|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
4-616 |
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: 794.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 4 EEFLERYRHSIAHVLAKAMIELYgEEVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSRED 83
Cdd:COG0441 65 EEGLEILRHSAAHLLAQAVKRLY-PDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 84 ALKLFAK--QKFKKELIEDLPDGEVISVYHTGDdFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRGDEHRDQLQRVYLF 161
Cdd:COG0441 144 AIELFKEkgEPYKVELIEDIPEDEEISLYRQGE-FVDLCRGPHVPSTGKIK--AFKLLSVAGAYWRGDEKNKMLQRIYGT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 162 VYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMF-DETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINN 240
Cdd:COG0441 221 AFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFqEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 241 KKLWLISGHWAHYINNMFmvpgvsgwlkadadlsgVMEnpndtslpektvkiqagsvIYNREnldtMAAKPMNCPNAMLT 320
Cdd:COG0441 301 RELWETSGHWDHYRENMF-----------------PTE-------------------SDGEE----YALKPMNCPGHILI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 321 YKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVS-YRAEL 399
Cdd:COG0441 341 YKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 400 STRPEDFMGDIEVWDRAEAALKKILTDKygegG--FEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCS 477
Cdd:COG0441 421 STRPEKRIGSDEIWDKAEAALREALEEL----GleYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLT 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 478 FQNAEGEQEMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDK 557
Cdd:COG0441 497 YVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNE 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 361961251 558 NMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGSnKQVNNVPLDAFLkvcAKMQKE 616
Cdd:COG0441 577 KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGG-GDLGTMSLDEFI---ARLKEE 631
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-616 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 622.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 1 MEREEFLERYRHSIAHVLAKAMIELYGEeVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELS 80
Cdd:PRK12444 66 IDSNEGVEIARHSAAHILAQAVKRLYGD-VNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 81 REDALKLFAK--QKFKKELIEDLPDGEVISVYHTGDdFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRGDEHRDQLQRV 158
Cdd:PRK12444 145 REEAAKLFQEmnDRLKLELLEAIPSGESITLYKQGE-FVDLCRGPHLPSTGYLK--AFQLTHVSGAYWRGDSNNQVLQRI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 159 YLFVYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLI 238
Cdd:PRK12444 222 YGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 239 NNKKLWLISGHWAHYINNMFmvpgvsgwlkadadLSGVmenpNDTSLpektvkiqagsviynrenldtmAAKPMNCPNAM 318
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMY--------------FSEV----DNKSF----------------------ALKPMNCPGHM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 319 LTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSYRAE 398
Cdd:PRK12444 342 LMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 399 LSTRPEDFMGDIEVWDRAEAALKKILTD---KYgeggfEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFG 475
Cdd:PRK12444 422 LSTRPEDSMGDDELWEQAEASLENVLQSlnyKY-----RLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 476 CSFQNAEGEQEMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREE-HNAYAKKVYDALSEMGIRTEVDY 554
Cdd:PRK12444 497 LNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERDE 576
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 361961251 555 TDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGSNKQvNNVPLDAFLKvcaKMQKE 616
Cdd:PRK12444 577 RDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS-EVIELDMFVE---SIKEE 634
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
11-616 |
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: 607.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 11 RHSIAHVLAKAMIELYGEeVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSREDALKLFAK 90
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPD-VKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 91 QK-FKKELIEDLPDGEVISVYHTGDDFVDLCRGPHVENSQelMNVAFQVKSVSGAYWRGDEHRDQLQRVYLFVYPDKNAL 169
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGKAFVDLCKGPHLPNTS--FIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 170 KEHLKWLQEAQERDHKKLGKELDLFMFD-ETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISG 248
Cdd:TIGR00418 158 AAYLLRLEEAKKRDHRKLGKELELFSFEpEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 249 HWAHYINNMFmvpgvsgwlkadadlsgvmenpndtslPEKTVKIQagsviynrenldTMAAKPMNCPNAMLTYKRRNRSY 328
