|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
2-575 |
0e+00 |
|
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: 814.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 2 DKEQFLHVYRHSLAHVLAKAVIEVFgKETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEISK 81
Cdd:COG0441 63 DDEEGLEILRHSAAHLLAQAVKRLY-PDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 82 KAALELFK--NQKFKVELIEDLPEDEILTIYRTGDdFVDLCRGPHVENSA-----ALLSVAwqlrsmsGSYWRGDEKRDQ 154
Cdd:COG0441 142 EEAIELFKekGEPYKVELIEDIPEDEEISLYRQGE-FVDLCRGPHVPSTGkikafKLLSVA-------GAYWRGDEKNKM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 155 LTRIYAYAFPTKEELKAHLAFIKDAQERDHKKIGPQLDLFMF-DETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEV 233
Cdd:COG0441 214 LQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFqEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 234 SAPVINNKRLWVTSGHWAHYKENMFLIpgadgDIEaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKS 313
Cdd:COG0441 294 KTPHILDRELWETSGHWDHYRENMFPT-----ESD-GEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 314 GELNGLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMS-CKAELSTRPDDFMGDIETWNIAEKELKEILDR 392
Cdd:COG0441 368 GALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 393 KygeG-NYEVNEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGV 471
Cdd:COG0441 448 L---GlEYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGI 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 472 LIENFKGAFPFWLSPVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADknmrEKIkGFK-----HYKDPYILVLGDK 546
Cdd:COG0441 525 LIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRN----EKI-GYKireaqLQKVPYMLVVGDK 599
|
570 580
....*....|....*....|....*....
gi 402282425 547 EAEENTVSINVRGtNEQLKDVPLDTFIEM 575
Cdd:COG0441 600 EVENGTVSVRRRG-GGDLGTMSLDEFIAR 627
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-577 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 626.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 1 MDKEQFLHVYRHSLAHVLAKAVIEVFGkETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEIS 80
Cdd:PRK12444 66 IDSNEGVEIARHSAAHILAQAVKRLYG-DVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 81 KKAALELFK--NQKFKVELIEDLPEDEILTIYRTGDdFVDLCRGPHVENSAALlsVAWQLRSMSGSYWRGDEKRDQLTRI 158
Cdd:PRK12444 145 REEAAKLFQemNDRLKLELLEAIPSGESITLYKQGE-FVDLCRGPHLPSTGYL--KAFQLTHVSGAYWRGDSNNQVLQRI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 159 YAYAFPTKEELKAHLAFIKDAQERDHKKIGPQLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVI 238
Cdd:PRK12444 222 YGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 239 NNKRLWVTSGHWAHYKENMFLIpgadgdiEADDT-FAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELN 317
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMYFS-------EVDNKsFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 318 GLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMSCKAELSTRPDDFMGDIETWNIAEKELKEILDR-KYge 396
Cdd:PRK12444 375 GLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSlNY-- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 397 gNYEVNEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENF 476
Cdd:PRK12444 453 -KYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHF 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 477 KGAFPFWLSPVQVGIVPI-RPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSI 555
Cdd:PRK12444 532 GGAFPAWLAPVQVKVIPVsNAVHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNV 611
|
570 580
....*....|....*....|..
gi 402282425 556 NVRGtNEQLKDVPLDTFIEMCR 577
Cdd:PRK12444 612 RKYG-EEKSEVIELDMFVESIK 632
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
11-577 |
0e+00 |
|
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: 602.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 11 RHSLAHVLAKAVIEVFgKETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEISKKAALELFKN 90
Cdd:TIGR00418 1 RHSIAHLLAEALKQLY-PDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 91 QK-FKVELIEDLPEDEILTIYRTGDDFVDLCRGPHVENSAalLSVAWQLRSMSGSYWRGDEKRDQLTRIYAYAFPTKEEL 169
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGKAFVDLCKGPHLPNTS--FIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 170 KAHLAFIKDAQERDHKKIGPQLDLFMFD-ETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSG 248
Cdd:TIGR00418 158 AAYLLRLEEAKKRDHRKLGKELELFSFEpEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 249 HWAHYKENMFLIPGADgdieaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQD 328
Cdd:TIGR00418 238 HWDNYKERMFPFTELD-----NREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 329 DDHTFLMEDQIAAEMGDIMDIADEIYSTLGMS-CKAELSTR-PDDFMGDIETWNIAEKELKEILDRKygEGNYEVNEGDG 406
Cdd:TIGR00418 313 DAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSfDKYELSTRdPEDFIGEDELWEKAEAALEEALKEL--GVPYEIDPGRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 407 AFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENFKGAFPFWLSP 486
Cdd:TIGR00418 391 AFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 487 VQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGtNEQLKD 566
Cdd:TIGR00418 471 VQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRK-GQKLEK 549
|
570
....*....|.
