|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
15-671 |
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: 1077.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 15 VPAGTTAADAvrAAGLPSRGAPDAIVVVRDaqGKLRDLSWIPDADTEVTPVPADTEDGRSVIRHSCAHVLAQAVQELFPA 94
Cdd:COG0441 14 FEAGVTVLDV--AKSISPGLAKAAVAAKVN--GELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 95 AKLGIGPPITDGFYYDFDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYeSKEAARAEL--ADEPYKLELVDDKSGDse 172
Cdd:COG0441 90 AKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEV-SREEAIELFkeKGEPYKVELIEDIPED-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 173 imevggDELTAYDNLNprtrervWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLE 252
Cdd:COG0441 167 ------EEISLYRQGE-------FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 253 LIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWY 332
Cdd:COG0441 234 RLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 333 SEGMYPpMHIDaefaedgtlrkpGQDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMT 412
Cdd:COG0441 314 RENMFP-TESD------------GEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 413 QDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGA 492
Cdd:COG0441 381 QDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTR-PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 493 AFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAP 572
Cdd:COG0441 460 AFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 573 VQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQINGV 652
Cdd:COG0441 540 VQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTM 619
|
650
....*....|....*....
gi 518566216 653 PRDEAVAAIAGWIAARDNT 671
Cdd:COG0441 620 SLDEFIARLKEEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
77-658 |
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: 694.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 77 RHSCAHVLAQAVQELFPAAKLGIGPPITDGFYYDFDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYESKEAARAELAD 156
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 157 EPYKLELVDDKSGdseimevgGDELTAYDNLNPrtrervWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRI 236
Cdd:TIGR00418 81 EPYKLELLDEIPN--------GVKRTPYGWGKA------FVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 237 YGTAWESQEALDRHLELIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPH 316
Cdd:TIGR00418 147 YGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 317 ITKSALYETSGHLQWYSEGMYPPMHIDAefaedgtlrkpgQDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRY 396
Cdd:TIGR00418 227 MYDLELWEISGHWDNYKERMFPFTELDN------------REFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 397 ERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKDPEKYVGSDEVWEEATETLRE 476
Cdd:TIGR00418 295 EQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAALEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 477 VAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFG 556
Cdd:TIGR00418 375 ALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 557 VLTEHYAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEA 636
Cdd:TIGR00418 455 ILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMES 534
|
570 580
....*....|....*....|..
gi 518566216 637 GAVSFRFGDRTQINGVPRDEAV 658
Cdd:TIGR00418 535 LAVNVRTRKGQKLEKMSLDEFL 556
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
57-668 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 596.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 57 DADTEVTPVPADTEDGRSV-IRHSCAHVLAQAVQELFPAAKLGIGPPITDGFYYDFDVpEAFTPEDLAALEKRMRAIIKE 135
Cdd:PLN02837 26 EAEPERVVLPTNESSEKLLkIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDM-EPLTDKDLKRIKKEMDRIISR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 136 GQLFSRRVYESKEAA-RAELADEPYKLELVDD-KSGDSEIMEVGGDeltaydnlnprtrervWGDLCRGPHIPTTRFI-- 211
Cdd:PLN02837 105 NLPLVREEVSREEAQkRIMAINEPYKLEILEGiKEEPITIYHIGEE----------------WWDLCAGPHVERTGKInk 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 212 PAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLELIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGI 291
Cdd:PLN02837 169 KAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 292 IRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSEGMYPPMHIDAEFaedgtlrkpgqdYYLKPMNCPMHHL 371
Cdd:PLN02837 249 VRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDEL------------YQLRPMNCPYHIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 372 IYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLE 451
Cdd:PLN02837 317 VYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEIN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 452 LSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYT 531
Cdd:PLN02837 397 LSTR-PEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 532 AADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVdASDDRM 611
Cdd:PLN02837 476 DSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV-CHGERL 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 518566216 612 PKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQINGVPRDEAVAAIAGWIAAR 668