Cdd:TIGR00418 238 HWDNYKERMF---------------------------PFTELDNR------------EFMLKPMNCPGHFLIFKSSLRSY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 329 KELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSY-RAELSTR-PEDF 406
Cdd:TIGR00418 279 RDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 407 MGDIEVWDRAEAALKKILTDKygEGGFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCSFQNAEGEQE 486
Cdd:TIGR00418 359 IGEDELWEKAEAALEEALKEL--GVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 487 MPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTY 566
Cdd:TIGR00418 437 RPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREA 516
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 361961251 567 KNYKDPYILVLGDKEMAENTVSINMRgSNKQVNNVPLDAFLKvcaKMQKE 616
Cdd:TIGR00418 517 QKQKIPYMLVVGDKEMESLAVNVRTR-KGQKLEKMSLDEFLE---KLRKE 562
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
182-520 |
1.33e-137 |
|
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: 403.08 E-value: 1.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 182 RDHKKLGKELDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAHYINNMFMVp 261
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 262 gvsgwlkadadlsgvmenpndtslpektvkiqagsviynRENLDTMAAKPMNCPNAMLTYKRRNRSYKELPIRYSEYDVL 341
Cdd:cd00771 80 ---------------------------------------EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 342 HRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGV-SYRAELSTRPEDFMGDIEVWDRAEAAL 420
Cdd:cd00771 121 HRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAAL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 421 KKILTDKygEGGFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCSFQNAEGEQEMPVVLHRAIYGSLE 500
Cdd:cd00771 201 REALEEI--GLPYEINEGEGAFYGPKIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIE 278
|
330 340
....*....|....*....|
gi 361961251 501 RFIGIIIENFKGSFPFWLSP 520
Cdd:cd00771 279 RFIGILIEHYAGKFPLWLAP 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 ... |
301-510 |
2.34e-31 |
|
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: 120.21 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 301 RENLDTMAAKPMNCPNAMLTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADI 380
Cdd:pfam00587 5 DENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 381 ISIADEIYKTFGVSYRA-ELSTRPEdfmgdievwdraeaalkkiltdkygeggfeinegdGAFYGPKIDLQIKD-ALGRE 458
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVvRLSNSDG-----------------------------------SAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 361961251 459 WQCGTVQLD-FQLPHNFGCSFQNAEGEQEMPVVLHRAIYGsLERFIGIIIENF 510
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
107-158 |
1.22e-10 |
|
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: 56.62 E-value: 1.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 361961251 107 ISVYHTGDDFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRgdehrdqLQRV 158
Cdd:smart00863 1 VRVVSIGDFSVELCGGTHVPNTGEIG--AFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
4-616 |
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: 794.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 4 EEFLERYRHSIAHVLAKAMIELYgEEVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSRED 83
Cdd:COG0441 65 EEGLEILRHSAAHLLAQAVKRLY-PDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 84 ALKLFAK--QKFKKELIEDLPDGEVISVYHTGDdFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRGDEHRDQLQRVYLF 161
Cdd:COG0441 144 AIELFKEkgEPYKVELIEDIPEDEEISLYRQGE-FVDLCRGPHVPSTGKIK--AFKLLSVAGAYWRGDEKNKMLQRIYGT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 162 VYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMF-DETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINN 240
Cdd:COG0441 221 AFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFqEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 241 KKLWLISGHWAHYINNMFmvpgvsgwlkadadlsgVMEnpndtslpektvkiqagsvIYNREnldtMAAKPMNCPNAMLT 320
Cdd:COG0441 301 RELWETSGHWDHYRENMF-----------------PTE-------------------SDGEE----YALKPMNCPGHILI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 321 YKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVS-YRAEL 399
Cdd:COG0441 341 YKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 400 STRPEDFMGDIEVWDRAEAALKKILTDKygegG--FEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCS 477
Cdd:COG0441 421 STRPEKRIGSDEIWDKAEAALREALEEL----GleYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLT 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 478 FQNAEGEQEMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDK 557
