|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-639 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 1288.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 1 MKEQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDGLYDLRRNIEENAEVEIVTIDSDEGVEIARHSAA 80
Cdd:PRK12444 1 MKEQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 81 HILAQAIKRIYGNVNLGVGPVIENGFYYDMDLPSSVNVEDLREIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLK 160
Cdd:PRK12444 81 HILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 161 LELLEAIPSEESVTLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVE 240
Cdd:PRK12444 161 LELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 241 EAAKRNHRKLGSELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNM 320
Cdd:PRK12444 241 EAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 321 YFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPEQIEDEI 400
Cdd:PRK12444 321 YFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 401 KSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDKLWEQAEAALANVLHSLNCKYRLNEGDGAFYGPKIDFHIKDALNRSH 480
Cdd:PRK12444 401 KSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 481 QCGTIQLDFQMPEKFDLNYIDEKNEKKRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWVAPVQVKVIPVSNAVHVQYADE 560
Cdd:PRK12444 481 QCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVHVQYADE 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585720 561 VADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVESMKEEINNRK 639
Cdd:PRK12444 561 VADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIKNRK 639
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
5-639 |
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: 1179.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 5 MIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDGLYDLRRNIEENAEVEIVTIDSDEGVEIARHSAAHILA 84
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 85 QAIKRIYGNVNLGVGPVIENGFYYDMDLPSSVNVEDLREIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLKLELL 164
Cdd:COG0441 81 QAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 165 EAIPSEESVTLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAK 244
Cdd:COG0441 161 EDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 245 RNHRKLGSELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMYFS 323
Cdd:COG0441 241 RDHRKLGKELDLFHFQEEvGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 324 EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPEQIEDEIKSV 403
Cdd:COG0441 321 ESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 404 MAQIDYVYKTFGF-EYEVELSTRPEDSMGDDKLWEQAEAALANVLHSLNCKYRLNEGDGAFYGPKIDFHIKDALNRSHQC 482
Cdd:COG0441 401 IDLVLEVYKDFGFeDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQC 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 483 GTIQLDFQMPEKFDLNYIDEKNEKKRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWVAPVQVKVIPVSNAvHVQYADEVA 562
Cdd:COG0441 481 GTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDK-HADYAKEVA 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585720 563 DKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVESMKEEINNRK 639
Cdd:COG0441 560 KKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEIRSRS 636
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
76-635 |
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: 797.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 76 RHSAAHILAQAIKRIYGNVNLGVGPVIENGFYYDMDLPSSVNVEDLREIEKEMKKIINENIKIERVEVSREEAAKLFqEM 155
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAF-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 156 NDRLKLELLEAIPSEESVTLYKQGE-FVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEE 234
Cdd:TIGR00418 80 LEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 235 YLHFVEEAAKRNHRKLGSELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHW 313
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEiGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 314 GHYKDNMY-FSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVT 392