gi 402282425 567 VPLDTFIEMCR 577
Cdd:TIGR00418 550 MSLDEFLEKLR 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
182-486 |
5.27e-148 |
|
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: 428.51 E-value: 5.27e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 182 RDHKKIGPQLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENMFLIp 261
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 262 gadgdIEADDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQDDDHTFLMEDQIAA 341
Cdd:cd00771 80 -----EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 342 EMGDIMDIADEIYSTLGM-SCKAELSTRPDDFMGDIETWNIAEKELKEILDRKygEGNYEVNEGDGAFYGPKIDLKMKDA 420
Cdd:cd00771 155 EIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEI--GLPYEINEGEGAFYGPKIDFHVKDA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402282425 421 LGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENFKGAFPFWLSP 486
Cdd:cd00771 233 LGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
266-476 |
9.81e-29 |
|
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: 112.89 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 266 DIEADDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQDDDHTFLMEDQIAAEMGD 345
Cdd:pfam00587 4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 346 IMDIADEIYSTLGMSckaelstrpddfmgdietwniaEKELKEILDRKygegnyevnegdGAFYGPKIDLKMKD-ALGRE 424
Cdd:pfam00587 84 YIKLIDRVYSRLGLE----------------------VRVVRLSNSDG------------SAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 402282425 425 WQVGTLQLD-FQLPQNFDLKYIAKDGSHKQPVVLHRAIFGsMERFIGVLIENF 476
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
107-158 |
3.54e-07 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 46.61 E-value: 3.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 402282425 107 LTIYRTGDDFVDLCRGPHVENSAALLSVAwqLRSMSGSYWRgdekrdqLTRI 158
Cdd:smart00863 1 VRVVSIGDFSVELCGGTHVPNTGEIGAFK--ILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
2-575 |
0e+00 |
|
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: 814.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 2 DKEQFLHVYRHSLAHVLAKAVIEVFgKETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEISK 81
Cdd:COG0441 63 DDEEGLEILRHSAAHLLAQAVKRLY-PDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 82 KAALELFK--NQKFKVELIEDLPEDEILTIYRTGDdFVDLCRGPHVENSA-----ALLSVAwqlrsmsGSYWRGDEKRDQ 154
Cdd:COG0441 142 EEAIELFKekGEPYKVELIEDIPEDEEISLYRQGE-FVDLCRGPHVPSTGkikafKLLSVA-------GAYWRGDEKNKM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 155 LTRIYAYAFPTKEELKAHLAFIKDAQERDHKKIGPQLDLFMF-DETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEV 233
Cdd:COG0441 214 LQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFqEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 234 SAPVINNKRLWVTSGHWAHYKENMFLIpgadgDIEaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKS 313
Cdd:COG0441 294 KTPHILDRELWETSGHWDHYRENMFPT-----ESD-GEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 314 GELNGLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMS-CKAELSTRPDDFMGDIETWNIAEKELKEILDR 392
Cdd:COG0441 368 GALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 393 KygeG-NYEVNEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGV 471
Cdd:COG0441 448 L---GlEYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGI 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 472 LIENFKGAFPFWLSPVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADknmrEKIkGFK-----HYKDPYILVLGDK 546
Cdd:COG0441 525 LIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRN----EKI-GYKireaqLQKVPYMLVVGDK 599
|
570 580
....*....|....*....|....*....