Cdd:COG0441 497 YVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNE 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 361961251 558 NMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGSnKQVNNVPLDAFLkvcAKMQKE 616
Cdd:COG0441 577 KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGG-GDLGTMSLDEFI---ARLKEE 631
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-616 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 622.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 1 MEREEFLERYRHSIAHVLAKAMIELYGEeVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELS 80
Cdd:PRK12444 66 IDSNEGVEIARHSAAHILAQAVKRLYGD-VNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 81 REDALKLFAK--QKFKKELIEDLPDGEVISVYHTGDdFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRGDEHRDQLQRV 158
Cdd:PRK12444 145 REEAAKLFQEmnDRLKLELLEAIPSGESITLYKQGE-FVDLCRGPHLPSTGYLK--AFQLTHVSGAYWRGDSNNQVLQRI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 159 YLFVYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLI 238
Cdd:PRK12444 222 YGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 239 NNKKLWLISGHWAHYINNMFmvpgvsgwlkadadLSGVmenpNDTSLpektvkiqagsviynrenldtmAAKPMNCPNAM 318
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMY--------------FSEV----DNKSF----------------------ALKPMNCPGHM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 319 LTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSYRAE 398
Cdd:PRK12444 342 LMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 399 LSTRPEDFMGDIEVWDRAEAALKKILTD---KYgeggfEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFG 475
Cdd:PRK12444 422 LSTRPEDSMGDDELWEQAEASLENVLQSlnyKY-----RLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 476 CSFQNAEGEQEMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREE-HNAYAKKVYDALSEMGIRTEVDY 554
Cdd:PRK12444 497 LNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERDE 576
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 361961251 555 TDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGSNKQvNNVPLDAFLKvcaKMQKE 616
Cdd:PRK12444 577 RDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS-EVIELDMFVE---SIKEE 634
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
11-616 |
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: 607.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 11 RHSIAHVLAKAMIELYGEeVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSREDALKLFAK 90
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPD-VKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 91 QK-FKKELIEDLPDGEVISVYHTGDDFVDLCRGPHVENSQelMNVAFQVKSVSGAYWRGDEHRDQLQRVYLFVYPDKNAL 169
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGKAFVDLCKGPHLPNTS--FIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 170 KEHLKWLQEAQERDHKKLGKELDLFMFD-ETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISG 248
Cdd:TIGR00418 158 AAYLLRLEEAKKRDHRKLGKELELFSFEpEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 249 HWAHYINNMFmvpgvsgwlkadadlsgvmenpndtslPEKTVKIQagsviynrenldTMAAKPMNCPNAMLTYKRRNRSY 328
Cdd:TIGR00418 238 HWDNYKERMF---------------------------PFTELDNR------------EFMLKPMNCPGHFLIFKSSLRSY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 329 KELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSY-RAELSTR-PEDF 406
Cdd:TIGR00418 279 RDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 407 MGDIEVWDRAEAALKKILTDKygEGGFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCSFQNAEGEQE 486
Cdd:TIGR00418 359 IGEDELWEKAEAALEEALKEL--GVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 487 MPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTY 566
Cdd:TIGR00418 437 RPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREA 516
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 361961251 567 KNYKDPYILVLGDKEMAENTVSINMRgSNKQVNNVPLDAFLKvcaKMQKE 616
Cdd:TIGR00418 517 QKQKIPYMLVVGDKEMESLAVNVRTR-KGQKLEKMSLDEFLE---KLRKE 562
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
2-618 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 567.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 2 EREEFLERYRHSIAHVLAKAMIELYGeeVQYAIGPQIE--DGAYYD-FWIPKSLTEEDFPTIENKMREIIKRREPWTREE 78
Cdd:PLN02908 114 DDDEGRDTFWHSSAHILGEALELEYG--CKLCIGPCTTrgEGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 79 LSREDALKLFAKQKFKKELIEDLPDGEVISVYHTGDdFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRGDEHRDQLQRV 158
Cdd:PLN02908 192 VTREEALEMFSENKFKVEIINDLPEDATITVYRCGP-LVDLCRGPHIPNTSFVK--AFACLKASSAYWRGDVDRESLQRV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 159 YLFVYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLI 238
