EG-RWPFWLNPYQAVIIPVNTKNV 360
Cdd:COG0442 408 HI---FKLgtkySKAMDATFLDENGKEQPVWM---GCYGiGVTRLIAAAIEQHhddKGiIWPPAIAPFQVVIVPINMKDE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 361 QQLDMCtalqKKLRNELEADDMEpvplndwhfnVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRK 440
Cdd:COG0442 482 AVLEAA----EELYAELKAAGID----------VLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGE 547
|
...
gi 6322654 441 SFE 443
Cdd:COG0442 548 KEE 550
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
53-221 |
2.89e-10 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 60.67 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 53 PLSPGSMFFLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVetTDEEKEEYGLKPMN 132
Cdd:cd00779 18 QTSSGLYSWLPLGLRVLKKIENIIREEMN-KIGAQEILMPILQPAELWKESGRWDAYGPELLRL--KDRHGKEFLLGPTH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 133 CPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALsGLTRLRKFHQDDGHIFCTPsqvKSEIFNSLKLIDIVYNKIF- 211
Cdd:cd00779 95 EEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFDID---EESLEETYEKMYQAYSRIFk 170
|
170 180
....*....|....*....|..
gi 6322654 212 ----PFVK--------GGSGAE 221
Cdd:cd00779 171 rlglPFVKveadsgaiGGSLSH 192
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
57-202 |
1.90e-08 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 55.64 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 57 GSMF-FLPN-GAKIFNKLIEFM--KLQQKfkfGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETTDEekeeyglkpmn 132
Cdd:cd00770 41 GSRFyYLKGdGALLERALINFAldFLTKR---GFTPVIPPFLVRKEVMEGTGQLPKFDEQLYKVEGEDL----------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 133 cpghCLI----------FGKKDRSYNELPLRFSDFSPLHRNEASGA---LSGLTRLRKFHQDDGHIFCTPSQVK------ 193
Cdd:cd00770 107 ----YLIataevplaalHRDEILEEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRVHQFEKVEQFVFTKPEESWeeleel 182
|
170
....*....|...
gi 6322654 194 ----SEIFNSLKL 202
Cdd:cd00770 183 isnaEEILQELGL 195
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
347-456 |
6.05e-08 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 50.28 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 347 PYQAVIIPVNTKNVQQLDMCTALQKKLRNEleaddmepvplndwHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEV 426
Cdd:cd00861 1 PFDVVIIPMNMKDEVQQELAEKLYAELQAA--------------GVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSA 66
|
90 100 110
....*....|....*....|....*....|
gi 6322654 427 QLQKYNIRerdNRKSFEKLTMSQiwEKFIE 456
Cdd:cd00861 67 AEGIVEIK---VRKTGEKEEISI--DELLE 91
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
57-216 |
6.45e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 47.59 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 57 GSMFFLPNGAKIFNKLIEFmkLQQKFK-FGFNEVVTPLIYKKTLWEK-SGHWENYADDMFKVETTDEEK--EEYGLKPMN 132
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKI--LDKEIKeTGHENVYFPLLIPESELEKeKEHIEGFAPEVAWVTHGGLEEleEPLALRPTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 133 CPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSgLTRLRKFHQDDGH-IFCTPSQVKSEIFNSLKLIDIVYNKI- 210
Cdd:cd00778 101 ETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRP-FLRTREFLWQEGHtAHATEEEAEEEVLQILDLYKEFYEDLl 179
|
....*..
gi 6322654 211 -FPFVKG 216
Cdd:cd00778 180 aIPVVKG 186
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
347-448 |
7.37e-06 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 44.31 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 347 PYQAVIIPVNTKNVQQLDMCtalqKKLRNELEADDMEpvplndwhfnVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEV 426
Cdd:cd00738 1 PIDVAIVPLTDPRVEAREYA----QKLLNALLANGIR----------VLYDDRERKIGKKFREADLRGVPFAVVVGEDEL 66
|
90 100
....*....|....*....|..