Cdd:PLN02837 555 PKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVENR 611
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
261-572 |
1.82e-164 |
|
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: 473.96 E-value: 1.82e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 261 DHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSEGMYPPM 340
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 341 HIDAEFAedgtlrkpgqdyyLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYC 420
Cdd:cd00771 81 EEDEEYG-------------LKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 421 AREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAAFYGPKIS 500
Cdd:cd00771 148 TPDQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTR-PEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518566216 501 VQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAP 572
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 ... |
356-562 |
9.71e-38 |
|
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: 138.70 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 356 GQDYYLKPMNCPMHHLIYRSRG-RSYReLPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLR 434
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGlRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 435 FVLDLLADYGLDDYYLELSTKDpekyvgsdevweeatetlrevaeasgltlvpdpgGAAFYGPKISVQVKD-ALGRNWQM 513
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD----------------------------------GSAFYGPKLDFEVVFpSLGKQRQT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518566216 514 STIQLD-FNMPDRFELEYTAADGTRKRPVLIHRALFGsIERFFGVLTEHY 562
Cdd:pfam00587 133 GTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
195-236 |
7.15e-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: 54.70 E-value: 7.15e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518566216 195 VWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRgdqnnasLQRI 236
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
15-671 |
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: 1077.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 15 VPAGTTAADAvrAAGLPSRGAPDAIVVVRDaqGKLRDLSWIPDADTEVTPVPADTEDGRSVIRHSCAHVLAQAVQELFPA 94
Cdd:COG0441 14 FEAGVTVLDV--AKSISPGLAKAAVAAKVN--GELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 95 AKLGIGPPITDGFYYDFDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYeSKEAARAEL--ADEPYKLELVDDKSGDse 172
Cdd:COG0441 90 AKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEV-SREEAIELFkeKGEPYKVELIEDIPED-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 173 imevggDELTAYDNLNprtrervWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLE 252
Cdd:COG0441 167 ------EEISLYRQGE-------FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 253 LIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWY 332
Cdd:COG0441 234 RLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 333 SEGMYPpMHIDaefaedgtlrkpGQDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMT 412
Cdd:COG0441 314 RENMFP-TESD------------GEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 413 QDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGA 492
Cdd:COG0441 381 QDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTR-PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 493 AFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAP 572
Cdd:COG0441 460 AFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 573 VQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQINGV 652
Cdd:COG0441 540 VQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTM 619
|
650
....*....|....*....
gi 518566216 653 PRDEAVAAIAGWIAARDNT 671
Cdd:COG0441 620 SLDEFIARLKEEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
77-658 |
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: 694.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 77 RHSCAHVLAQAVQELFPAAKLGIGPPITDGFYYDFDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYESKEAARAELAD 156
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 157 EPYKLELVDDKSGdseimevgGDELTAYDNLNPrtrervWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRI 236
Cdd:TIGR00418 81 EPYKLELLDEIPN--------GVKRTPYGWGKA------FVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 237 YGTAWESQEALDRHLELIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPH 316
Cdd:TIGR00418 147 YGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 317 ITKSALYETSGHLQWYSEGMYPPMHIDAefaedgtlrkpgQDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRY 396
Cdd:TIGR00418 227 MYDLELWEISGHWDNYKERMFPFTELDN------------REFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 397 ERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKDPEKYVGSDEVWEEATETLRE 476
Cdd:TIGR00418 295 EQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAALEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 477 VAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFG 556
Cdd:TIGR00418 375 ALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 557 VLTEHYAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEA 636
Cdd:TIGR00418 455 ILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMES 534
|
570 580
....*....|....*....|..