Cdd:PLN02908 269 YGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 239 NNKKLWLISGHWAHYINNMFmvpgvsgwlkadadlsgvmenpndtslpektvkiqagsvIYNRENLDtMAAKPMNCPNAM 318
Cdd:PLN02908 349 YNMDLWETSGHAAHYKENMF---------------------------------------VFEIEKQE-FGLKPMNCPGHC 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 319 LTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSYRAE 398
Cdd:PLN02908 389 LMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 399 LSTRPEDFMGDIEVWDRAEAALKKILtDKYGeGGFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCSF 478
Cdd:PLN02908 469 LSTRPEKYLGDLETWDKAEAALTEAL-NAFG-KPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSY 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 479 QNAEGEQ-EMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDK 557
Cdd:PLN02908 547 SAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR 626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 361961251 558 NMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRgSNKQVNNVPLDAFLKVCAKMQKEHT 618
Cdd:PLN02908 627 KIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTR-DNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
2-607 |
2.09e-154 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 458.21 E-value: 2.09e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 2 EREEFLERYRHSIAHVLAKAMIELYgEEVQYAIGPQIEDGAYYDFWIpKSLTEEDFPTIENKMREIIKRREPWTREELSR 81
Cdd:PLN02837 38 ESSEKLLKIRHTCAHVMAMAVQKLF-PDAKVTIGPWIENGFYYDFDM-EPLTDKDLKRIKKEMDRIISRNLPLVREEVSR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 82 EDALKLFA--KQKFKKELIEDLPDgEVISVYHTGDDFVDLCRGPHVENSQELMNVAFQVKSVSGAYWRGDEHRDQLQRVY 159
Cdd:PLN02837 116 EEAQKRIMaiNEPYKLEILEGIKE-EPITIYHIGEEWWDLCAGPHVERTGKINKKAVELESVAGAYWRGDEKNQMLQRIY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 160 LFVYPDKNALKEHLKWLQEAQERDHKKLGKELDLFMF-DETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLI 238
Cdd:PLN02837 195 GTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIqDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 239 NNKKLWLISGHWAHYINNMFmvpgvsgwlkadadlsgvmenpNDTSLPEKTVKIqagsviynrenldtmaaKPMNCPNAM 318
Cdd:PLN02837 275 AKADLWKTSGHLDFYKENMY----------------------DQMDIEDELYQL-----------------RPMNCPYHI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 319 LTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVS-YRA 397
Cdd:PLN02837 316 LVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSkYEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 398 ELSTRPEDFMGDIEVWDRAEAALKKILTDKYGEggFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCS 477
Cdd:PLN02837 396 NLSTRPEKSVGSDDIWEKATTALRDALDDKGWE--YKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDIT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 478 FQNAEGEQEMPVVLHRAIYGSLERFIGIIIENFKGSFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDK 557
Cdd:PLN02837 474 YVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEVCHGER 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 361961251 558 nMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRgSNKQVNNVPLDAFL 607
Cdd:PLN02837 554 -LPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSR-HGGELGTMPVDDFI 601
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
182-520 |
1.33e-137 |
|
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: 403.08 E-value: 1.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 182 RDHKKLGKELDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAHYINNMFMVp 261
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 262 gvsgwlkadadlsgvmenpndtslpektvkiqagsviynRENLDTMAAKPMNCPNAMLTYKRRNRSYKELPIRYSEYDVL 341
Cdd:cd00771 80 ---------------------------------------EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 342 HRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGV-SYRAELSTRPEDFMGDIEVWDRAEAAL 420
Cdd:cd00771 121 HRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAAL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 421 KKILTDKygEGGFEINEGDGAFYGPKIDLQIKDALGREWQCGTVQLDFQLPHNFGCSFQNAEGEQEMPVVLHRAIYGSLE 500
Cdd:cd00771 201 REALEEI--GLPYEINEGEGAFYGPKIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIE 278
|
330 340
....*....|....*....|
gi 361961251 501 RFIGIIIENFKGSFPFWLSP 520
Cdd:cd00771 279 RFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
327-598 |
3.63e-36 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 143.47 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 327 SYKELPI------RYSeydvlHRKEKSGQMNGLFRVQEFRQDDDHTFV--MESQIEaEIADIISIADEIYKTFGVSYraE 398
