|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
3-579 |
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: 955.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 3 IDTIRHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKL 82
Cdd:COG0441 68 LEILRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 83 FE--NQPYKLELIEEIAGVAPLKIYESGNFIDLCKGPHIKSTlqlhsGQakeiIDALKLTKIAGAYWKGNEKRPMLTRIY 160
Cdd:COG0441 148 FKekGEPYKVELIEDIPEDEEISLYRQGEFVDLCRGPHVPST-----GK----IKAFKLLSVAGAYWRGDEKNKMLQRIY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 161 GVAFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHI 240
Cdd:COG0441 219 GTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 241 GKLDLWKTSGHWDLYRENMYsPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVR 320
Cdd:COG0441 299 LDRELWETSGHWDHYRENMF-PTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 321 GFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPG 400
Cdd:COG0441 378 GFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPG 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 401 GGVFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWL 480
Cdd:COG0441 458 EGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 481 APVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVG 560
Cdd:COG0441 538 APVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLG 617
|
570
....*....|....*....
gi 1278570524 561 MIKLNKFLEKIKMKIENKK 579
Cdd:COG0441 618 TMSLDEFIARLKEEIRSRS 636
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
7-575 |
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: 718.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 7 RHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKLFE-N 85
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKvL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 86 QPYKLELIEEIAGVAPLKIYESGN-FIDLCKGPHIKSTlqlhsgqakEIIDALKLTKIAGAYWKGNEKRPMLTRIYGVAF 164
Cdd:TIGR00418 81 EPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNT---------SFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 165 KTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLD 244
Cdd:TIGR00418 152 ADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 245 LWKTSGHWDLYRENMYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQ 324
Cdd:TIGR00418 232 LWEISGHWDNYKERMFPFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 325 DDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTR-PEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGGV 403
Cdd:TIGR00418 312 DDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 404 FYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAPV 483
Cdd:TIGR00418 392 FYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 484 QIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGMIK 563
Cdd:TIGR00418 472 QVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMS 551
|
570
....*....|..
gi 1278570524 564 LNKFLEKIKMKI 575
Cdd:TIGR00418 552 LDEFLEKLRKEV 563
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
6-578 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 654.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 6 IRHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDfKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKLFE- 84
Cdd:PLN02837 46 IRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFD-MEPLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 85 -NQPYKLELIEEIAGvAPLKIYESGN-FIDLCKGPHIKSTLQLHSgqakeiiDALKLTKIAGAYWKGNEKRPMLTRIYGV 162
Cdd:PLN02837 125 iNEPYKLEILEGIKE-EPITIYHIGEeWWDLCAGPHVERTGKINK-------KAVELESVAGAYWRGDEKNQMLQRIYGT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 163 AFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGK 242
Cdd:PLN02837 197 AWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 243 LDLWKTSGHWDLYRENMYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGF 322
Cdd:PLN02837 277 ADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 323 TQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGG 402
Cdd:PLN02837 357 TQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 403 VFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAP 482
Cdd:PLN02837 437 AFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAP 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 483 VQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKdKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGMI 562
Cdd:PLN02837 517 VQARVLPVTDNELEYCKEVVAKLKAKGIRAEVC-HGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTM 595
|
570
....*....|....*.
