|
Name |
Accession |
Description |
Interval |
E-value |
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
34-513 |
0e+00 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 531.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 34 INSAEITGMTRQEALKAVTQQAKRRGLGGDLTSDKLRDWLISRQRYWGTPIPVVHCPACGTLPVPYRDLPVLLPSVATFT 113
Cdd:COG0495 384 INSGEFDGLDSEEAKEAIIEWLEEKGLGKRKVNYRLRDWLISRQRYWGEPIPIIHCEDCGVVPVPEDQLPVELPEDVDFD 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 114 GKGASPLESAPEWVNCACPRCKAAARREVDTMDTFVDSAWYYLRYTDPHNTDRPFNSDLADYWMPVDLYIGGKEHAVMHL 193
Cdd:COG0495 464 PTGGSPLARAPEWVNVTCPKCGGPARRETDTMDTFVDSSWYYLRYTDPHNDEAPFDPEAANYWLPVDQYIGGIEHAILHL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 194 FYARFFSHFCHDLKMTKHKEPFHKLLVQGLIknqtfrlastgqclkrEEVDLTGtepvhlktgeKLQVTWEKMSKSKHNG 273
Cdd:COG0495 544 LYARFFTKVLRDLGLVSFDEPFKRLLTQGMV----------------LEVGKDG----------VVIGGIEKMSKSKGNV 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 274 IEPEELVKEYGIDTLRLYLLFAAPPEQDILWDTKtdAMPGVQRWQTRLWALVTKLLEertsGTLPSPELLSKKEKAEARK 353
Cdd:COG0495 598 VDPDEIIEKYGADTLRLFEMFAGPPERDLEWSDS--GVEGAYRFLNRVWRLVVDEAE----ALKLDVADLSEADKELRRA 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 354 IweqkNLVISEVTEYFtkDHL-FNAAISRLMSLTNVLHQASRPLILHSREFEDALAALCIMVAPMAPHIASEMWKGLAHv 432
Cdd:COG0495 672 L----HKTIKKVTEDI--ERLrFNTAIAALMELVNALYKAKDSGEADRAVLREALETLVLLLAPFAPHIAEELWERLGH- 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 433 qnklcphhhwDVDVLQQSWPKVDPEYLQpAEVVEMSVLINNKACGKVPVPQRAARnfEEVHELVLQSELGVKHLQGRTIK 512
Cdd:COG0495 745 ----------EGSVADAPWPEADEAALV-EDEVTIVVQVNGKVRGKIEVPADASK--EELEAAALADEKVQKFLEGKTIR 811
|
.
gi 675615417 513 K 513
Cdd:COG0495 812 K 812
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
31-527 |
3.57e-152 |
|
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 456.14 E-value: 3.57e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 31 EKVINSAEITGMTRQEALKAVTQQAKRRGLGGDLTSDKLRDWLISRQRYWGTPIPVVHCPACGTLPVPYRDLPVLLPSVA 110
Cdd:TIGR00396 374 GVLVNSGEFNGLNSSEARNAIIDMLEKEGKGKRKVNYRLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDLPVILPEDV 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 111 TFTGKGASPLESAPEWVNCACPRCKAAARREVDTMDTFVDSAWYYLRYTDPHNTDRPFNSDLADYWMPVDLYIGGKEHAV 190
Cdd:TIGR00396 454 VYDGDGGSPLSRIPEWVNVTCPSCGKPALRETDTMDTFAGSSWYYLRYLDPKNTDGPFDKEKAEYWLPVDLYIGGIEHAI 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 191 MHLFYARFFSHFCHDLKMTKHKEPFHKLLVQGLIknQTFRLASTGQcLKREEVDLTGTEPVHLKTGEKLQVTWEKMSKSK 270
Cdd:TIGR00396 534 LHLLYARFFHKFLRDIGYVNTKEPFKKLINQGMV--LGFYYPPNGK-VPADVLTERDEKGKDKAGGELVYVGYEKMSKSK 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 271 HNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILWDtkTDAMPGVQRWQTRLWALVTKLLEErTSGTLPSPELLSKKEKAE 350
Cdd:TIGR00396 611 GNGIDPQEIVESYGADALRLFIMFMGPIAASLEWN--ESGLEGARRFLDRVWNLVYEITGE-LDAASLTVTALEEAQKEL 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 351 ARKIweqkNLVISEVTEYFTKDHLFNAAISRLMSLTNVLHQASRPLILhsrefEDALAALCIMVAPMAPHIASEMWKGLA 430
Cdd:TIGR00396 688 RRDV----HKFLKKVTEDLEKRESFNTAISAMMELLNKLYKAKKEALM-----LEYLKGFVTVLSPFAPHLAEELWEKLG 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 431 HVQNklcphhhwdvDVLQQSWPKVDPEYLQPAEvVEMSVLINNKACGKVPVPQRAARnfEEVHELVLQSELGVKHLQGRT 510
Cdd:TIGR00396 759 SEPF----------IIDNAKWPVVDETALVEDK-TLIVVQVNGKFRAKITVPKDADE--EQVEELAKQDPEVKKYLENKT 825
|
490
....*....|....*..