gi 518566216 637 GAVSFRFGDRTQINGVPRDEAV 658
Cdd:TIGR00418 535 LAVNVRTRKGQKLEKMSLDEFL 556
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
57-668 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 596.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 57 DADTEVTPVPADTEDGRSV-IRHSCAHVLAQAVQELFPAAKLGIGPPITDGFYYDFDVpEAFTPEDLAALEKRMRAIIKE 135
Cdd:PLN02837 26 EAEPERVVLPTNESSEKLLkIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDM-EPLTDKDLKRIKKEMDRIISR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 136 GQLFSRRVYESKEAA-RAELADEPYKLELVDD-KSGDSEIMEVGGDeltaydnlnprtrervWGDLCRGPHIPTTRFI-- 211
Cdd:PLN02837 105 NLPLVREEVSREEAQkRIMAINEPYKLEILEGiKEEPITIYHIGEE----------------WWDLCAGPHVERTGKInk 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 212 PAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLELIEEALRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGI 291
Cdd:PLN02837 169 KAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 292 IRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSEGMYPPMHIDAEFaedgtlrkpgqdYYLKPMNCPMHHL 371
Cdd:PLN02837 249 VRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDEL------------YQLRPMNCPYHIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 372 IYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDYYLE 451
Cdd:PLN02837 317 VYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEIN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 452 LSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYT 531
Cdd:PLN02837 397 LSTR-PEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 532 AADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVdASDDRM 611
Cdd:PLN02837 476 DSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV-CHGERL 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 518566216 612 PKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQINGVPRDEAVAAIAGWIAAR 668
Cdd:PLN02837 555 PKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVENR 611
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
16-668 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 594.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 16 PAGTTAADAvrAAGLPSRGAPDAivVVRDAQGKLRDLSWIPDADTEVTPVPADTEDGRSVIRHSCAHVLAQAVQELFPAA 95
Cdd:PRK12444 19 VKGITLEEI--AGSISSSLKKKA--VAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILAQAVKRLYGDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 96 KLGIGPPITDGFYYDFDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYESKEAARA-ELADEPYKLELVDDKSGDSEIm 174
Cdd:PRK12444 95 NLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLfQEMNDRLKLELLEAIPSGESI- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 175 evggdelTAYdnlnpRTRERVwgDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLELI 254
Cdd:PRK12444 174 -------TLY-----KQGEFV--DLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 255 EEALRRDHRKLGVELDLFSFPDEiGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSE 334
Cdd:PRK12444 240 EEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 335 GMYppmhidaeFAE-DGTlrkpgqDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMTQ 413
Cdd:PRK12444 319 NMY--------FSEvDNK------SFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 414 DDAHIYCAREGMRDELTSLLRFVLDLLADYGLDdYYLELSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAA 493
Cdd:PRK12444 385 DDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFE-YEVELSTR-PEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 494 FYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAPV 573
Cdd:PRK12444 463 FYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPV 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 574 QVVGIPVADQ-HVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQINGV 652
Cdd:PRK12444 543 QVKVIPVSNAvHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVI 622
|
650
....*....|....*.
gi 518566216 653 PRDEAVAAIAGWIAAR 668
Cdd:PRK12444 623 ELDMFVESIKEEIKNR 638
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
9-645 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 531.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 9 PATPIRV--PAGTTAaDAVRAAGLP-------SRGAPDAiVVVRDAQGKLRDLSWIPDADTEVTPVPADTEDGRSVIRHS 79
Cdd:PLN02908 48 GGDPIKVtlPDGAVK-DGKKWVTTPmdiakeiSKGLANS-ALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 80 CAHVLAQAVQELFpAAKLGIGPPIT--DGFYYD-FDVPEAFTPEDLAALEKRMRAIIKEGQLFSRRVYeSKEAARAELAD 156
Cdd:PLN02908 126 SAHILGEALELEY-GCKLCIGPCTTrgEGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEV-TREEALEMFSE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 157 EPYKLELVDDKSGDSEImevggdelTAYdnlnpRTRERVwgDLCRGPHIPTTRFIPAFKLTRSSAAYWRGDQNNASLQRI 236
Cdd:PLN02908 204 NKFKVEIINDLPEDATI--------TVY-----RCGPLV--DLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 237 YGTAWESQEALDRHLELIEEALRRDHRKLGVELDLFSFpDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPH 316
Cdd:PLN02908 269 YGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFF-HELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 317 ITKSALYETSGHLQWYSEGMYppmhidaefaedgTLRKPGQDYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRY 396