gi 6322654 427 QLQKYNIRERDNRksfEKLTMS 448
Cdd:cd00738 67 ENGKVTVKSRDTG---ESETLH 85
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
295-459 |
1.50e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 44.30 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 295 FQL----PERFDLKFKDQDNSYKRPIMihratfGS----IERFMALLI----DSNEGRWPFWLNPYQAVIIPVNTKNVQQ 362
Cdd:PRK09194 410 FQLgtkySEAMNATVLDENGKAQPLIM------GCygigVSRLVAAAIeqnhDEKGIIWPKAIAPFDVHIVPVNMKDEEV 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 363 LDMCTalqkKLRNELEADDMEpvplndwhfnVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKSf 442
Cdd:PRK09194 484 KELAE----KLYAELQAAGIE----------VLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEK- 548
|
170
....*....|....*..
gi 6322654 443 EKLTMSQIWEKFIELEK 459
Cdd:PRK09194 549 EEVPVDELVEFLKALKK 565
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
33-179 |
4.19e-04 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 42.70 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 33 ATPATMTSMVSQRQDLFMTDP-------------LSPGSMFFLPNGAKIFNKLIEFMKLQQKFKFGFNEVVTPLIYKKTL 99
Cdd:PRK00960 177 AEPGTIVSESKKREITFDGDPteeaeklgwvkrfPGRGQWFYTPPMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 100 WEKSGH--------------------WENYADDMF--KVETTDEEKEE-----YGLKPMNCPGHCLIFGKKDRSYNELPL 152
Cdd:PRK00960 257 MYKMRYleglpegmyyvcppkrdpeyFEEFVDEMMvkKEVPIEKLKEKlrdpgYVLAPAQCEPFYQFFQGETVDVDELPI 336
|
170 180
....*....|....*....|....*...
gi 6322654 153 RFSDFS-PLHRNEaSGALSGLTRLRKFH 179
Cdd:PRK00960 337 KFFDRSgWTYRWE-GGGAHGLERVNEFH 363
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
57-200 |
6.33e-04 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 41.59 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 57 GSMFFLPNGAKIFNKLIEFmkLQQKFK-FGFNEVVTPLIYKKTLWEKSGHWENYADD---MFKVETTDEEKEEYGLKPMN 132
Cdd:cd00772 23 GIINFLPLAKAILDKIENV--LDKMFKeHGAQNALFPFFILASFLEKEAEHDEGFSKelaVFKDAGDEELEEDFALRPTL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322654 133 CPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASgALSGLTRLRKFHQDDGHIF-CTPSQVKSEIFNSL 200
Cdd:cd00772 101 EENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNML 168
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
67-180 |
6.44e-04 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 41.43 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 67 KIFNKLIEFMKlqqkfKFGFNEVVTPLI-YKKTLWEKSGhwENYADDMFKVEttDEEKEEYGLKPMNCPGHCLIFGKKdR 145
Cdd:cd00773 7 YIEDTLREVFE-----RYGYEEIDTPVFeYTELFLRKSG--DEVSKEMYRFK--DKGGRDLALRPDLTAPVARAVAEN-L 76
|
90 100 110
....*....|....*....|....*....|....*
gi 6322654 146 SYNELPLRFSDFSPLHRNEASGALsgltRLRKFHQ 180
Cdd:cd00773 77 LSLPLPLKLYYIGPVFRYERPQKG----RYREFYQ 107
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
304-448 |
1.70e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 40.61 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 304 KFKDQDNsykRPIMIHRATFG-SIERFMALLI----DSNEGRWPFWLNPYQAVIIPVNTKNvqqlDMCTALQKKLRNELE 378
Cdd:PRK12325 300 KVQGPDG---KEVPVHMGSYGiGVSRLVAAIIeashDDKGIIWPESVAPFKVGIINLKQGD----EACDAACEKLYAALS 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 379 ADDMEPVplndwhfnvdLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVqlqKYNIRERDNRKSFEKLTMS 448
Cdd:PRK12325 373 AAGIDVL----------YDDTDERPGAKFATMDLIGLPWQIIVGPKGL---AEGKVELKDRKTGEREELS 429
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
61-152 |
5.72e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 39.07 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322654 61 FLPNGAKIFNKLIEFMKLQQKfKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVetTDEEKEEYGLKPMNCPGHCLIF 140
Cdd:PRK12325 42 WLPLGLKVLKKIENIVREEQN-RAGAIEILMPTIQPADLWRESGRYDAYGKEMLRI--KDRHDREMLYGPTNEEMITDIF 118
|
90
....*....|..
gi 6322654 141 GKKDRSYNELPL 152
Cdd:PRK12325 119 RSYVKSYKDLPL 130
|
|
| |