Cdd:TIGR00418 240 DNYKERMFpFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 393 PEQIEDEIKSVMAQIDYVYKTFGFEYE-VELSTR-PEDSMGDDKLWEQAEAALANVLHSLNCKYRLNEGDGAFYGPKIDF 470
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDkYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 471 HIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKKRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWVAPVQVKVIPVS 550
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 551 NaVHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVES 630
Cdd:TIGR00418 480 E-RHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEK 558
|
....*
gi 446585720 631 MKEEI 635
Cdd:TIGR00418 559 LRKEV 563
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
6-639 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 744.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 6 IEIKFPDGSVKEFVKGITLE-EIAGSISSSLKKKAVAGKVNDGLYDLRRNIEENAEVEIVTIDSDEGVEIARHSAAHILA 84
Cdd:PLN02908 52 IKVTLPDGAVKDGKKWVTTPmDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 85 QAIKRIYGnVNLGVGPVIEN--GFYYDMDL-PSSVNVEDLREIEKEMKKIINENIKIERVEVSREEAAKLFQEmnDRLKL 161
Cdd:PLN02908 132 EALELEYG-CKLCIGPCTTRgeGFYYDAFYgDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSE--NKFKV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 162 ELLEAIPSEESVTLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEE 241
Cdd:PLN02908 209 EIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 242 AAKRNHRKLGSELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMY 321
Cdd:PLN02908 289 AKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 322 FSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPEQIEDEIK 401
Cdd:PLN02908 369 VFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 402 SVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDKLWEQAEAALANVLHSLNCKYRLNEGDGAFYGPKIDFHIKDALNRSHQ 481
Cdd:PLN02908 449 GVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 482 CGTIQLDFQMPEKFDLNYIDEKNEKK-RPVVIHRAVLGSLDRFLAILIEHFGGAFPAWVAPVQVKVIPVSNAvHVQYADE 560
Cdd:PLN02908 529 CATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEK-SQDYAEE 607
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585720 561 VADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVESMKEEINNRK 639
Cdd:PLN02908 608 VRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
55-638 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 585.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 55 IEENAEVEIVTIDSDEGVEIARHSAAHILAQAIKRIYGNVNLGVGPVIENGFYYDMDLPSSVNvEDLREIEKEMKKIINE 134
Cdd:PLN02837 26 EAEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDMEPLTD-KDLKRIKKEMDRIISR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 135 NIKIERVEVSREEAAKLFQEMNDRLKLELLEAIpSEESVTLYKQG-EFVDLCRGPHLPSTGYL--KAFQLTHVSGAYWRG 211
Cdd:PLN02837 105 NLPLVREEVSREEAQKRIMAINEPYKLEILEGI-KEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 212 DSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAKRNHRKLGSELELFMFSEEAPG-MPFYLPKGQIIRNELEAFLREIQKE 290
Cdd:PLN02837 184 DEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGgLVFWHPKGAIVRHIIEDSWKKMHFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 291 YNYQEVRTPFMMNQEVWERSGHWGHYKDNMYFS-EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEF 369
Cdd:PLN02837 264 HGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQmDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 370 SGALNGLLRVRTFCQDDAHLFVTPEQIEDEIKSVMAQIDYVYKTFGF-EYEVELSTRPEDSMGDDKLWEQAEAALANVLH 448
Cdd:PLN02837 344 SGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFsKYEINLSTRPEKSVGSDDIWEKATTALRDALD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 449 SLNCKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKKRPVVIHRAVLGSLDRFLAILI 528
Cdd:PLN02837 424 DKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLI 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 529 EHFGGAFPAWVAPVQVKVIPVSNAvHVQYADEVADKLAQAGVRVERdVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGA 608
Cdd:PLN02837 504 EHYAGDFPLWLAPVQARVLPVTDN-ELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKEVETRT 581
|
570 580 590
....*....|....*....|....*....|.