Cdd:PRK03991 303 SYKNLPLkmyelsTYS-----FRLEQRGELVGLKRLRAFTMPDMHTLCkdMEQAME-EFEKQYEMILETGEDLGRDY--E 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 399 LSTR-PEDFmgdievWDRAEAALKKiLTDKYG--------EGGFeinegdgaFYGP-KIDLQIKDALGREWQCGTVQLDF 468
Cdd:PRK03991 375 VAIRfTEDF------YEENKDWIVE-LVKREGkpvlleilPERK--------HYWVlKVEFAFIDSLGRPIENPTVQIDV 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 469 QLPHNFGCSFQNAEGEQEMPVVLHRAIYGSLERFIGIIIEN-----FKG---SFPFWLSPEQVGIVPIREEHNAYAKKVY 540
Cdd:PRK03991 440 ENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKaakeeEEGkvpMLPTWLSPTQVRVIPVSERHLDYAEEVA 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 541 DALSEMGIRTEVDYTDKNMKEKIKtyKNYKD--PYILVLGDKEMAENTVSINMRGSNKQV 598
Cdd:PRK03991 520 DKLEAAGIRVDVDDRDESLGKKIR--DAGKEwiPYVVVIGDKEMESGKLTVTIREESEKV 577
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
301-510 |
2.34e-31 |
|
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: 120.21 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 301 RENLDTMAAKPMNCPNAMLTYKRRNRSYKELPIRYSEYDVLHRKEKSGQMNGLFRVQEFRQDDDHTFVMESQIEAEIADI 380
Cdd:pfam00587 5 DENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 381 ISIADEIYKTFGVSYRA-ELSTRPEdfmgdievwdraeaalkkiltdkygeggfeinegdGAFYGPKIDLQIKD-ALGRE 458
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVvRLSNSDG-----------------------------------SAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 361961251 459 WQCGTVQLD-FQLPHNFGCSFQNAEGEQEMPVVLHRAIYGsLERFIGIIIENF 510
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
520-609 |
8.77e-25 |
|
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: 98.34 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 520 PEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGsNKQVN 599
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRD-GGDLG 79
|
90
....*....|
gi 361961251 600 NVPLDAFLKV 609
Cdd:cd00860 80 SMSLDEFIEK 89
|
|
| 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 ... |
210-507 |
5.92e-23 |
|
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: 97.85 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 210 GWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAHYINNMFMVPGVSGWLKadadlsgvmenpnDTSLpekt 289
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELR-------------DTDL---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 290 vkiqagsviynrenldtmAAKPMNCPNAMLTYKRRNRSYKELPIRYSEYDVLHRKEKSGQmNGLFRVQEFRQDDDHTFVM 369
Cdd:cd00670 64 ------------------VLRPAACEPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 370 ESQIEAEIADIISIADEIYKTFGVSYRAELSTRPEdfmgdievwdraeaalkkiltdkYGEGGfeiNEGDGAFYGPKIDL 449
Cdd:cd00670 125 PEEAEEERREWLELAEEIARELGLPVRVVVADDPF-----------------------FGRGG---KRGLDAGRETVVEF 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 450 QIKDAL-GREWQCGTVQLDFQLPHnFGCSF-QNAEGEQEMPVVLHRAiyGSLERFIGIII 507
Cdd:cd00670 179 ELLLPLpGRAKETAVGSANVHLDH-FGASFkIDEDGGGRAHTGCGGA--GGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
522-613 |
1.99e-16 |
|
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: 74.93 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 522 QVGIVPI---REEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMRGSNKQV 598
Cdd:pfam03129 1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....*
gi 361961251 599 nNVPLDAFLKVCAKM 613
Cdd:pfam03129 81 -TVSLDELVEKLKEL 94
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
107-158 |
1.22e-10 |
|
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: 56.62 E-value: 1.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 361961251 107 ISVYHTGDDFVDLCRGPHVENSQELMnvAFQVKSVSGAYWRgdehrdqLQRV 158
Cdd:smart00863 1 VRVVSIGDFSVELCGGTHVPNTGEIG--AFKILSVSGAYWG-------LQRI 43
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
12-131 |
3.50e-10 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 62.87 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 12 HSIAHVLAKAMIELYGEEVQYAIGPQIEDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSREDALKLFAKQ 91
Cdd:PRK01584 457 HTATHLLHKALRLVLGDHVRQKGSNITAERLRFDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREKGAMA 536
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 361961251 92 KFKKELiedlpdGEVISVYHTGDDFVDLCRGPHVENSQEL 131
Cdd:PRK01584 537 LFGEKY------EDIVKVYEIDGFSKEVCGGPHVENTGEL 570
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
522-607 |
5.63e-10 |
|
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: 56.39 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 522 QVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSI-NMRgSNKQVnN 600
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVkDLE-TGEQE-T 80
|
....*..