Cdd:PLN02908 348 IYNMDLWETSGHAAHYKENMF-------------VFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRN 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 397 ERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLdDYYLELSTKdPEKYVGSDEVWEEATETLRE 476
Cdd:PLN02908 415 ELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGF-TYELKLSTR-PEKYLGDLETWDKAEAALTE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 477 VAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRK-RPVLIHRALFGSIERFF 555
Cdd:PLN02908 493 ALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMF 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 556 GVLTEHYAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVE 635
Cdd:PLN02908 573 AILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAA 652
|
650
....*....|
gi 518566216 636 AGAVSFRFGD 645
Cdd:PLN02908 653 TGTVNVRTRD 662
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
261-572 |
1.82e-164 |
|
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: 473.96 E-value: 1.82e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 261 DHRKLGVELDLFSFPDEIGSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSEGMYPPM 340
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 341 HIDAEFAedgtlrkpgqdyyLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYC 420
Cdd:cd00771 81 EEDEEYG-------------LKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 421 AREGMRDELTSLLRFVLDLLADYGLDDYYLELSTKdPEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAAFYGPKIS 500
Cdd:cd00771 148 TPDQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTR-PEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518566216 501 VQVKDALGRNWQMSTIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAP 572
Cdd:cd00771 227 FHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
285-642 |
7.05e-40 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 155.41 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 285 FHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKS---ALYEtsgHLQWYSEGMYppmhidaefaedgTLRKPGQDYYL 361
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLshpAIRE---HADKFGERQY-------------RVKSDKKDLML 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 362 KPMNCPMHHLIYRSRGRSYRELPLRLFEFGSV-YRYERSGVVHGLTRVRGMTQDDAHIYCAR-EGMRDELTSLLRFVLDL 439
Cdd:PRK03991 286 RFAACFGQFLMLKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILET 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 440 LADYGLDDYYLELSTKDpekyvgsdeVWEEATETLREVAEASG----LTLVPdpgGAAFYGP-KISVQVKDALGRNWQMS 514
Cdd:PRK03991 366 GEDLGRDYEVAIRFTED---------FYEENKDWIVELVKREGkpvlLEILP---ERKHYWVlKVEFAFIDSLGRPIENP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 515 TIQLDFNMPDRFELEYTAADGTRKRPVLIHRALFGSIERFFGVLTEHYA--------GAFPAWLAPVQVVGIPVADQHVA 586
Cdd:PRK03991 434 TVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAAkeeeegkvPMLPTWLSPTQVRVIPVSERHLD 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 518566216 587 YLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFR 642
Cdd:PRK03991 514 YAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVT 569
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
356-562 |
9.71e-38 |
|
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: 138.70 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 356 GQDYYLKPMNCPMHHLIYRSRG-RSYReLPLRLFEFGSVYRYERSGVVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLR 434
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGlRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 435 FVLDLLADYGLDDYYLELSTKDpekyvgsdevweeatetlrevaeasgltlvpdpgGAAFYGPKISVQVKD-ALGRNWQM 513
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD----------------------------------GSAFYGPKLDFEVVFpSLGKQRQT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518566216 514 STIQLD-FNMPDRFELEYTAADGTRKRPVLIHRALFGsIERFFGVLTEHY 562
Cdd:pfam00587 133 GTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
572-661 |
3.11e-31 |
|
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: 116.83 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 572 PVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQING 651
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|
gi 518566216 652 VPRDEAVAAI 661
Cdd:cd00860 81 MSLDEFIEKL 90
|
|
| 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 ... |
292-559 |
5.44e-24 |
|
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: 101.31 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 292 IRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYSEGMYppmhidaeFAEDGTLRKPGQDYYLKPMNCPMHHL 371
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMY--------TFEDKGRELRDTDLVLRPAACEPIYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 372 IYRSRGRSYRELPLRLFEFGSVYRYERSGvVHGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLdDYYLE 451
Cdd:cd00670 76 IFSGEILSYRALPLRLDQIGPCFRHEPSG-RRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PVRVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 452 LSTkDPEKYVGSDEVWEEATETLREVaeasgLTLVPDPGGAafygpkisvqvkdalgrnWQMSTIQLDFNMPDRFELEYT 531
Cdd:cd00670 154 VAD-DPFFGRGGKRGLDAGRETVVEF-----ELLLPLPGRA------------------KETAVGSANVHLDHFGASFKI 209
|
250 260
....*....|....*....|....*...