gi 402282425 547 EAEENTVSINVRGtNEQLKDVPLDTFIEM 575
Cdd:COG0441 600 EVENGTVSVRRRG-GGDLGTMSLDEFIAR 627
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-577 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 626.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 1 MDKEQFLHVYRHSLAHVLAKAVIEVFGkETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEIS 80
Cdd:PRK12444 66 IDSNEGVEIARHSAAHILAQAVKRLYG-DVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 81 KKAALELFK--NQKFKVELIEDLPEDEILTIYRTGDdFVDLCRGPHVENSAALlsVAWQLRSMSGSYWRGDEKRDQLTRI 158
Cdd:PRK12444 145 REEAAKLFQemNDRLKLELLEAIPSGESITLYKQGE-FVDLCRGPHLPSTGYL--KAFQLTHVSGAYWRGDSNNQVLQRI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 159 YAYAFPTKEELKAHLAFIKDAQERDHKKIGPQLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVI 238
Cdd:PRK12444 222 YGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 239 NNKRLWVTSGHWAHYKENMFLIpgadgdiEADDT-FAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELN 317
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMYFS-------EVDNKsFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 318 GLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMSCKAELSTRPDDFMGDIETWNIAEKELKEILDR-KYge 396
Cdd:PRK12444 375 GLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSlNY-- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 397 gNYEVNEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENF 476
Cdd:PRK12444 453 -KYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHF 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 477 KGAFPFWLSPVQVGIVPI-RPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSI 555
Cdd:PRK12444 532 GGAFPAWLAPVQVKVIPVsNAVHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNV 611
|
570 580
....*....|....*....|..
gi 402282425 556 NVRGtNEQLKDVPLDTFIEMCR 577
Cdd:PRK12444 612 RKYG-EEKSEVIELDMFVESIK 632
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
11-577 |
0e+00 |
|
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: 602.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 11 RHSLAHVLAKAVIEVFgKETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEISKKAALELFKN 90
Cdd:TIGR00418 1 RHSIAHLLAEALKQLY-PDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 91 QK-FKVELIEDLPEDEILTIYRTGDDFVDLCRGPHVENSAalLSVAWQLRSMSGSYWRGDEKRDQLTRIYAYAFPTKEEL 169
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGKAFVDLCKGPHLPNTS--FIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 170 KAHLAFIKDAQERDHKKIGPQLDLFMFD-ETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSG 248
Cdd:TIGR00418 158 AAYLLRLEEAKKRDHRKLGKELELFSFEpEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 249 HWAHYKENMFLIPGADgdieaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQD 328
Cdd:TIGR00418 238 HWDNYKERMFPFTELD-----NREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 329 DDHTFLMEDQIAAEMGDIMDIADEIYSTLGMS-CKAELSTR-PDDFMGDIETWNIAEKELKEILDRKygEGNYEVNEGDG 406
Cdd:TIGR00418 313 DAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSfDKYELSTRdPEDFIGEDELWEKAEAALEEALKEL--GVPYEIDPGRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 407 AFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENFKGAFPFWLSP 486
Cdd:TIGR00418 391 AFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 487 VQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGtNEQLKD 566
Cdd:TIGR00418 471 VQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRK-GQKLEK 549
|
570
....*....|.
gi 402282425 567 VPLDTFIEMCR 577
Cdd:TIGR00418 550 MSLDEFLEKLR 560
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
2-584 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 573.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 2 DKEQFLHVYRHSLAHVLAKAVIEVFGkeTQYAIGP--EIADGFYYD-FLLPRPATNDDLKTIEEKMKEILKRKEDWKREE 78
Cdd:PLN02908 114 DDDEGRDTFWHSSAHILGEALELEYG--CKLCIGPctTRGEGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 79 ISKKAALELFKNQKFKVELIEDLPEDEILTIYRTGDdFVDLCRGPHVENSAALLSVAwqLRSMSGSYWRGDEKRDQLTRI 158
Cdd:PLN02908 192 VTREEALEMFSENKFKVEIINDLPEDATITVYRCGP-LVDLCRGPHIPNTSFVKAFA--CLKASSAYWRGDVDRESLQRV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 159 YAYAFPTKEELKAHLAFIKDAQERDHKKIGPQLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVI 238
Cdd:PLN02908 269 YGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 239 NNKRLWVTSGHWAHYKENMFLIpgadgDIEADDtFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNG 318
Cdd:PLN02908 349 YNMDLWETSGHAAHYKENMFVF-----EIEKQE-FGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 319 LFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMSCKAELSTRPDDFMGDIETWNIAEKELKEILDRKYGEgn 398
Cdd:PLN02908 423 LTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKP-- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 399 YEVNEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQ-PVVLHRAIFGSMERFIGVLIENFK 477
Cdd:PLN02908 501 WQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIErPVMIHRAILGSVERMFAILLEHYA 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 478 GAFPFWLSPVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKG--FKHYKdpYILVLGDKEAEENTVSI 555
Cdd:PLN02908 581 GKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREaqLAQYN--YILVVGEAEAATGTVNV 658
|
570 580
....*....|....*....|....*....
