|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
6-665 |
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: 1083.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 6 ISITV-NNERKEVDASFTGVELFAE-----DKNIIAVRLNGELRDLYTSLHNGDTVESVALDSEDGIAIMRHSATHVMAQ 79
Cdd:COG0441 2 IKITLpDGSVREFEAGVTVLDVAKSispglAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 80 AVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEARE--EEANQPYKLELIG 157
Cdd:COG0441 82 AVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIElfKEKGEPYKVELIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 158 DKEAaldpaaaGEiskhELSMYdnldREGNkvWSDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQRIYGTAWPS 237
Cdd:COG0441 162 DIPE-------DE----EISLY----RQGE--FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 238 KEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLY 317
Cdd:COG0441 225 KKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 318 ETSGHLQWYKDGMYPpMKLDEErdengnvtrqgaDYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGVVH 397
Cdd:COG0441 305 ETSGHWDHYRENMFP-TESDGE------------EYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 398 GLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGL 477
Cdd:COG0441 372 GLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPE-KRIGSDEIWDKAEAALREALEELGL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 478 ELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAILLEHYA 557
Cdd:COG0441 451 EYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYA 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 558 GAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRF 637
Cdd:COG0441 531 GAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRR 610
|
650 660
....*....|....*....|....*...
gi 490216947 638 RDGSQLNGVPVEQAKEWILSIIKQRVQV 665
Cdd:COG0441 611 RGGGDLGTMSLDEFIARLKEEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
70-657 |
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: 684.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 70 RHSATHVMAQAVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEAREE-EAN 148
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAfKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 149 QPYKLELIGDKEAALDPAAAGEiskhelsmydnldregNKVWSDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQ 228
Cdd:TIGR00418 81 EPYKLELLDEIPNGVKRTPYGW----------------GKAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 229 RIYGTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQT 308
Cdd:TIGR00418 145 RIYGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 309 PHITKGGLYETSGHLQWYKDGMYPPMKLDEErdengnvtrqgaDYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVY 388
Cdd:TIGR00418 225 PIMYDLELWEISGHWDNYKERMFPFTELDNR------------EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSH 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 389 RYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEHKFVGSDEIWEEATNTL 468
Cdd:TIGR00418 293 RYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 469 AEVAKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERF 548
Cdd:TIGR00418 373 EEALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 549 FAILLEHYAGAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDV 628
Cdd:TIGR00418 453 IAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEM 532
|
570 580
....*....|....*....|....*....
gi 490216947 629 NNNAVSFRFRDGSQLNGVPVEQAKEWILS 657
Cdd:TIGR00418 533 ESLAVNVRTRKGQKLEKMSLDEFLEKLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-662 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 599.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 1 MAENTISITV-NNERKEVDASFTgVELFAED------KNIIAVRLNGELRDLYTSLHNGDTVESVALDSEDGIAIMRHSA 73
Cdd:PRK12444 1 MKEQMIEIKFpDGSVKEFVKGIT-LEEIAGSissslkKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 74 THVMAQAVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEARE--EEANQPY 151
Cdd:PRK12444 80 AHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKlfQEMNDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 152 KLELIGDKEaaldpaaageiSKHELSMYdnldREGNKVwsDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQRIY 231
Cdd:PRK12444 160 KLELLEAIP-----------SGESITLY----KQGEFV--DLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 232 GTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEiGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHI 311
Cdd:PRK12444 223 GVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 312 TKGGLYETSGHLQWYKDGMYppmklDEERDEngnvtrqgADYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYE 391
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMY-----FSEVDN--------KSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 392 KSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLnDFYLELSTKDEhKFVGSDEIWEEATNTLAEV 471
Cdd:PRK12444 369 FSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGF-EYEVELSTRPE-DSMGDDELWEQAEASLENV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 472 AKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAI 551
Cdd:PRK12444 447 LQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 552 LLEHYAGAFPAWLAPVQVTGVPVADE-FAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNN 630
Cdd:PRK12444 527 LIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMEN 606
|
650 660 670
....*....|....*....|....*....|..