gi 446585720 609 VNVR-KYGEEKSEVVeLNGFVESMKEEINNR 638
Cdd:PLN02837 582 LTVRsRHGGELGTMP-VDDFINRIQLAVENR 611
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
247-541 |
0e+00 |
|
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: 516.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 247 HRKLGSELELFMFSEEA-PGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMYFSEV 325
Cdd:cd00771 2 HRRLGGELELFFFFDEAgPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 326 DNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPEQIEDEIKSVMA 405
Cdd:cd00771 82 EDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 406 QIDYVYKTFGF-EYEVELSTRPEDSMGDDKLWEQAEAALANVLHSLNCKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGT 484
Cdd:cd00771 162 LIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCST 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446585720 485 IQLDFQMPEKFDLNYIDEKNEKKRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWVAP 541
Cdd:cd00771 242 IQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
269-635 |
1.41e-60 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 212.81 E-value: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 269 YLPKGQIIRNELEAFLREIQKEYNYQEVRTPFM--MNQEVWERsgHWGHYKDNMYFSEVDNKSFALKPMNCPGHMLMFKN 346
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMydLSHPAIRE--HADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 347 KLHSYRELPIRMCEFGQV-HRHEFSGALNGLLRVRTFCQDDAHLFVTP-EQIEDEIKSVMAQIDYVYKTFGFEYEVELS- 423
Cdd:PRK03991 300 MTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDYEVAIRf 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 424 TRpedsmgddKLWEQAEAALANVLHSLNCKYRLNEGDGAFY--GPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYID 501
Cdd:PRK03991 380 TE--------DFYEENKDWIVELVKREGKPVLLEILPERKHywVLKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVD 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 502 EKNEKKRPVVIHRAVLGSLDRFL-AIL----IEHFGG---AFPAWVAPVQVKVIPVSNAvHVQYADEVADKLAQAGVRVE 573
Cdd:PRK03991 452 ENGEEKYPIILHCSPTGSIERVIyALLekaaKEEEEGkvpMLPTWLSPTQVRVIPVSER-HLDYAEEVADKLEAAGIRVD 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585720 574 RDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVESMKEEI 635
Cdd:PRK03991 531 VDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEET 592
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
321-531 |
1.03e-40 |
|
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: 146.40 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 321 YFSEVDNK-SFALKPMNCPGHMLMFKNK-LHSYReLPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPEQIED 398
Cdd:pfam00587 1 YKVEDENGdELALKPTNEPGHTLLFREEgLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 399 EIKSVMAQIDYVYKTFGFE-YEVELSTRPEdsmgddklweqaeaalanvlhslnckyrlnegdGAFYGPKIDFHIKD-AL 476
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEvRVVRLSNSDG---------------------------------SAFYGPKLDFEVVFpSL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446585720 477 NRSHQCGTIQLD-FQMPEKFDLNYIDEKNEKKRPVVIHRAVLGsLDRFLAILIEHF 531
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-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 ... |
276-528 |
6.33e-36 |
|
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: 134.83 E-value: 6.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 276 IRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMYF-----SEVDNKSFALKPMNCPGHMLMFKNKLHS 350
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTfedkgRELRDTDLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 351 YRELPIRMCEFGQVHRHEFSGAlNGLLRVRTFCQDDAHLFVTPEQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEdsM 430
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF--F 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 431 GDdklweqaeaalanvlhslnckyRLNEGDGAFYGPKIDFHIKDALNRSH-QCGTIQLDFQMPEKFDLNYIDEKNEKKRP 509
Cdd:cd00670 161 GR----------------------GGKRGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFKIDEDGGGRAH 218
|
250
....*....|....*....
gi 446585720 510 VVIHRAvlGSLDRFLAILI 528
Cdd:cd00670 219 TGCGGA--GGEERLVLALL 235
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
541-632 |
7.24e-36 |
|
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: 129.55 E-value: 7.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 541 PVQVKVIPVSNAvHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSE 620
Cdd:cd00860 1 PVQVVVIPVTDE-HLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 446585720 621 VVELNGFVESMK 632
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
276-523 |
1.65e-24 |
|
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: 101.81 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 276 IRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWghYKDNMYFSEVDNKSFALKPMNCPGHMLMFKNKLhsyRELP 355
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHI---RKLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 356 IRMCEFGQVHRHEFSGalNGLLRVRTFCQDDAHLFVTPEQIEDEIKSVMAQIDYVYKTFGFEyevelstrpedsmgDDKL 435
Cdd:cd00768 76 LRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIK--------------LDIV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 436 WEQaeaalanvlhslncKYRLNEGDGaFYGPKIDFHIKDALNRSHQCGTIQLDFQMPE-KFDLNYIDEKNEKKRPVVIHR 514
Cdd:cd00768 140 FVE--------------KTPGEFSPG-GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQArAADLYFLDEALEYRYPPTIGF 204
|
....*....