gi 402282425 556 NVRgTNEQLKDVPLDTFIEMCRTMNEEHS 584
Cdd:PLN02908 659 RTR-DNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
11-573 |
8.93e-171 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 498.65 E-value: 8.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 11 RHSLAHVLAKAVIEVFgKETQYAIGPEIADGFYYDFLLpRPATNDDLKTIEEKMKEILKRKEDWKREEISKKAALELFK- 89
Cdd:PLN02837 47 RHTCAHVMAMAVQKLF-PDAKVTIGPWIENGFYYDFDM-EPLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 90 -NQKFKVELIEDLPEDEIlTIYRTGDDFVDLCRGPHVENSAALLSVAWQLRSMSGSYWRGDEKRDQLTRIYAYAFPTKEE 168
Cdd:PLN02837 125 iNEPYKLEILEGIKEEPI-TIYHIGEEWWDLCAGPHVERTGKINKKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 169 LKAHLAFIKDAQERDHKKIGPQLDLFMF-DETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTS 247
Cdd:PLN02837 204 LKAYLHFKEEAKRRDHRRLGQDLDLFSIqDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 248 GHWAHYKENMFlipgADGDIEaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQ 327
Cdd:PLN02837 284 GHLDFYKENMY----DQMDIE-DELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 328 DDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMS-CKAELSTRPDDFMGDIETWNIAEKELKEILDRKYGEgnYEVNEGDG 406
Cdd:PLN02837 359 DDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWE--YKVDEGGG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 407 AFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENFKGAFPFWLSP 486
Cdd:PLN02837 437 AFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAP 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 487 VQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKnMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGTNEqLKD 566
Cdd:PLN02837 517 VQARVLPVTDNELEYCKEVVAKLKAKGIRAEVCHGER-LPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGE-LGT 594
|
....*..
gi 402282425 567 VPLDTFI 573
Cdd:PLN02837 595 MPVDDFI 601
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
182-486 |
5.27e-148 |
|
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: 428.51 E-value: 5.27e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 182 RDHKKIGPQLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENMFLIp 261
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 262 gadgdIEADDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQDDDHTFLMEDQIAA 341
Cdd:cd00771 80 -----EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 342 EMGDIMDIADEIYSTLGM-SCKAELSTRPDDFMGDIETWNIAEKELKEILDRKygEGNYEVNEGDGAFYGPKIDLKMKDA 420
Cdd:cd00771 155 EIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEI--GLPYEINEGEGAFYGPKIDFHVKDA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402282425 421 LGREWQVGTLQLDFQLPQNFDLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIENFKGAFPFWLSP 486
Cdd:cd00771 233 LGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
293-575 |
8.49e-41 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 156.57 E-value: 8.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 293 SYRDLPIR-YNTVDVIHRKEKSGELNGLFRVQLFRQDDDHTFlmedqiAAEMGDIMDIADEIYStLGMSCKAELS----- 366
Cdd:PRK03991 303 SYKNLPLKmYELSTYSFRLEQRGELVGLKRLRAFTMPDMHTL------CKDMEQAMEEFEKQYE-MILETGEDLGrdyev 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 367 ----TRpdDFMGDIETW--NIAEKELKEILDRKYGEGNYevnegdgaFYGPKIDLKMKDALGREWQVGTLQLDFQLPQNF 440
Cdd:PRK03991 376 airfTE--DFYEENKDWivELVKREGKPVLLEILPERKH--------YWVLKVEFAFIDSLGRPIENPTVQIDVENAERF 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 441 DLKYIAKDGSHKQPVVLHRAIFGSMERFIGVLIEN-----FKG---AFPFWLSPVQVGIVPIRPEHNDYAKKVAQKLFKS 512
Cdd:PRK03991 446 GIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKaakeeEEGkvpMLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAA 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402282425 513 RVRFEVDYADKNMREKIKgfKHYKD--PYILVLGDKEAEENTVSINVRGTNEQlKDVPLDTFIEM 575
Cdd:PRK03991 526 GIRVDVDDRDESLGKKIR--DAGKEwiPYVVVIGDKEMESGKLTVTIREESEK-VEMTLEELIER 587