gi 1278570524 563 KLNKFLEKIKMKIENK 578
Cdd:PLN02837 596 PVDDFINRIQLAVENR 611
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
184-482 |
1.56e-167 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 477.81 E-value: 1.56e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 184 DHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYsPI 263
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMF-PF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 264 KIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQDDAHIWCTPEQLNQEIIKL 343
Cdd:cd00771 80 EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 344 LKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGGVFYGPKIDIKVKDSLEREWQC 423
Cdd:cd00771 160 LDLIKEVYSDFGFFDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQC 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570524 424 TTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAP 482
Cdd:cd00771 240 STIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
267-472 |
1.17e-44 |
|
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: 156.42 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 267 EEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQDDAHIWCTPEQLNQEIIKLLKH 346
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 347 GLKILKTFGFKDYIIYLSTRPekyagtikgwekatnslkyalknlklkyqidpgGGVFYGPKIDIKVKD-SLEREWQCTT 425
Cdd:pfam00587 88 IDRVYSRLGLEVRVVRLSNSD---------------------------------GSAFYGPKLDFEVVFpSLGKQRQTGT 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278570524 426 IQVD-FNLPERFNITFINKKGKKEKSYMLHRALLGsFERFIGVLIEHY 472
Cdd:pfam00587 135 IQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
104-159 |
3.98e-07 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 46.61 E-value: 3.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278570524 104 IYESGNF-IDLCKGPHIKSTLQlhsgqakeiIDALKLTKIAGAYWKgnekrpmLTRI 159
Cdd:smart00863 3 VVSIGDFsVELCGGTHVPNTGE---------IGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
3-579 |
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: 955.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 3 IDTIRHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKL 82
Cdd:COG0441 68 LEILRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 83 FE--NQPYKLELIEEIAGVAPLKIYESGNFIDLCKGPHIKSTlqlhsGQakeiIDALKLTKIAGAYWKGNEKRPMLTRIY 160
Cdd:COG0441 148 FKekGEPYKVELIEDIPEDEEISLYRQGEFVDLCRGPHVPST-----GK----IKAFKLLSVAGAYWRGDEKNKMLQRIY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 161 GVAFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHI 240
Cdd:COG0441 219 GTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 241 GKLDLWKTSGHWDLYRENMYsPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVR 320
Cdd:COG0441 299 LDRELWETSGHWDHYRENMF-PTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 321 GFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPG 400
Cdd:COG0441 378 GFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPG 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 401 GGVFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWL 480
Cdd:COG0441 458 EGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 481 APVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVG 560
Cdd:COG0441 538 APVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLG 617
|
570
....*....|....*....
gi 1278570524 561 MIKLNKFLEKIKMKIENKK 579
Cdd:COG0441 618 TMSLDEFIARLKEEIRSRS 636
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
7-575 |
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: 718.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 7 RHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKLFE-N 85
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKvL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 86 QPYKLELIEEIAGVAPLKIYESGN-FIDLCKGPHIKSTlqlhsgqakEIIDALKLTKIAGAYWKGNEKRPMLTRIYGVAF 164
Cdd:TIGR00418 81 EPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNT---------SFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 165 KTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLD 244
Cdd:TIGR00418 152 ADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 245 LWKTSGHWDLYRENMYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQ 324
Cdd:TIGR00418 232 LWEISGHWDNYKERMFPFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 325 DDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTR-PEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGGV 403
Cdd:TIGR00418 312 DDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 404 FYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAPV 483
Cdd:TIGR00418 392 FYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 484 QIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGMIK 563
Cdd:TIGR00418 472 QVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMS 551
|
570
....*....|..
gi 1278570524 564 LNKFLEKIKMKI 575
Cdd:TIGR00418 552 LDEFLEKLRKEV 563
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
6-578 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 654.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 6 IRHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDfKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKLFE- 84
Cdd:PLN02837 46 IRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFD-MEPLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 85 -NQPYKLELIEEIAGvAPLKIYESGN-FIDLCKGPHIKSTLQLHSgqakeiiDALKLTKIAGAYWKGNEKRPMLTRIYGV 162
Cdd:PLN02837 125 iNEPYKLEILEGIKE-EPITIYHIGEeWWDLCAGPHVERTGKINK-------KAVELESVAGAYWRGDEKNQMLQRIYGT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 163 AFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGK 242
Cdd:PLN02837 197 AWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 243 LDLWKTSGHWDLYRENMYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGF 322
Cdd:PLN02837 277 ADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 323 TQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGG 402
Cdd:PLN02837 357 TQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 403 VFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAP 482
Cdd:PLN02837 437 AFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAP 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 483 VQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKdKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGMI 562
Cdd:PLN02837 517 VQARVLPVTDNELEYCKEVVAKLKAKGIRAEVC-HGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTM 595
|
570
....*....|....*.