gi 446585720 515 AvlGSLDRF 523
Cdd:cd00768 205 G--LGLERL 211
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
6-70 |
4.21e-24 |
|
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340458 [Multi-domain] Cd Length: 65 Bit Score: 95.63 E-value: 4.21e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585720 6 IEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDGLYDLRRNIEENAEVEIVTIDSDE 70
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
543-634 |
7.83e-22 |
|
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: 90.34 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 543 QVKVIPVSNAV--HVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSE 620
Cdd:pfam03129 1 QVVVIPLGEKAeeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 446585720 621 VVELNGFVESMKEE 634
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
173-221 |
8.70e-15 |
|
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: 68.56 E-value: 8.70e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446585720 173 VTLYKQGEF-VDLCRGPHLPSTGYLKAFQLTHVSGAYWRgdsnnqvLQRI 221
Cdd:smart00863 1 VRVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
265-637 |
2.56e-14 |
|
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: 75.54 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 265 GMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGhwGhyKDN----MY-FSEVDNKSFALKPMNCPG 339
Cdd:COG0124 9 GTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKI--G--EDIvekeMYtFEDRGGRSLTLRPEGTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 340 ---HMLMFKNKLhsyrELPIRMCEFGQVHRHEFSGAlnGllRVRTFCQDDAHLFVTPEQIED-EIKSVMAQIdyvYKTFG 415
Cdd:COG0124 85 varAVAEHGNEL----PFPFKLYYIGPVFRYERPQK--G--RYRQFHQFGVEVIGSDSPLADaEVIALAADL---LKALG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 416 FE-YEVELSTR--PEDSMGD-----DKLW----------EQAEAALANVLHS-LNCKyrlNEGDGAFYG--PKI-DFHIK 473
Cdd:COG0124 154 LKdFTLEINSRglPEERAEAllrylDKLDkighedvldeDSQRRLETNPLRAiLDSK---GPDCQEVLAdaPKLlDYLGE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 474 DALNRSHQCGTIQLDFQMPEKFD------LNY----IDEknekkrpvvihrAVLGSLDRFLAI--------LIEHFGG-- 533
Cdd:COG0124 231 EGLAHFEEVLELLDALGIPYVIDprlvrgLDYytgtVFE------------IVTDGLGAQGSVcgggrydgLVEQLGGpp 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 534 ---------------------AFPAWVAPVQVKVIPVSNAVhVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQK 592
Cdd:COG0124 299 tpavgfaiglerllllleelgLLPAAEPPPDVYVVPLGEEA-RAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSG 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446585720 593 IPYVLVIGDKEMENGAVNVR--KYGEEKSevVELNGFVESMKEEINN 637
Cdd:COG0124 378 APFVLILGEDELANGTVTLKdlATGEQET--VPLDELVEYLKELLAE 422
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
6-65 |
7.48e-14 |
|
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.
Pssm-ID: 427005 [Multi-domain] Cd Length: 60 Bit Score: 66.42 E-value: 7.48e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 6 IEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDGLYDLRRNIEENAEVEIVT 65
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
536-623 |
7.55e-14 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 73.73 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 536 PAWVAPVQVKVIPVSNAvHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGA--VNVRK 613
Cdd:PRK14938 269 PDWLNPIQVRILPVKKD-FLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTltVKIRA 347
|
90
....*....|
gi 446585720 614 YGEEKSEVVE 623
Cdd:PRK14938 348 NNEQKSMTVE 357
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
539-637 |
5.92e-13 |
|
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: 68.09 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 539 VAPVQVKVIPV-----SNAVHVQYADEVADKLAQAGVRVERDVRDEKL-GYKIREAQMQKIPYVLVIGDKEMENGAVNVR 612
Cdd:cd00862 8 VAPIQVVIVPIgikdeKREEVLEAADELAERLKAAGIRVHVDDRDNYTpGWKFNDWELKGVPLRIEIGPRDLEKNTVVIV 87
|
90 100
....*....|....*....|....*
gi 446585720 613 KYGEEKSEVVELNGFVESMKEEINN 637
Cdd:cd00862 88 RRDTGEKKTVPLAELVEKVPELLDE 112
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
173-221 |
2.97e-12 |
|
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: 61.31 E-value: 2.97e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446585720 173 VTLYKQGE-FVDLCRGPHLPSTGYLKAFQLThvsgaywRGDSNNQVLQRI 221
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
541-629 |
2.35e-11 |
|
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: 60.49 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 541 PVQVKVIPV--SNAVHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEK 618
Cdd:cd00738 1 PIDVAIVPLtdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|.