gi 490216947 631 NAVSFRFRDGSQLNGVPVEQAKEWILSIIKQR 662
Cdd:PRK12444 607 GAVNVRKYGEEKSEVIELDMFVESIKEEIKNR 638
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-566 |
2.06e-163 |
|
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: 470.88 E-value: 2.06e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 255 DHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYPPM 334
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 335 KLDEErdengnvtrqgadYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYC 414
Cdd:cd00771 81 EEDEE-------------YGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 415 TREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGLELVDDPGGAAFYGPKIS 494
Cdd:cd00771 148 TPDQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTRPE-KFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490216947 495 VQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAILLEHYAGAFPAWLAP 566
Cdd:cd00771 227 FHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
348-556 |
2.13e-37 |
|
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: 137.54 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 348 RQGADYYLKPMNCPMHNLIF-KSRQRSYReLPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSL 426
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 427 LNFVLGLLKDFGLNDFYLELSTKDehkfvgsdeiweeatntlaevakesglelvddpgGAAFYGPKISVQARDAI-GRTW 505
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVVRLSNSD----------------------------------GSAFYGPKLDFEVVFPSlGKQR 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490216947 506 QVSTIQLD-FNLPERFKLEYIAADGSHQRPVMIHRALFGsIERFFAILLEHY 556
Cdd:pfam00587 131 QTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
189-230 |
4.23e-12 |
|
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: 60.86 E-value: 4.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490216947 189 VWSDLCRGPHLPNTRYIKAFKLERVAAAYWRgsehnpmLQRI 230
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
6-665 |
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: 1083.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 6 ISITV-NNERKEVDASFTGVELFAE-----DKNIIAVRLNGELRDLYTSLHNGDTVESVALDSEDGIAIMRHSATHVMAQ 79
Cdd:COG0441 2 IKITLpDGSVREFEAGVTVLDVAKSispglAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 80 AVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEARE--EEANQPYKLELIG 157
Cdd:COG0441 82 AVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIElfKEKGEPYKVELIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 158 DKEAaldpaaaGEiskhELSMYdnldREGNkvWSDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQRIYGTAWPS 237
Cdd:COG0441 162 DIPE-------DE----EISLY----RQGE--FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 238 KEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLY 317
Cdd:COG0441 225 KKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 318 ETSGHLQWYKDGMYPpMKLDEErdengnvtrqgaDYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGVVH 397
Cdd:COG0441 305 ETSGHWDHYRENMFP-TESDGE------------EYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 398 GLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGL 477
Cdd:COG0441 372 GLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPE-KRIGSDEIWDKAEAALREALEELGL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 478 ELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAILLEHYA 557
Cdd:COG0441 451 EYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYA 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 558 GAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRF 637
Cdd:COG0441 531 GAFPLWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRR 610
|
650 660
....*....|....*....|....*...
gi 490216947 638 RDGSQLNGVPVEQAKEWILSIIKQRVQV 665
Cdd:COG0441 611 RGGGDLGTMSLDEFIARLKEEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
70-657 |
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: 684.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 70 RHSATHVMAQAVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEAREE-EAN 148
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAfKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 149 QPYKLELIGDKEAALDPAAAGEiskhelsmydnldregNKVWSDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQ 228
Cdd:TIGR00418 81 EPYKLELLDEIPNGVKRTPYGW----------------GKAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 229 RIYGTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQT 308
Cdd:TIGR00418 145 RIYGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 309 PHITKGGLYETSGHLQWYKDGMYPPMKLDEErdengnvtrqgaDYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVY 388
Cdd:TIGR00418 225 PIMYDLELWEISGHWDNYKERMFPFTELDNR------------EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSH 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 389 RYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEHKFVGSDEIWEEATNTL 468
Cdd:TIGR00418 293 RYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 469 AEVAKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERF 548
Cdd:TIGR00418 373 EEALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 549 FAILLEHYAGAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDV 628
Cdd:TIGR00418 453 IAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEM 532
|
570 580
....*....|....*....|....*....