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
266-476 |
9.81e-29 |
|
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: 112.89 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 266 DIEADDTFAIKPMNCPNAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELNGLFRVQLFRQDDDHTFLMEDQIAAEMGD 345
Cdd:pfam00587 4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 346 IMDIADEIYSTLGMSckaelstrpddfmgdietwniaEKELKEILDRKygegnyevnegdGAFYGPKIDLKMKD-ALGRE 424
Cdd:pfam00587 84 YIKLIDRVYSRLGLE----------------------VRVVRLSNSDG------------SAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 402282425 425 WQVGTLQLD-FQLPQNFDLKYIAKDGSHKQPVVLHRAIFGsMERFIGVLIENF 476
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| 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 ... |
210-473 |
4.48e-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: 106.71 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 210 GWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENMFLIPGADGDIEADDtFAIKPMNCPNAIKIYQR 289
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRDTD-LVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 290 KTRSYRDLPIRYNTVDVIHRKEKSGElNGLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMSCKAELSTRP 369
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 370 DdfmgdietwniaekelkeildrkYGEGNyevNEGDGAFYGPKIDLKMKDAL-GREWQVGTLQLDFQLPQNFDLKYIAKD 448
Cdd:cd00670 159 F-----------------------FGRGG---KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDED 212
|
250 260
....*....|....*....|....*
gi 402282425 449 GSHKQPVVLHRaiFGSMERFIGVLI 473
Cdd:cd00670 213 GGGRAHTGCGG--AGGEERLVLALL 235
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
486-575 |
7.10e-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: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 486 PVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGtNEQLK 565
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRD-GGDLG 79
|
90
....*....|
gi 402282425 566 DVPLDTFIEM 575
Cdd:cd00860 80 SMSLDEFIEK 89
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
488-577 |
2.72e-15 |
|
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: 71.46 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 488 QVGIVPI---RPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGTNEQL 564
Cdd:pfam03129 1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|...
gi 402282425 565 KdVPLDTFIEMCR 577
Cdd:pfam03129 81 T-VSLDELVEKLK 92
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
213-468 |
2.54e-14 |
|
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: 72.15 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 213 LFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWahYKENMFLIPGADGDieaddtFAIKPMNCPNaikiyqrKTR 292
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEED------LYLRPTLEPG-------LVR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 293 SY----RDLPIRYNTVDVIHRKEKSGelNGLFRVQLFRQDDDHTFLMEDQIAAEMGDIMDIADEIYSTLGMSckaelstr 368
Cdd:cd00768 66 LFvshiRKLPLRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIK-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 369 pddfmgdietwniaekelkeiLDRKYGEGNYEvnEGDGAFYGPKIDLKMKDALGREWQVGTLQLDFQLP-QNFDLKYIAK 447
Cdd:cd00768 136 ---------------------LDIVFVEKTPG--EFSPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQaRAADLYFLDE 192
|
250 260
....*....|....*....|.
gi 402282425 448 DGSHKQPVVLHRAIfgSMERF 468
Cdd:cd00768 193 ALEYRYPPTIGFGL--GLERL 211
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
481-592 |
4.15e-12 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 67.95 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 481 PFWLSPVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKgfKHYKD--PYILVLGDKEAEENTVSINVR 558
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIR--RAGTEwiPFVIIIGEREVKTSTLTVKIR 346
|
90 100 110
....*....|....*....|....*....|....