gi 446585720 619 SEVVELNGFVE 629
Cdd:cd00738 81 SETLHVDELPE 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
493-634 |
8.02e-11 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 64.72 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 493 EKFDLNYIDEkNEKKRPVVihravLGS----LDRFLAILIEHF----GGAFPAWVAPVQVKVIPVS--NAVHVQYADEVA 562
Cdd:PRK09194 418 EAMNATVLDE-NGKAQPLI-----MGCygigVSRLVAAAIEQNhdekGIIWPKAIAPFDVHIVPVNmkDEEVKELAEKLY 491
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585720 563 DKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVVELNGFVESMKEE 634
Cdd:PRK09194 492 AELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKAL 563
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
541-617 |
2.86e-09 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 54.52 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 541 PVQVKVIPVS--NAVHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNV--RKYGE 616
Cdd:cd00861 1 PFDVVIIPMNmkDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIkvRKTGE 80
|
.
gi 446585720 617 E 617
Cdd:cd00861 81 K 81
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
263-390 |
4.14e-09 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 57.59 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 263 APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMY-FSEVDNKSFALKPMNCPGHM 341
Cdd:cd00779 20 SSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLrLKDRHGKEFLLGPTHEEVIT 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446585720 342 LMFKNKLHSYRELPIRMCEFGQVHRHE----FsgalnGLLRVRTFCQDDAHLF 390
Cdd:cd00779 100 DLVANEIKSYKQLPLNLYQIQTKFRDEirprF-----GLMRGREFLMKDAYSF 147
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
541-632 |
5.12e-08 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 50.62 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 541 PVQVKVIPVSNAVHVQYAdEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSE 620
Cdd:cd00859 1 EVDVYVVPLGEGALSEAL-ELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79
|
90
....*....|..
gi 446585720 621 VVELNGFVESMK 632
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
76-194 |
5.47e-08 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 54.04 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 76 RHSAAHILAQAIKRIYGnvnlgvGPVIENGFYYD---MDL-PSSVNVEDLREIEKEMKKIINENIKIERVEVSREEAAKL 151
Cdd:COG2872 99 LHTALHLLSAVVYREYG------APVTGGQIGEDrarIDFdLPEFDEEDLEEIEAEANELIAADLPVRIYWITREELEAI 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446585720 152 FQEMndrlKLELLEAIPSEESVTLYKQGEFvDL--CRGPHLPSTG 194
Cdd:COG2872 173 PGLV----RTMSVLPPPGVGRVRIVEIGGV-DLqpCGGTHVANTG 212
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-528 |
6.24e-08 |
|
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: 54.14 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 265 GMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWER-SGHWGHYKDNMYF------SEVDNKsFALKPMN- 336
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKeKEHIEGFAPEVAWvthgglEELEEP-LALRPTSe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 337 ---CPghmlMFKNKLHSYRELPIRMCEFGQVHRHEFSgALNGLLRVRTFCQDDAH-LFVTPEQIEDEIKsvmaQIDYVYK 412
Cdd:cd00778 102 taiYP----MFSKWIRSYRDLPLKINQWVNVFRWETK-TTRPFLRTREFLWQEGHtAHATEEEAEEEVL----QILDLYK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 413 TFGFEYE---VELSTRPEdsmgddklWEqaeaalanvlhslncKYrlnegDGAFYGPKIDFHIKDAlnRSHQCGTI-QLD 488
Cdd:cd00778 173 EFYEDLLaipVVKGRKTE--------WE---------------KF-----AGADYTYTIEAMMPDG--RALQSGTShNLG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446585720 489 FQMPEKFDLNYIDEKNEKKRPvviHRAVLGSLDRFLAILI 528
Cdd:cd00778 223 QNFSKAFDIKYQDKDGQKEYV---HQTSWGISTRLIGAII 259
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
239-395 |
2.12e-06 |
|
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: 49.87 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 239 VEEAAKRNHRKLGSELELFMFSEEA--PGMPFYLPKGQIIRNE--LEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWG 314
Cdd:cd00770 13 VFDFKPKDHVELGEKLDILDFERGAkvSGSRFYYLKGDGALLEraLINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 315 HYKDNMYFSEVDNKSF---ALKPMNCpghmlMFKNKLHSYRELPIRMCEFGQVHRHEfSGALN----GLLRVRTFCQDDA 387
Cdd:cd00770 93 KFDEQLYKVEGEDLYLiatAEVPLAA-----LHRDEILEEEELPLKYAGYSPCFRKE-AGSAGrdtrGLFRVHQFEKVEQ 166
|
....*...