gi 490216947 629 NNNAVSFRFRDGSQLNGVPVEQAKEWILS 657
Cdd:TIGR00418 533 ESLAVNVRTRKGQKLEKMSLDEFLEKLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-662 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 599.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 1 MAENTISITV-NNERKEVDASFTgVELFAED------KNIIAVRLNGELRDLYTSLHNGDTVESVALDSEDGIAIMRHSA 73
Cdd:PRK12444 1 MKEQMIEIKFpDGSVKEFVKGIT-LEEIAGSissslkKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 74 THVMAQAVQEIRPDAKLGVGPVIKDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEARE--EEANQPY 151
Cdd:PRK12444 80 AHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKlfQEMNDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 152 KLELIGDKEaaldpaaageiSKHELSMYdnldREGNKVwsDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQRIY 231
Cdd:PRK12444 160 KLELLEAIP-----------SGESITLY----KQGEFV--DLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 232 GTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEiGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHI 311
Cdd:PRK12444 223 GVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 312 TKGGLYETSGHLQWYKDGMYppmklDEERDEngnvtrqgADYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYE 391
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMY-----FSEVDN--------KSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 392 KSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLnDFYLELSTKDEhKFVGSDEIWEEATNTLAEV 471
Cdd:PRK12444 369 FSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGF-EYEVELSTRPE-DSMGDDELWEQAEASLENV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 472 AKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAI 551
Cdd:PRK12444 447 LQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 552 LLEHYAGAFPAWLAPVQVTGVPVADE-FAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNN 630
Cdd:PRK12444 527 LIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMEN 606
|
650 660 670
....*....|....*....|....*....|..
gi 490216947 631 NAVSFRFRDGSQLNGVPVEQAKEWILSIIKQR 662
Cdd:PRK12444 607 GAVNVRKYGEEKSEVIELDMFVESIKEEIKNR 638
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
61-650 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 598.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 61 DSEDGIAIMRHSATHVMAQAVQEIRPDAKLGVGPVIKDGFYYDFDVDtPFTPDDLKQIEKHMQRIIKESQSFRRRVVTED 140
Cdd:PLN02837 38 ESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDME-PLTDKDLKRIKKEMDRIISRNLPLVREEVSRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 141 EA--REEEANQPYKLELI-GDKEaalDPAAAGEISKHelsmydnldregnkvWSDLCRGPHLPNTRYI--KAFKLERVAA 215
Cdd:PLN02837 117 EAqkRIMAINEPYKLEILeGIKE---EPITIYHIGEE---------------WWDLCAGPHVERTGKInkKAVELESVAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 216 AYWRGSEHNPMLQRIYGTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSR 295
Cdd:PLN02837 179 AYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 296 EQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYPPMKLDEERdengnvtrqgadYYLKPMNCPMHNLIFKSRQRSYR 375
Cdd:PLN02837 259 KMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDEL------------YQLRPMNCPYHILVYKRKLHSYR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 376 ELPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEhKFV 455
Cdd:PLN02837 327 DLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPE-KSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 456 GSDEIWEEATNTLAEVAKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPV 535
Cdd:PLN02837 406 GSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 536 MIHRALFGSIERFFAILLEHYAGAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMdSSDDRFGKKIRNASKS 615
Cdd:PLN02837 486 MIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQ 564
|
570 580 590
....*....|....*....|....*....|....*
gi 490216947 616 KVPFTLIAGEEDVNNNAVSFRFRDGSQLNGVPVEQ 650
Cdd:PLN02837 565 KIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDD 599
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
31-663 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 549.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 31 KNIIAVRLNGELRDLYTSLHNGDTVESVALDSEDGIAIMRHSATHVMAQAVqEIRPDAKLGVGPVI--KDGFYYD-FDVD 107
Cdd:PLN02908 84 NSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEAL-ELEYGCKLCIGPCTtrGEGFYYDaFYGD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 108 TPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEAREEEANQPYKLELIGDKeaaldPAAAgeiskhELSMYdnldREGN 187
Cdd:PLN02908 163 RTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDL-----PEDA------TITVY----RCGP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 188 KVwsDLCRGPHLPNTRYIKAFKLERVAAAYWRGSEHNPMLQRIYGTAWPSKEELKAYTTRMEEAAKRDHRKLGQEMDLFS 267