gi 402282425 559 GTNEQlKDVPLDtfiEMCRTMNEEHSLELLTKVP 592
Cdd:PRK14938 347 ANNEQ-KSMTVE---ELVKEIKRADELKERSNLP 376
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
202-473 |
2.65e-09 |
|
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: 58.38 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 202 GMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAP-VINNKRLWVTSGHWAHYKENMFLIPGAdGDIEADDTFAIKPMN- 279
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPlLIPESELEKEKEHIEGFAPEVAWVTHG-GLEELEEPLALRPTSe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 280 ---CPnaikIYQRKTRSYRDLPIRYNTVDVIHRKEKSGElNGLFRVQLFRQDDDHT-FLMEDQIAAEMGDIMDIADEIYS 355
Cdd:cd00778 102 taiYP----MFSKWIRSYRDLPLKINQWVNVFRWETKTT-RPFLRTREFLWQEGHTaHATEEEAEEEVLQILDLYKEFYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 356 TLgMSCKAELSTRPddfmgdietwniaEKElkeildrKYGegnyevnegdGAFYGPKIDLKMKDalGREWQVGTLQldfQ 435
Cdd:cd00778 177 DL-LAIPVVKGRKT-------------EWE-------KFA----------GADYTYTIEAMMPD--GRALQSGTSH---N 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 402282425 436 LPQNF----DLKYIAKDGSHKQPvvlHRAIFGSMERFIGVLI 473
Cdd:cd00778 221 LGQNFskafDIKYQDKDGQKEYV---HQTSWGISTRLIGAII 259
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
12-131 |
8.97e-09 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 58.25 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 12 HSLAHVLAKAVIEVFGKETQYAIGPEIADGFYYDFLLPRPATNDDLKTIEEKMKEILKRKEDWKREEISKKAALElfknq 91
Cdd:PRK01584 457 HTATHLLHKALRLVLGDHVRQKGSNITAERLRFDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEARE----- 531
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 402282425 92 KFKVELIEDLPEDeILTIYRTGDDFVDLCRGPHVENSAAL 131
Cdd:PRK01584 532 KGAMALFGEKYED-IVKVYEIDGFSKEVCGGPHVENTGEL 570
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
486-574 |
1.01e-08 |
|
HisRS Histidyl-anticodon binding domain. HisRS 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: 238436 [Multi-domain] Cd Length: 91 Bit Score: 52.54 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 486 PVQVGIVPIRPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGTNEQLk 565
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE- 79
|
....*....
gi 402282425 566 DVPLDTFIE 574
Cdd:cd00859 80 TVALDELVE 88
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
182-389 |
3.13e-07 |
|
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: 52.18 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 182 RDHKKIGPQLDLFMFDETA--PGM--PYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENM 257
Cdd:cd00770 19 KDHVELGEKLDILDFERGAkvSGSrfYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKFDEQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 258 FLipgadgdIEADDTFAIKPMNCPNAiKIYQRKTRSYRDLPIRYNTVDVIHRKEKSG---ELNGLFRVQLFRQDDDHTFL 334
Cdd:cd00770 99 YK-------VEGEDLYLIATAEVPLA-ALHRDEILEEEELPLKYAGYSPCFRKEAGSagrDTRGLFRVHQFEKVEQFVFT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402282425 335 MEDQIAAEMGDIMDIADEIYSTLGMS------CKAELStRPDDFMGDIETWNIAEKELKEI 389
Cdd:cd00770 171 KPEESWEELEELISNAEEILQELGLPyrvvniCTGDLG-FAAAKKYDIEAWMPGQGKYREI 230
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
107-158 |
3.54e-07 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 46.61 E-value: 3.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 402282425 107 LTIYRTGDDFVDLCRGPHVENSAALLSVAwqLRSMSGSYWRgdekrdqLTRI 158
Cdd:smart00863 1 VRVVSIGDFSVELCGGTHVPNTGEIGAFK--ILSVSGAYWG-------LQRI 43
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
486-563 |
1.06e-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: 47.01 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 486 PVQVGIVPI---RPEHNDYAKKVAQKLFKSRVRFEVDYADKNMREKIKGFKHYKDPYILVLGDKEAEENTVSINVRGTNE 562
Cdd:cd00738 1 PIDVAIVPLtdpRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
.