gi 361961251 601 VPLDAFL 607
Cdd:cd00859 81 VALDELV 87
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
513-597 |
1.70e-09 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 60.24 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 513 SFPFWLSPEQVGIVPIREEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMR 592
Cdd:PRK14938 267 TLPDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
....*
gi 361961251 593 GSNKQ 597
Cdd:PRK14938 347 ANNEQ 351
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
182-413 |
4.96e-09 |
|
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: 57.95 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 182 RDHKKLGKELDLFMFDETA--PGM--PYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAHYINNM 257
Cdd:cd00770 19 KDHVELGEKLDILDFERGAkvSGSrfYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKFDEQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 258 FMVPGVSGWLKADADlsgvmenpndtslpektVKIQAgsvIYNRENLDtmaakpmncpnamltykrrnrsYKELPIRYSE 337
Cdd:cd00770 99 YKVEGEDLYLIATAE-----------------VPLAA---LHRDEILE----------------------EEELPLKYAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 338 YDVLHRKE--KSGQMN-GLFRVQEFRQDDDHTFVMESQIEAEIADIISIADEIYKTFGVSYR-AELSTrpEDfMG----- 408
Cdd:cd00770 137 YSPCFRKEagSAGRDTrGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRvVNICT--GD-LGfaaak 213
|
....*..
gi 361961251 409 --DIEVW 413
Cdd:cd00770 214 kyDIEAW 220
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
215-502 |
1.34e-08 |
|
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: 55.59 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 215 QALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAhyinnmfmvpgvsgwlkadADLSGVMEnpndtslpektvkiqa 294
Cdd:cd00768 3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEP-------------------KDLLPVGA---------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 295 gsviynRENLDtMAAKPMNCPNAMLTYKRRNRSykeLPIRYSEYDVLHRKEKSGqmNGLFRVQEFRQDDDHTFVMESQIE 374
Cdd:cd00768 48 ------ENEED-LYLRPTLEPGLVRLFVSHIRK---LPLRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 375 AEIADIISIADEIYKTFGvsyraelstrpedfmgdievwdraeAALKKILTDKYGEggfeinEGDGAFYGPKIDLQIKDA 454
Cdd:cd00768 116 SEFEELIELTEELLRALG-------------------------IKLDIVFVEKTPG------EFSPGGAGPGFEIEVDHP 164
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 361961251 455 LGREWQCGTVQLDFQLPHN-FGCSFQNAEGEQEMPVVLHRAIygSLERF 502
Cdd:cd00768 165 EGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGFGL--GLERL 211
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
107-158 |
1.69e-08 |
|
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: 50.52 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 361961251 107 ISVYHTGDDFVDLCRGPHVENSQELMNVAFQvksvsgaywRGDEHRDQLQRV 158
Cdd:pfam07973 1 VRVVSIGDFDVDLCGGTHVPNTGEIGAFKIL---------KGESKNKGLRRI 43
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
520-592 |
6.05e-08 |
|
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: 50.86 E-value: 6.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 361961251 520 PEQVGIVPI---REEHNAYAKKVYDALSEMGIRTEVDYTDKNMKEKIKTYKNYKDPYILVLGDKEMAENTVSINMR 592
Cdd:cd00738 1 PIDVAIVPLtdpRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSR 76
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
9-130 |
1.70e-07 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 52.50 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 9 RYR----HSIAHVLAKAMIELYGEEVqyaIGPQI-EDGAYYDFWIPkSLTEEDFPTIENKMREIIKRREPWTREELSRED 83
Cdd:COG2872 93 RYRhmrlHTALHLLSAVVYREYGAPV---TGGQIgEDRARIDFDLP-EFDEEDLEEIEAEANELIAADLPVRIYWITREE 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 361961251 84 ALKLfakQKFKKELIEDLPDG-EVISVYHTGDdfVDL--CRGPHVENSQE 130
Cdd:COG2872 169 LEAI---PGLVRTMSVLPPPGvGRVRIVEIGG--VDLqpCGGTHVANTGE 213
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
513-553 |
4.85e-05 |
|
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: 43.32 E-value: 4.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 361961251 513 SFPFWLSPEQVGIVPI--REEHNAYAKKVYDALSEMGIRTEVD 553
Cdd:cd00858 19 RLPPALAPIKVAVLPLvkRDELVEIAKEISEELRELGFSVKYD 61
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
178-260 |
1.87e-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: 43.72 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 178 EAQERDHKKLgkeLDLFMFDETAPGMPYWLPRGWKMYQALLQYSREVQRRHGYTEISAPLINNKKLWLISGHWAHYINNM 257
Cdd:cd00779 1 DAEIISHKLL---LRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPEL 77
|
...