Cdd:PLN02908 228 LV--DLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 268 FpDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYppmKLDEERDENGnvt 347
Cdd:PLN02908 306 F-HELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMF---VFEIEKQEFG--- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 348 rqgadyyLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSLL 427
Cdd:PLN02908 379 -------LKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 428 NFVLGLLKDFGLnDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGLELVDDPGGAAFYGPKISVQARDAIGRTWQV 507
Cdd:PLN02908 452 DFLDYVYEVFGF-TYELKLSTRPE-KYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQC 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 508 STIQLDFNLPERFKLEYIAADGSH-QRPVMIHRALFGSIERFFAILLEHYAGAFPAWLAPVQVTGVPVADEFAPHLQKFI 586
Cdd:PLN02908 530 ATVQLDFQLPIRFKLSYSAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVR 609
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490216947 587 SDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRDgsqlNGVPVEQAKEWILSIIKQRV 663
Cdd:PLN02908 610 AQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRD----NVVHGEKKIEELLTEFKEER 682
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-566 |
2.06e-163 |
|
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: 470.88 E-value: 2.06e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 255 DHRKLGQEMDLFSFPDEIGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYPPM 334
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 335 KLDEErdengnvtrqgadYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYC 414
Cdd:cd00771 81 EEDEE-------------YGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 415 TREQMRDELKSLLNFVLGLLKDFGLNDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGLELVDDPGGAAFYGPKIS 494
Cdd:cd00771 148 TPDQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTRPE-KFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490216947 495 VQARDAIGRTWQVSTIQLDFNLPERFKLEYIAADGSHQRPVMIHRALFGSIERFFAILLEHYAGAFPAWLAP 566
Cdd:cd00771 227 FHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
373-642 |
6.72e-42 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 161.19 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 373 SYRELPLRLFEFGTV-YRYEKSGVVHGLTRVRGLTQDDSHIYCTR-EQMRDELKSLLNFVLGLLKDFGLN---------D 441
Cdd:PRK03991 303 SYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDyevairfteD 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 442 FYlelstkDEHKfvgsdeiweeatNTLAEVAKESG----LELVddPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLP 517
Cdd:PRK03991 383 FY------EENK------------DWIVELVKREGkpvlLEIL--PERKHYWVLKVEFAFIDSLGRPIENPTVQIDVENA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 518 ERFKLEYIAADGSHQRPVMIHRALFGSIERFFAILLEHYA--------GAFPAWLAPVQVTGVPVADEFAPHLQKFISDL 589
Cdd:PRK03991 443 ERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAAkeeeegkvPMLPTWLSPTQVRVIPVSERHLDYAEEVADKL 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490216947 590 EENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRDGSQ 642
Cdd:PRK03991 523 EAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESE 575
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
348-556 |
2.13e-37 |
|
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: 137.54 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 348 RQGADYYLKPMNCPMHNLIF-KSRQRSYReLPLRLFEFGTVYRYEKSGVVHGLTRVRGLTQDDSHIYCTREQMRDELKSL 426
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 427 LNFVLGLLKDFGLNDFYLELSTKDehkfvgsdeiweeatntlaevakesglelvddpgGAAFYGPKISVQARDAI-GRTW 505
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVVRLSNSD----------------------------------GSAFYGPKLDFEVVFPSlGKQR 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490216947 506 QVSTIQLD-FNLPERFKLEYIAADGSHQRPVMIHRALFGsIERFFAILLEHY 556
Cdd:pfam00587 131 QTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-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 ... |
283-553 |
4.93e-25 |
|
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: 104.01 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 283 GAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYppmkldeeRDENGNVTRQGADYYLKPMNCPM 362
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMY--------TFEDKGRELRDTDLVLRPAACEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 363 HNLIFKSRQRSYRELPLRLFEFGTVYRYEKSGvVHGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLnDF 442
Cdd:cd00670 73 IYQIFSGEILSYRALPLRLDQIGPCFRHEPSG-RRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 443 YLELSTkDEHKFVGSDEiweeatntlaevakesglelvddpGGAAFYGPKISVQARDAI-GRTWQVSTIQLDFNLPERFK 521
Cdd:cd00670 151 RVVVAD-DPFFGRGGKR------------------------GLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGA 205
|
250 260 270
....*....|....*....|....*....|..