gi 1278570524 563 KLNKFLEKIKMKIENK 578
Cdd:PLN02837 596 PVDDFINRIQLAVENR 611
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
3-579 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 632.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 3 IDTIRHSLAHILAYAVQELYPGVKFGIGPVIENGFYYDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKKL 82
Cdd:PRK12444 72 VEIARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 83 FE--NQPYKLELIEEIAGVAPLKIYESGNFIDLCKGPHIKSTlqlhsgqakEIIDALKLTKIAGAYWKGNEKRPMLTRIY 160
Cdd:PRK12444 152 FQemNDRLKLELLEAIPSGESITLYKQGEFVDLCRGPHLPST---------GYLKAFQLTHVSGAYWRGDSNNQVLQRIY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 161 GVAFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEEvGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHI 240
Cdd:PRK12444 223 GVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 241 GKLDLWKTSGHWDLYRENMYSPiKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVR 320
Cdd:PRK12444 302 MNQELWERSGHWDHYKDNMYFS-EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 321 GFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFkDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPG 400
Cdd:PRK12444 381 TFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGF-EYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 401 GGVFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWL 480
Cdd:PRK12444 460 DGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 481 APVQIWVIPVGSS-HRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDV 559
Cdd:PRK12444 540 APVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS 619
|
570 580
....*....|....*....|
gi 1278570524 560 GMIKLNKFLEKIKMKIENKK 579
Cdd:PRK12444 620 EVIELDMFVESIKEEIKNRK 639
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
4-579 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 541.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 4 DTIRHSLAHILAYAVQELYpGVKFGIGPVIEN--GFYYD-FDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAK 80
Cdd:PLN02908 120 DTFWHSSAHILGEALELEY-GCKLCIGPCTTRgeGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEAL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 81 KLFENQPYKLELIEEIAGVAPLKIYESGNFIDLCKGPHIKSTlqlhsgqakEIIDALKLTKIAGAYWKGNEKRPMLTRIY 160
Cdd:PLN02908 199 EMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNT---------SFVKAFACLKASSAYWRGDVDRESLQRVY 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 161 GVAFKTKKELDNYFKLQQEAEKRDHRILGQKLELFLIDEeVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHI 240
Cdd:PLN02908 270 GISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHE-LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 241 GKLDLWKTSGHWDLYRENMYSpIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVR 320
Cdd:PLN02908 349 YNMDLWETSGHAAHYKENMFV-FEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVR 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 321 GFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFkDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPG 400
Cdd:PLN02908 428 RFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGF-TYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEG 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 401 GGVFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINKKG-KKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLW 479
Cdd:PLN02908 507 DGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEaKIERPVMIHRAILGSVERMFAILLEHYAGKWPFW 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 480 LAPVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDV 559
Cdd:PLN02908 587 LSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVH 666
|
570 580
....*....|....*....|
gi 1278570524 560 GMIKLNKFLEKIKMKIENKK 579
Cdd:PLN02908 667 GEKKIEELLTEFKEERAEFK 686
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
184-482 |
1.56e-167 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 477.81 E-value: 1.56e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 184 DHRILGQKLELFLIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYsPI 263
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMF-PF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 264 KIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQDDAHIWCTPEQLNQEIIKL 343
Cdd:cd00771 80 EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 344 LKHGLKILKTFGFKDYIIYLSTRPEKYAGTIKGWEKATNSLKYALKNLKLKYQIDPGGGVFYGPKIDIKVKDSLEREWQC 423
Cdd:cd00771 160 LDLIKEVYSDFGFFDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQC 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570524 424 TTIQVDFNLPERFNITFINKKGKKEKSYMLHRALLGSFERFIGVLIEHYAGAFPLWLAP 482
Cdd:cd00771 240 STIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
208-578 |
7.30e-53 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 190.47 E-value: 7.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 208 WQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYSpIKIDEEEYMIKPMNCPFHVKIFQSK 287
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLSHPAIREHADKFGERQYR-VKSDKKDLMLRFAACFGQFLMLKDM 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 288 IRSYKDLPIKFAEFGTV-YRYERSGTLHGLTRVRGFTQDDAHIWCTP-EQLNQEIIKLLKHGLKILKTFGFKDYIIYLST 365
Cdd:PRK03991 301 TISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDYEVAIRFT 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 366 RP--EKYAGTIKgwEKATNSLKYALknlklkYQIDPGGGVFYGPKIDIKVKDSLEREWQCTTIQVDFNLPERFNITFINK 443
Cdd:PRK03991 381 EDfyEENKDWIV--ELVKREGKPVL------LEILPERKHYWVLKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 444 KGKKEKSYMLHRALLGSFERFIGVLIEHYAG--------AFPLWLAPVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVK 515