gi 361961251 258 FMV 260
Cdd:cd00779 78 LRL 80
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
515-592 |
3.66e-04 |
|
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: 42.28 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 515 PFWLSPEQVGIVPI------REEHNAYAKKVYDALSEMGIRTEVDYTDknmkekIKT--YKNYK-----DPYILVLGDKE 581
Cdd:cd00862 5 PPRVAPIQVVIVPIgikdekREEVLEAADELAERLKAAGIRVHVDDRD------NYTpgWKFNDwelkgVPLRIEIGPRD 78
|
90
....*....|.
gi 361961251 582 MAENTVSINMR 592
Cdd:cd00862 79 LEKNTVVIVRR 89
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
474-615 |
7.32e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 42.38 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 474 FGCSFQNAEGEqemPVVLHRAIYGslerfIGI------IIENF---KG-SFPFWLSPEQVGIVPI---REEHNAYAKKVY 540
Cdd:PRK09194 420 MNATVLDENGK---AQPLIMGCYG-----IGVsrlvaaAIEQNhdeKGiIWPKAIAPFDVHIVPVnmkDEEVKELAEKLY 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 541 DALSEMGIrtEVDYTDKNMKEKIKtyknYKD------PYILVLGDKEMAENTVSINMRgSNKQVNNVPLDAFLKVCAKMQ 614
Cdd:PRK09194 492 AELQAAGI--EVLLDDRKERPGVK----FADadligiPHRIVVGDRGLAEGIVEYKDR-RTGEKEEVPVDELVEFLKALK 564
|
.
gi 361961251 615 K 615
Cdd:PRK09194 565 K 565
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
520-611 |
8.34e-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: 38.72 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 520 PEQVGIVPIR---EEHNAYAKKVYDALSEMGIrtEVDYTDKNmkEKIKtyKNYKD------PYILVLGDKEMAENTVSIN 590
Cdd:cd00861 1 PFDVVIIPMNmkdEVQQELAEKLYAELQAAGV--DVLLDDRN--ERPG--VKFADadligiPYRIVVGKKSAAEGIVEIK 74
|
90 100
....*....|....*....|.
gi 361961251 591 MRgSNKQVNNVPLDAFLKVCA 611
Cdd:cd00861 75 VR-KTGEKEEISIDELLEFLQ 94
|
|
| PLN02900 |
PLN02900 |
alanyl-tRNA synthetase |
12-143 |
5.61e-03 |
|
alanyl-tRNA synthetase
Pssm-ID: 215487 [Multi-domain] Cd Length: 936 Bit Score: 40.00 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 361961251 12 HSIAHVLAKAMIELYGEEVQYAiGPQI-EDGAYYDFWIPKSLTEEDFPTIENKMREIIKRREPWTREELSREDAlklfak 90
Cdd:PLN02900 598 HTATHLLNSALKEVLGDHVDQK-GSLVaFEKLRFDFSHGKPMTPEELREVESLVNEWIGDALPVEAKEMPLADA------ 670
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 361961251 91 qKFKKELI----EDLPDG-EVISVyhtGDDF-VDLCRGPHVENSQELMnvAFQVKSVSG 143
Cdd:PLN02900 671 -KRINGLRavfgEKYPDPvRVVSV---GGVYsMELCGGTHVSNTAEAE--AFKLLSEEG 723
|
|
| |