gi 490216947 522 LEYIAADGSHQRPVMIHRalFGSIERFFAILL 553
Cdd:cd00670 206 SFKIDEDGGGRAHTGCGG--AGGEERLVLALL 235
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
566-656 |
9.61e-23 |
|
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: 92.57 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 566 PVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRDGSQLNG 645
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 490216947 646 VPVEQAKEWIL 656
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
286-548 |
1.62e-16 |
|
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: 78.70 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 286 IINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHlqWYKDgMYPPMKLDEErdengnvtrqgaDYYLKPMNCPMHNL 365
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGH--EPKD-LLPVGAENEE------------DLYLRPTLEPGLVR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 366 IFKSRQRSyreLPLRLFEFGTVYRYEKSGVvhGLTRVRGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGLNDfyle 445
Cdd:cd00768 66 LFVSHIRK---LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 446 lstkdehkfvgsDEIWEEATNtlaevakesglelvdDPGGAAFYGPKISVQARDAIGRTWQVSTIQLDFNLPER-FKLEY 524
Cdd:cd00768 137 ------------DIVFVEKTP---------------GEFSPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYF 189
|
250 260
....*....|....*....|....
gi 490216947 525 IAADGSHQRPVMIHRALfgSIERF 548
Cdd:cd00768 190 LDEALEYRYPPTIGFGL--GLERL 211
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
568-658 |
5.46e-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: 70.69 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 568 QVTGVPV---ADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRDGSQLN 644
Cdd:pfam03129 1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 490216947 645 GVPVEQAKEWILSI 658
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
189-230 |
4.23e-12 |
|
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: 60.86 E-value: 4.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490216947 189 VWSDLCRGPHLPNTRYIKAFKLERVAAAYWRgsehnpmLQRI 230
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
545-661 |
1.43e-11 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 67.07 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 545 IERFFAILLEhyAGAFPAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAG 624
Cdd:COG0124 308 LERLLLLLEE--LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILG 385
|
90 100 110
....*....|....*....|....*....|....*...
gi 490216947 625 EEDVNNNAVSFR-FRDGSQLNgVPVEQAKEWILSIIKQ 661
Cdd:COG0124 386 EDELANGTVTLKdLATGEQET-VPLDELVEYLKELLAE 422
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
561-655 |
4.37e-11 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 65.25 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 561 PAWLAPVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRDG 640
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRAN 348
|
90
....*....|....*
gi 490216947 641 SQLNGVPVEQAKEWI 655
Cdd:PRK14938 349 NEQKSMTVEELVKEI 363
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
189-230 |
2.46e-10 |
|
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: 55.91 E-value: 2.46e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490216947 189 VWSDLCRGPHLPNTRYIKAFKLErvaaaywRGSEHNPMLQRI 230
Cdd:pfam07973 9 FDVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
566-653 |
4.56e-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: 51.00 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 566 PVQVTGVPVADEFAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFR-FRDGSQLN 644
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKdLETGEQET 80
|
....*....