Cdd:PRK03991 453 NGEEKYPIILHCSPTGSIERVIYALLEKAAKeeeegkvpMLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278570524 516 DKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGMIKLNKFLEKIKMKIENK 578
Cdd:PRK03991 533 DRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETKGY 595
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
267-472 |
1.17e-44 |
|
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: 156.42 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 267 EEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTLHGLTRVRGFTQDDAHIWCTPEQLNQEIIKLLKH 346
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 347 GLKILKTFGFKDYIIYLSTRPekyagtikgwekatnslkyalknlklkyqidpgGGVFYGPKIDIKVKD-SLEREWQCTT 425
Cdd:pfam00587 88 IDRVYSRLGLEVRVVRLSNSD---------------------------------GSAFYGPKLDFEVVFpSLGKQRQTGT 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278570524 426 IQVD-FNLPERFNITFINKKGKKEKSYMLHRALLGsFERFIGVLIEHY 472
Cdd:pfam00587 135 IQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-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 ... |
219-469 |
1.84e-33 |
|
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: 127.51 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 219 IEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYS----PIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDL 294
Cdd:cd00670 8 LERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTfedkGRELRDTDLVLRPAACEPIYQIFSGEILSYRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 295 PIKFAEFGTVYRYERSGTlHGLTRVRGFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGfKDYIIYLSTRPEKYAGTi 374
Cdd:cd00670 88 PLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG-LPVRVVVADDPFFGRGG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 375 kgwekatnslkyalknlklkyqiDPGGGVFYGPKIDIKVKDSLE-REWQCTTIQVDFNLPERFNITFINKKGKKEKSYML 453
Cdd:cd00670 165 -----------------------KRGLDAGRETVVEFELLLPLPgRAKETAVGSANVHLDHFGASFKIDEDGGGRAHTGC 221
|
250
....*....|....*.
gi 1278570524 454 HRAllGSFERFIGVLI 469
Cdd:cd00670 222 GGA--GGEERLVLALL 235
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
482-572 |
4.09e-28 |
|
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: 107.59 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 482 PVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGM 561
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 1278570524 562 IKLNKFLEKIK 572
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 ... |
215-464 |
1.41e-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: 81.78 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 215 LRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYrenMYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRsykDL 294
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGAENEEDLYLRPTLEPGLVRLFVSHIR---KL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 295 PIKFAEFGTVYRYERSGTlhGLTRVRGFTQDDAHIWCTPEQLNQEIIKLLKHGLKILKTFGFK-DYIIYLSTRPEKYAGt 373
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKlDIVFVEKTPGEFSPG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 374 ikgwekatnslkyalknlklkyqidpgggvFYGPKIDIKVKDSLEREWQCTTIQVDFNLPER-FNITFINKKGKKEKSYM 452
Cdd:cd00768 152 ------------------------------GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPT 201
|
250
....*....|..
gi 1278570524 453 LHRALlgSFERF 464
Cdd:cd00768 202 IGFGL--GLERL 211
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
484-572 |
1.00e-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: 72.62 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 484 QIWVIPVGS---SHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVG 560
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|..
gi 1278570524 561 MIKLNKFLEKIK 572
Cdd:pfam03129 81 TVSLDELVEKLK 92
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
196-389 |
1.40e-12 |
|
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: 68.16 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 196 LIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYSPIK-----IDEEEY 270
Cdd:cd00772 15 LADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVFKdagdeELEEDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 271 MIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYERSgTLHGLTRVRGFTQDDAHIW-CTPEQLNQEIIKLLKHGLK 349
Cdd:cd00772 95 ALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278570524 350 ILKTFGFKDYIIYLSTRPEKYAGTIKGWE-KATNSLKYALK 389
Cdd:cd00772 174 IARDLAAIDFIEGEADEGAKFAGASKSREfEALMEDGKAKQ 214
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
179-327 |
2.80e-10 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 61.05 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 179 EAEKRDHRILgqkLELFLIdEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYREN 258
Cdd:cd00779 1 DAEIISHKLL---LRAGFI-RQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPE 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278570524 259 MYSPIKIDEEEYMIKPMNCPFHVKIFQSKIRSYKDLPIKFAEFGTVYRYE---RsgtlHGLTRVRGFTQDDA 327
Cdd:cd00779 77 LLRLKDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEirpR----FGLMRGREFLMKDA 144
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
477-572 |
1.11e-08 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 57.55 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 477 PLWLAPVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREK 556
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRAN 348
|
90
....*....|....*.