gi 518566216 532 AADGTRKRPVLIHRalFGSIERFFGVLT 559
Cdd:cd00670 210 DEDGGGRAHTGCGG--AGGEERLVLALL 235
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
292-554 |
6.61e-17 |
|
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: 79.85 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 292 IRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLQWYsegMYPPMHIdaefaedgtlrkPGQDYYLKPMNCPMHHL 371
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGAE------------NEEDLYLRPTLEPGLVR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 372 IYRSRGRSyreLPLRLFEFGSVYRYERSGVvhGLTRVRGMTQDDAHIYCAREGMRDELTSLLRFVLDLLADYGLDDyyle 451
Cdd:cd00768 66 LFVSHIRK---LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 452 lstkdpekyvgsDEVWEEATetlrevaeasgltlvPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPDR-FELEY 530
Cdd:cd00768 137 ------------DIVFVEKT---------------PGEFSPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYF 189
|
250 260
....*....|....*....|....
gi 518566216 531 TAADGTRKRPVLIHRALfgSIERF 554
Cdd:cd00768 190 LDEALEYRYPPTIGFGL--GLERL 211
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
574-661 |
8.38e-17 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 76.09 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 574 QVVGIPV---ADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQIN 650
Cdd:pfam03129 1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|.
gi 518566216 651 GVPRDEAVAAI 661
Cdd:pfam03129 81 TVSLDELVEKL 91
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
195-236 |
7.15e-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: 54.70 E-value: 7.15e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518566216 195 VWGDLCRGPHIPTTRFIPAFKLTRSSAAYWRgdqnnasLQRI 236
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
572-662 |
2.51e-09 |
|
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: 54.47 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 572 PVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFR-FGDRTQIN 650
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKdLETGEQET 80
|
90
....*....|..
gi 518566216 651 gVPRDEAVAAIA 662
Cdd:cd00859 81 -VALDELVEELK 91
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
567-661 |
2.64e-09 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 59.86 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 567 PAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDR 646
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRAN 348
|
90
....*....|....*
gi 518566216 647 TQINGVPRDEAVAAI 661
Cdd:PRK14938 349 NEQKSMTVEELVKEI 363
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
198-236 |
2.64e-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: 50.14 E-value: 2.64e-08
10 20 30
....*....|....*....|....*....|....*....
gi 518566216 198 DLCRGPHIPTTRFIPAFKLTrssaaywRGDQNNASLQRI 236
Cdd:pfam07973 12 DLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
551-667 |
3.25e-08 |
|
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: 56.28 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 551 IERFFGVLTEhyAGAFPAWLAPVQVVGIPVADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPK--KIVNHTNthVPFMLL 628
Cdd:COG0124 308 LERLLLLLEE--LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKqlKYADKSG--APFVLI 383
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 518566216 629 AGDRDVEAGAVSFR-FGDRTQINgVPRDEAVAAIAGWIAA 667
Cdd:COG0124 384 LGEDELANGTVTLKdLATGEQET-VPLDELVEYLKELLAE 422
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
572-661 |
2.14e-07 |
|
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: 49.32 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 572 PVQVVGIPVAD---QHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTHVPFMLLAGDRDVEAGAVSFRFGDRTQ 648
Cdd:cd00738 1 PIDVAIVPLTDprvEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|...
gi 518566216 649 INGVPRDEAVAAI 661
Cdd:cd00738 81 SETLHVDELPEFL 93
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
571-661 |
5.73e-07 |
|
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: 50.76 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 571 APVQVVGIPV------ADQHVAYLDEVAAQLRSHGVRVEVDASDDRMPKKIVNHTNTH-VPFMLLAGDRDVEAGAV--SF 641
Cdd:cd00862 9 APIQVVIVPIgikdekREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKgVPLRIEIGPRDLEKNTVviVR 88
|
90 100
....*....|....*....|.