gi 490216947 645 gVPVEQAKE 653
Cdd:cd00859 81 -VALDELVE 88
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
273-499 |
5.80e-07 |
|
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: 51.60 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 273 GPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWY--KDGMYPPMKLDEERDEngnvtrqg 350
Cdd:cd00772 21 GRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGfsKELAVFKDAGDEELEE-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 351 aDYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEKSgVVHGLTRVRGLTQDDSH-IYCTREQMRDELKSLLNF 429
Cdd:cd00772 93 -DFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHsAHADAEEADEEFLNMLSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 430 VLGLLKDFGLNDFYLELSTKDEhKFVGSDEIWEEATNTLAEVAKESGLELVDDPGGAAFYGPKISVQARD 499
Cdd:cd00772 171 YAEIARDLAAIDFIEGEADEGA-KFAGASKSREFEALMEDGKAKQAETGHIFGEGFARAFDLKAKFLDKD 239
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
566-656 |
3.32e-05 |
|
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: 43.16 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 566 PVQVTGVPV------ADEFAphlQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRFRD 639
Cdd:cd00738 1 PIDVAIVPLtdprveAREYA---QKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRD 77
|
90
....*....|....*..
gi 490216947 640 GSQLNGVPVEQAKEWIL 656
Cdd:cd00738 78 TGESETLHVDELPEFLV 94
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
6-64 |
6.02e-05 |
|
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340458 [Multi-domain] Cd Length: 65 Bit Score: 41.32 E-value: 6.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490216947 6 ISITVNNER-KEVDASFTGVELFAED-----KNIIAVRLNGELRDLYTSLHNGDTVESVALDSED 64
Cdd:cd01667 1 IKITLPDGSvKEFPKGTTPLDIAKSIspglaKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
71-212 |
1.56e-04 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 44.76 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 71 HSATHVMAQAVQEIRPDAKLGVGPVI-KDGFYYDFDVDTPFTPDDLKQIEKHMQRIIKESQSFRRRVVTEDEAREEEAnq 149
Cdd:PRK01584 457 HTATHLLHKALRLVLGDHVRQKGSNItAERLRFDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREKGA-- 534
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490216947 150 pykLELIGDKeaaldpaaAGEISKheLSMYDNLDREgnkvwsdLCRGPHLPNTRYIKAFKLER 212
Cdd:PRK01584 535 ---MALFGEK--------YEDIVK--VYEIDGFSKE-------VCGGPHVENTGELGTFKIQK 577
|
|
| AlaS |
COG0013 |
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ... |
48-147 |
2.23e-04 |
|
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439784 [Multi-domain] Cd Length: 880 Bit Score: 44.66 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 48 SLHNGDTVESVaLDSEDGIAIMR-HSATHVMAQAVQEIrpdakLG---------VGPvikDGFYYDFDVDTPFTPDDLKQ 117
Cdd:COG0013 545 ELKVGDTVTAQ-VDAERRRAIARnHSATHLLHAALREV-----LGehvtqagslVAP---DRLRFDFSHFEALTPEELAE 615
|
90 100 110
....*....|....*....|....*....|
gi 490216947 118 IEKHMQRIIKESQSFRRRVVTEDEAREEEA 147
Cdd:COG0013 616 IEDLVNEKIRENLPVETREMPLDEAKALGA 645
|
|
| ThiS |
COG2104 |
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; ... |
6-56 |
4.01e-04 |
|
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441707 [Multi-domain] Cd Length: 66 Bit Score: 38.90 E-value: 4.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490216947 6 ISITVNNERKEVDASFTGVELFAE---DKNIIAVRLNGEL--RDLY--TSLHNGDTVE 56
Cdd:COG2104 1 MKITVNGEPREVPEGTTLADLLEElglDPKGVAVAVNGEIvpRSQWasTVLKEGDRVE 58