gi 1278570524 557 GDVGMIKLNKFLEKIK 572
Cdd:PRK14938 349 NEQKSMTVEELVKEIK 364
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
201-328 |
5.49e-08 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 55.55 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 201 VGAGLPIWQPKGV-ILRKIiEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRENMYspiKID---EEEYMIKPMn 276
Cdd:COG0442 35 LASGIYTYLPLGYrVLEKI-EAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELA---RVTdrlEREFCLGPT- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570524 277 cpfH----VKIFQSKIRSYKDLPIKFAEFGTVYRYERSGTlHGLTRVRGFTQDDAH 328
Cdd:COG0442 110 ---HeeviTDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPR-FGLLRTREFLMKDAY 161
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
181-355 |
1.39e-07 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 53.33 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 181 EKRDHRILGQKLELflIDEE-----VGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLY 255
Cdd:cd00770 17 KPKDHVELGEKLDI--LDFErgakvSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 256 RENMYspiKIDEEE-YMI----KPMNcpfhvKIFQSKIRSYKDLPIKFAEFGTVYRYERSGT---LHGLTRVRGFTQDDA 327
Cdd:cd00770 95 DEQLY---KVEGEDlYLIataeVPLA-----ALHRDEILEEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRVHQFEKVEQ 166
|
170 180
....*....|....*....|....*...
gi 1278570524 328 HIWCTPEQLNQEIIKLLKHGLKILKTFG 355
Cdd:cd00770 167 FVFTKPEESWEELEELISNAEEILQELG 194
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
1-160 |
1.72e-07 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 52.50 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 1 MRidtiRHSLAHILAYAVQELYPG--VKFGIGPviENGfYYDFDFKNPiSNEDLPKIEKKMKELIKKDIVFKKKIISKKE 78
Cdd:COG2872 97 MR----LHTALHLLSAVVYREYGApvTGGQIGE--DRA-RIDFDLPEF-DEEDLEEIEAEANELIAADLPVRIYWITREE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 79 AkklfENQPY--KLELIEEIAGVAPLKIYESGNFiDL--CKGPHIKSTlqlhsgqaKEiIDALKLTKIAgAYWKGNekrp 154
Cdd:COG2872 169 L----EAIPGlvRTMSVLPPPGVGRVRIVEIGGV-DLqpCGGTHVANT--------GE-IGRIKITKIE-KKGKGN---- 229
|
....*.
gi 1278570524 155 mlTRIY 160
Cdd:COG2872 230 --RRVY 233
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
179-296 |
1.76e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 53.71 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 179 EAEKRDHRILgqkLELFLIDEEvGAGLPIWQPKGV-ILRKIiEDYLYQELTNHGYQWIVSPHIGKLDLWKTSGHWDLYRE 257
Cdd:PRK12325 17 EAEIVSHRLM---LRAGMIRQQ-AAGIYSWLPLGLkVLKKI-ENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1278570524 258 NMyspIKID---EEEYMIKPMNCPFHVKIFQSKIRSYKDLPI 296
Cdd:PRK12325 92 EM---LRIKdrhDREMLYGPTNEEMITDIFRSYVKSYKDLPL 130
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
482-572 |
3.92e-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: 48.16 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 482 PVQIWVIPVG---SSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGD 558
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 1278570524 559 VGMIKLNKFLEKIK 572
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
179-345 |
3.96e-07 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 52.71 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 179 EAEKRDHRILGQKLELFL----IDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNH-GYQWIVSPHIGKLDLWKTSGHWD 253
Cdd:PRK00960 185 ESKKREITFDGDPTEEAEklgwVKRFPGRGQWFYTPPMTKLFRAFEKLVIEEVLKPlGFDECLFPKLIPLEVMYKMRYLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 254 LYRENMY--SPIKIDEE-------EYMIK--------------------PMNCPFHVKIFQSKIRSYKDLPIK-FAEFGT 303
Cdd:PRK00960 265 GLPEGMYyvCPPKRDPEyfeefvdEMMVKkevpieklkeklrdpgyvlaPAQCEPFYQFFQGETVDVDELPIKfFDRSGW 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1278570524 304 VYRYErSGTLHGLTRVRGFtQDDAHIWC-TPEQLNQEIIKLLK 345