gi 402282425 563 Q 563
Cdd:cd00738 81 S 81
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
107-158 |
1.17e-06 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 429764 [Multi-domain] Cd Length: 43 Bit Score: 45.51 E-value: 1.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 402282425 107 LTIYRTGDDFVDLCRGPHVENSA-----ALLsvawqlrsmsgsywRGDEKRDQLTRI 158
Cdd:pfam07973 1 VRVVSIGDFDVDLCGGTHVPNTGeigafKIL--------------KGESKNKGLRRI 43
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
202-474 |
5.03e-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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 48.52 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 202 GMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENMFLIPGADGDIEADDTFAIKPMNCP 281
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVFKDAGDEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 282 NAIKIYQRKTRSYRDLPIRYNTVDVIHRKEKSGELnGLFRVQLFRQDDDHTFLME-DQIAAEMGDIMDIADEIYSTLGMS 360
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRF-GFLRAREFIMKDGHSAHADaEEADEEFLNMLSAYAEIARDLAAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 361 ckaelstrpdDFMgdietwnIAEKELKEildrkygegnyevnEGDGAFYGPKIDLKMKDALGREWQVG-TLQLDFQLPQN 439
Cdd:cd00772 182 ----------DFI-------EGEADEGA--------------KFAGASKSREFEALMEDGKAKQAETGhIFGEGFARAFD 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 402282425 440 FDLKYIAKDGSHKqpvVLHRAIFG-SMERFIGVLIE 474
Cdd:cd00772 231 LKAKFLDKDGKEK---FFEMGCWGiGISRFIGAIIE 263
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
481-574 |
1.73e-05 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. 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, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 46.14 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 481 PFWLSPVQVGIVPIRPEHN------DYAKKVAQKLFKSRVRFEVDYADknmrEKIKGFKHYK-----DPYILVLGDKEAE 549
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRD----NYTPGWKFNDwelkgVPLRIEIGPRDLE 80
|
90 100
....*....|....*....|....*
gi 402282425 550 ENTVSINVRGTNEQlKDVPLDTFIE 574
Cdd:cd00862 81 KNTVVIVRRDTGEK-KTVPLAELVE 104
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
178-310 |
1.95e-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. 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: 43.33 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 178 DAQERDHKKIgpqLDLFMFDETAPGMPYWLPRGWKLFNALLEFWRGIHEAHGYQEVSAPVINNKRLWVTSGHWAHYKENM 257
Cdd:cd00779 1 DAEIISHKLL---LRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPEL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 402282425 258 FLIPgadgDIEaDDTFAIKPMNCPNAIKIYQRKTRSYRDLPIR-YNtvdvIHRK 310
Cdd:cd00779 78 LRLK----DRH-GKEFLLGPTHEEVITDLVANEIKSYKQLPLNlYQ----IQTK 122
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
486-576 |
5.99e-04 |
|
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: 39.11 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 486 PVQVGIVPIRPeHNDYAKKVAQKLFK--SRVRFEVDYADKNMRekiKGFKhYKD------PYILVLGDKEAEENTVSINV 557
Cdd:cd00861 1 PFDVVIIPMNM-KDEVQQELAEKLYAelQAAGVDVLLDDRNER---PGVK-FADadligiPYRIVVGKKSAAEGIVEIKV 75
|
90
....*....|....*....
gi 402282425 558 RGTNEQLKdVPLDTFIEMC 576
Cdd:cd00861 76 RKTGEKEE-ISIDELLEFL 93
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
480-519 |
1.23e-03 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS 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: 238435 [Multi-domain] Cd Length: 121 Bit Score: 39.08 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 402282425 480 FPFWLSPVQVGIVPI--RPEHNDYAKKVAQKLFKSRVRFEVD 519
Cdd:cd00858 20 LPPALAPIKVAVLPLvkRDELVEIAKEISEELRELGFSVKYD 61
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
484-577 |
4.69e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 39.68 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402282425 484 LSPVQVGIVPIRPeHNDYAKKVAQKLFKS--RVRFEVDYADKNMRekiKGFKhYKD------PYILVLGDKEAEENTVSI 555
Cdd:PRK09194 466 IAPFDVHIVPVNM-KDEEVKELAEKLYAElqAAGIEVLLDDRKER---PGVK-FADadligiPHRIVVGDRGLAEGIVEY 540
|
90 100
....*....|....*....|..
gi 402282425 556 NVRGTNEQlKDVPLDTFIEMCR 577
Cdd:PRK09194 541 KDRRTGEK-EEVPVDELVEFLK 561
|
|
| |