gi 446585720 388 HLFVTPEQ 395
Cdd:cd00770 167 FVFTKPEE 174
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-418 |
2.97e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 49.29 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 265 GMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHY--KDNMYFS----EVDNKSFALKPMNCP 338
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGfsKELAVFKdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 339 GHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSgALNGLLRVRTFCQDDAHLF-VTPEQIEDEIKSVMAqidyVYKTFGFE 417
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLS----AYAEIARD 177
|
.
gi 446585720 418 Y 418
Cdd:cd00772 178 L 178
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
522-633 |
4.79e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 46.39 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 522 RFLAILIEHF----GGAFPAWVAPVQVKVIP--VSNAVHVQYADEVADKLAQAGVRVERDVRDEKLGYKIREAQMQKIPY 595
Cdd:PRK12325 322 RLVAAIIEAShddkGIIWPESVAPFKVGIINlkQGDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPW 401
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446585720 596 VLVIGDKEMENGAVNV--RKYGEekSEVVELNGFVESMKE 633
Cdd:PRK12325 402 QIIVGPKGLAEGKVELkdRKTGE--REELSVEAAINRLTA 439
|
|
| PLN02961 |
PLN02961 |
alanine-tRNA ligase |
41-151 |
1.29e-04 |
|
alanine-tRNA ligase
Pssm-ID: 178546 [Multi-domain] Cd Length: 223 Bit Score: 43.92 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 41 AGKVNDGLYDLRRNIEENAEVeIVTIDSDEGVEIAR-HSAAHILAQAIKRIygnvnlGVGPVIENGFYYDMDLP-----S 114
Cdd:PLN02961 50 YGVFEGSNPESASPFEAGDEV-TVTVDESRRKLHSRlHSAGHLLDVCMARV------GLGPLEPGKGYHFPDGPfveykG 122
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446585720 115 SVNVEDL----REIEKEMKKIINENIKIERVEVSREEAAKL 151
Cdd:PLN02961 123 KIPQGELdskqDELEAEANELIAEGGKVSAAVLPYDEAAEL 163
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
274-425 |
1.73e-04 |
|
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: 43.75 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 274 QIIRNELEAFLREIQKEYNYQEVRTPFMMNQEVWERSGHWGHYKdNMY-FSEVDNKSFALKPMNCPGHMLMFKNKLhSYR 352
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSK-EMYrFKDKGGRDLALRPDLTAPVARAVAENL-LSL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585720 353 ELPIRMCEFGQVHRHEFSGAlnglLRVRTFCQDDAHLFVTPEQIED-EIKSVMAQIdyvYKTFGFE-YEVELSTR 425
Cdd:cd00773 80 PLPLKLYYIGPVFRYERPQK----GRYREFYQVGVEIIGSDSPLADaEVIALAVEI---LEALGLKdFQIKINHR 147
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
269-568 |
3.90e-04 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 43.19 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 269 YLPKGQIIRNELEAFLRE--IQKEYNYQEVRTPFMMNQEVWERSGHWGHYKDNMyfseVDNK------------------ 328