Cdd:PRK00960 345 TYRWE-GGGAHGLERVNEF-HRIEIVWLgTPEQVEEIRDELLK 385
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
104-159 |
3.98e-07 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 46.61 E-value: 3.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278570524 104 IYESGNF-IDLCKGPHIKSTLQlhsgqakeiIDALKLTKIAGAYWKgnekrpmLTRI 159
Cdd:smart00863 3 VVSIGDFsVELCGGTHVPNTGE---------IGAFKILSVSGAYWG-------LQRI 43
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
213-366 |
4.10e-06 |
|
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: 48.37 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 213 VILRKIIEDYLYQELTNHGYQWIVSPHIGKLDLWkTSGHWDLYRENMYSPIKIDEEEYMIKPMNCPFHVKIFqSKIRSYK 292
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELF-LRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAV-AENLLSL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278570524 293 DLPIKFAEFGTVYRYERsgtlHGLTRVRGFTQDDAHIW-CTPEQLNQEIIKLLKHglkILKTFGFKDYIIYLSTR 366
Cdd:cd00773 80 PLPLKLYYIGPVFRYER----PQKGRYREFYQVGVEIIgSDSPLADAEVIALAVE---ILEALGLKDFQIKINHR 147
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
196-372 |
4.77e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 48.36 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 196 LIDEEVGAGLPIWQPKGVILRKIIEDYLYQELTNHGYQWIVSPH-IGKLDLWKTSGHWDLYRENMYSPIKI----DEEEY 270
Cdd:cd00778 15 LIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLlIPESELEKEKEHIEGFAPEVAWVTHGgleeLEEPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 271 MIKPMN----CPFHVKIfqskIRSYKDLPIKFAEFGTVYRYERSgTLHGLTRVRGFTQDDAH-IWCTPEQLNQEIIKLLK 345
Cdd:cd00778 95 ALRPTSetaiYPMFSKW----IRSYRDLPLKINQWVNVFRWETK-TTRPFLRTREFLWQEGHtAHATEEEAEEEVLQILD 169
|
170 180
....*....|....*....|....*..
gi 1278570524 346 HGLKILKTFGFKDYIIYLSTRPEKYAG 372
Cdd:cd00778 170 LYKEFYEDLLAIPVVKGRKTEWEKFAG 196
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
39-125 |
6.57e-06 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 49.00 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 39 YDFDFKNPISNEDLPKIEKKMKELIKKDIVFKKKIISKKEAKK-----LFEnqpyklELIEEIagvapLKIYESGNF-ID 112
Cdd:PRK01584 489 FDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREkgamaLFG------EKYEDI-----VKVYEIDGFsKE 557
|
90
....*....|...
gi 1278570524 113 LCKGPHIKSTLQL 125
Cdd:PRK01584 558 VCGGPHVENTGEL 570
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
102-159 |
5.05e-05 |
|
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: 40.51 E-value: 5.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570524 102 LKIYESGN-FIDLCKGPHIKSTLQlhsgqakeiIDALKLTkiagaywKGNEKRPMLTRI 159
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGE---------IGAFKIL-------KGESKNKGLRRI 43
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
482-572 |
1.43e-04 |
|
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: 40.99 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 482 PVQIWVIPVGSSHRNYANFVNLQLTTNNLRTEVKDKNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRAREREKGDVGM 561
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQET 80
|
90
....*....|.
gi 1278570524 562 IKLNKFLEKIK 572
Cdd:cd00859 81 VALDELVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
481-577 |
9.64e-04 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 40.74 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570524 481 APVQIWVIPVG------SSHRNYANFVNLQLTTNNLRTEVKD-KNETVSKKIREGEIQKIPYLLVVGDKEIKTKSVRARE 553
Cdd:cd00862 9 APIQVVIVPIGikdekrEEVLEAADELAERLKAAGIRVHVDDrDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100
....*....|....*....|....
gi 1278570524 554 REKGDVGMIKLNKFLEKIKMKIEN 577
Cdd:cd00862 89 RDTGEKKTVPLAELVEKVPELLDE 112
|
|
| |