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
254-439 |
1.34e-03 |
|
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: 41.39 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 254 RDHRKLGQEMDLFSFPD--EI-GPGLAVFHPKGA----AIINAMEDYsreqHRKHHYSFVQTPHITKGGLYETSGHLQWY 326
Cdd:cd00770 19 KDHVELGEKLDILDFERgaKVsGSRFYYLKGDGAllerALINFALDF----LTKRGFTPVIPPFLVRKEVMEGTGQLPKF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 327 KDGMYppmKLDEErdengnvtrqgaDYYLKPM-NCPMHNLIFKSRQrSYRELPLRLFEFGTVYRYEKSGV---VHGLTRV 402
Cdd:cd00770 95 DEQLY---KVEGE------------DLYLIATaEVPLAALHRDEIL-EEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRV 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 490216947 403 RGLTQDDSHIYCTREQMRDELKSLLNFVLGLLKDFGL 439
Cdd:cd00770 159 HQFEKVEQFVFTKPEESWEELEELISNAEEILQELGL 195
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
52-210 |
1.40e-03 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 40.95 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 52 GDTVEsVALDSEDGIAIMR-HSATHVMAQAVqEIRPDAKLGVGPVIKDGFYYDFDVDTpFTPDDLKQIEKHMQRIIKESQ 130
Cdd:COG2872 81 GDEVT-GEIDWERRYRHMRlHTALHLLSAVV-YREYGAPVTGGQIGEDRARIDFDLPE-FDEEDLEEIEAEANELIAADL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 131 SFRRRVVTEDEAReeeanqpyKLELIGDKEAALDPAAAGEISkheLSMYDNLDREGnkvwsdlCRGPHLPNTRYIKAFKL 210
Cdd:COG2872 158 PVRIYWITREELE--------AIPGLVRTMSVLPPPGVGRVR---IVEIGGVDLQP-------CGGTHVANTGEIGRIKI 219
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
272-392 |
1.55e-03 |
|
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: 41.02 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 272 IGPGLAVFHPKGAAIINAMEDYSREQHRKHHYSFVQTPHITKGGLYETSGHLQWYKDGMYppmKLdeeRDengnvtRQGA 351
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELL---RL---KD------RHGK 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490216947 352 DYYLKPMNCPMHNLIFKSRQRSYRELPLRLFEFGTVYRYEK 392
Cdd:cd00779 87 EFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEI 127
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
560-660 |
2.09e-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: 38.69 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 560 FPAWLAPVQVTGVPVA--DEFAPHLQKFISDLEENMVRCEMDSSDDrFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFRF 637
Cdd:cd00858 20 LPPALAPIKVAVLPLVkrDELVEIAKEISEELRELGFSVKYDDSGS-IGRRYARQDEIGTPFCVTVDFDTLEDGTVTIRE 98
|
90 100
....*....|....*....|...
gi 490216947 638 RDGSQLNGVPVEQAKEWILSIIK 660
Cdd:cd00858 99 RDSMRQVRVKIEELPSYLRELIR 121
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
572-651 |
6.67e-03 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 39.33 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216947 572 VPVADEfAPHLQKFISDLEENMVRCEMDSSDDRFGKKIRNASKSKVPFTLIAGEEDVNNNAVSFR-FRDGSQLNgVPVEQ 650
Cdd:PRK12420 344 IPLGTE-LQCLQIAQQLRSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRnMKEGSEVK-VPLSS 421
|
.
gi 490216947 651 A 651
Cdd:PRK12420 422 L 422
|
|
| Ubl_ThiS |
cd00565 |
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine ... |
8-58 |
9.46e-03 |
|
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.
Pssm-ID: 340451 [Multi-domain] Cd Length: 64 Bit Score: 35.17 E-value: 9.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490216947 8 ITVNNERKEVDASFTGVELFAE---DKNIIAVRLNGEL--RDLY--TSLHNGDTVESV 58
Cdd:cd00565 1 ITVNGEPREVDEGLTLAELLEElgfTPKGVAVELNGEIvpRSEWaeTILKDGDRIEIV 58
|
|
| |