Cdd:PRK04173 33 YGPLGVELKNNIKRAWWKsfVQEREDVVGIDSPIIMPPEVWEASGHVDNFSDPL----VECKkckkryradhlieelgid 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 329 -----SFALKPMN------CP---GHM--------LM----------------------------FKNKLHSYRE-LPIR 357
Cdd:PRK04173 109 aeglsNEELKELIrendikCPecgGENwtevrqfnLMfktfigpvedskslgylrpetaqgifvnFKNVLRTARKkLPFG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 358 MCEFGQVHRHEFSgALNGLLRVRTFCQDDAHLFVTPEQiEDEIksvmaqIDYvYKTFGFEYEVELSTRPEdsmgddklwe 437
Cdd:PRK04173 189 IAQIGKSFRNEIT-PRNFIFRTREFEQMELEFFVKPGT-DNEW------FAY-WIELRKNWLLDLGIDPE---------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 438 qaeaalanvlhslncKYRLNEgdgafygpkidfHIKDalNRSH---QCGTIQLDFQMPEKF------------------- 495
Cdd:PRK04173 250 ---------------NLRFRE------------HLPE--ELAHyskATWDIEYKFPFGRFWgelegianrtdydlsrhsk 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 496 ----DLNYIDEKNEKKR--PVVIHRAVlGsLDR-FLAILIEHF------GG------AFPAWVAPVQVKVIP-VSNAVHV 555
Cdd:PRK04173 301 hsgeDLSYFDDETTGEKyiPYVIEPSA-G-LDRlLLAFLEDAYteeelgGGdkrtvlRLPPALAPVKVAVLPlVKKEKLS 378
|
410
....*....|...
gi 446585720 556 QYADEVADKLAQA 568
Cdd:PRK04173 379 EKAREIYAELRKD 391
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
542-617 |
8.76e-04 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 42.03 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 542 VQVKVIPVSNAVHvqyadevADKLAQA-----GVRVERDVRDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVR--KY 614
Cdd:PRK12420 339 ADVFIIPLGTELQ-------CLQIAQQlrsttGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRnmKE 411
|
...
gi 446585720 615 GEE 617
Cdd:PRK12420 412 GSE 414
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
68-202 |
1.70e-03 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 41.30 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585720 68 SDEGVEIAR-HSAAHILAQAIKRIYG-NVNLGVGPVIENGFYYDMDLPSSVNVEDLREIEKemkkIINENIK----IERV 141
Cdd:PRK01584 447 ADHSYETTKlHTATHLLHKALRLVLGdHVRQKGSNITAERLRFDFSHPEKMTDDEIKKVED----IVNLQIKndlsVKKE 522
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585720 142 EVSREEAAK-----LFQEmndrlklelleaiPSEESVTLYKQGEF-VDLCRGPHLPSTGYLKAFQLT 202
Cdd:PRK01584 523 VMSLEEAREkgamaLFGE-------------KYEDIVKVYEIDGFsKEVCGGPHVENTGELGTFKIQ 576
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
535-575 |
2.88e-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: 37.92 E-value: 2.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446585720 535 FPAWVAPVQVKVIP-VSNAVHVQYADEVADKLAQAGVRVERD 575
Cdd:cd00858 20 LPPALAPIKVAVLPlVKRDELVEIAKEISEELRELGFSVKYD 61
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
559-631 |
3.82e-03 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 40.16 E-value: 3.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585720 559 DEVADKLAQAGVRVE--RDVRDEKLGYKiREAQMQKIPYVLVigdkeMENGAVNVRKYGEEKSEVVELNGFVESM 631
Cdd:PLN02309 388 EELAEKLAGSGVKVAkfRADGDQKEFAK-QELQLGSFPTILL-----FPKNSSRPIKYPSEKRDVDSLLSFVNSL 456
|
|
| |