gi 518566216 642 R-FGDRTQingVPRDEAVAAI 661
Cdd:cd00862 89 RdTGEKKT---VPLAELVEKV 106
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
279-515 |
8.78e-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: 50.83 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 279 GSGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPHITKSALYETSGHLqwySEGMYPPMHIdaefAEDGTLRKPGQD 358
Cdd:cd00772 21 GRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEH---DEGFSKELAV----FKDAGDEELEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 359 YYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYERSgVVHGLTRVRGMTQDDAHIYCA-REGMRDELTSLLRFVL 437
Cdd:cd00772 94 FALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518566216 438 DLLADYGLDDYYLELSTKDpEKYVGSDEVWEEATETLREVAEASGLTLVPDPGGAAFYGPKISVQVKDALGRNWQMST 515
Cdd:cd00772 173 EIARDLAAIDFIEGEADEG-AKFAGASKSREFEALMEDGKAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEMGC 249
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
77-218 |
1.92e-06 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 49.42 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 77 RHSCAHVLAQAVQELFPAAKLG--IGPpitDGFYYDFDVPEaFTPEDLAALEKRMRAIIKEGqlfsRRVyESKEAARAEL 154
Cdd:COG2872 99 LHTALHLLSAVVYREYGAPVTGgqIGE---DRARIDFDLPE-FDEEDLEEIEAEANELIAAD----LPV-RIYWITREEL 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518566216 155 ADEPY--KLELVDDKSGDSE--IMEVGGDELTAydnlnprtrervwgdlCRGPHIPTTRFIPAFKLTR 218
Cdd:COG2872 170 EAIPGlvRTMSVLPPPGVGRvrIVEIGGVDLQP----------------CGGTHVANTGEIGRIKITK 221
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
291-404 |
1.76e-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: 40.64 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 291 IIRRELEdysrrkhiEAGYQFVNTPHITKSALYETSGHLQWYSEGMYppmhidaEFaedgTLRKpGQDYYLKPMNCPMHH 370
Cdd:cd00779 40 IIREEMN--------KIGAQEILMPILQPAELWKESGRWDAYGPELL-------RL----KDRH-GKEFLLGPTHEEVIT 99
|
90 100 110
....*....|....*....|....*....|....*..
gi 518566216 371 LIYRSRGRSYRELPLRLFEFGSVYRYE---RSGVVHG 404
Cdd:cd00779 100 DLVANEIKSYKQLPLNLYQIQTKFRDEirpRFGLMRG 136
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
298-483 |
3.13e-03 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 39.89 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 298 DYSRRKHIEA---------GYQFVNTPHITKSALYeTSGHLQWYSEGMYppmhidaEFaEDgtlrKPGQDYYLKP-MNCP 367
Cdd:cd00773 1 EAALRRYIEDtlrevferyGYEEIDTPVFEYTELF-LRKSGDEVSKEMY-------RF-KD----KGGRDLALRPdLTAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 368 MHHLIyrSRGRSYRELPLRLFEFGSVYRYERsgvvHGLTRVRGMTQDDAHIYcAREGMRDELtSLLRFVLDLLADYGLDD 447
Cdd:cd00773 68 VARAV--AENLLSLPLPLKLYYIGPVFRYER----PQKGRYREFYQVGVEII-GSDSPLADA-EVIALAVEILEALGLKD 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 518566216 448 YYLEL-STKDPEKYVGSDEVWEEATETLREVAEASGL 483
Cdd:cd00773 140 FQIKInHRGILDGIAGLLEDREEYIERLIDKLDKEAL 176
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
573-642 |
6.04e-03 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 39.71 E-value: 6.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518566216 573 VQVVGIPVADQHVAYLdeVAAQLRSH-GVRVEVDASdDRMPKKIVNHTNTH-VPFMLLAGDRDVEAGAVSFR 642
Cdd:PRK12420 339 ADVFIIPLGTELQCLQ--IAQQLRSTtGLKVELELA-GRKLKKALNYANKEnIPYVLIIGEEEVSTGTVMLR 407
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
280-397 |
6.30e-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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 39.12 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518566216 280 SGLAVFHPKGGIIRRELEDYSRRKHIEAGYQFVNTPH-ITKSALYETSGHLqwysEGMYPpmhidaEFA--EDGTLRKPG 356
Cdd:cd00778 22 KGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLlIPESELEKEKEHI----EGFAP------EVAwvTHGGLEELE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 518566216 357 QDYYLKPMN----CPMhhliYRSRGRSYRELPLRLFEFGSVYRYE 397
Cdd:cd00778 92 EPLALRPTSetaiYPM----FSKWIRSYRDLPLKINQWVNVFRWE 132
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
566-607 |
8.68e-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: 36.77 E-value: 8.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518566216 566 FPAWLAPVQVVGIPVA--DQHVAYLDEVAAQLRSHGVRVEVDAS 607
Cdd:cd00858 20 LPPALAPIKVAVLPLVkrDELVEIAKEISEELRELGFSVKYDDS 63
|
|
| |