gi 675615417 511 IKKAFLSPrTALINFLV 527
Cdd:TIGR00396 826 IKKVIYVP-GKLVNFVI 841
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
29-518 |
7.46e-103 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 330.63 E-value: 7.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 29 GLEKVINSAE----ITGMTRQEALKAVTQQAKRRGLGGDLTSDKLRDWLISRQRYWGTPIPVVHCPACG-TLPVPYRDLP 103
Cdd:PLN02563 460 GEGVIVNSSSsgldINGLSSKEAAKKVIEWLEETGNGKKKVNYKLRDWLFARQRYWGEPIPVVFLEDSGePVPVPESDLP 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 104 VLLPSVATFT--GKGASPLESAPEWVNCACPRCKAAARREVDTMDTFVDSAWYYLRYTDPHNTDRPFNSDLADYWMPVDL 181
Cdd:PLN02563 540 LTLPELDDFTptGTGEPPLAKAVSWVNTVDPSSGKPARRETNTMPQWAGSCWYYLRFMDPKNSNALVDKEKEKYWMPVDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 182 YIGGKEHAVMHLFYARFFSHFCHDLKMTKHKEPFHKLLVQGLI---------KNQTFRLASTG----------QCLKREE 242
Cdd:PLN02563 620 YVGGAEHAVLHLLYARFWHKVLYDIGVVSTKEPFQCLVNQGMIlgeveytafKDSDGEYVSADtadrlgelqqEKIPEEK 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 243 VDLTGTEPVhLKTGEKLQVTWE--KMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILWDTKtdAMPGVQRWQTR 320
Cdd:PLN02563 700 VIKSGDSFV-LKDDPSIRLIARahKMSKSRGNVVNPDDVVSEYGADSLRLYEMFMGPLRDSKTWSTS--GVEGVHRFLGR 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 321 LWALVTKLleERTSGTLPSPELLSKKEKAEarkiwEQKNLV---ISEVTEYfTKDHLFNAAISRLMSLTNVLHQ-ASRPl 396
Cdd:PLN02563 777 TWRLVVGA--PLPDGSFRDGTVVTDEEPSL-----EQLRLLhkcIAKVTEE-IESTRFNTAISAMMEFTNAAYKwDKVP- 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 397 ilhsREfedALAALCIMVAPMAPHIASEMWKGLAHVQNklcphhhwdvdVLQQSWPKVDPEYLQPAEVVeMSVLINNKAC 476
Cdd:PLN02563 848 ----RE---AIEPFVLLLSPYAPHLAEELWFRLGHSNS-----------LAYEPWPEANPSYLVDDTVV-LPVQINGKTR 908
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 675615417 477 GKVPVPQRAARnfEEVHELVLQSELGVKHLQGRTIKKAFLSP 518
Cdd:PLN02563 909 GTIEVEEGCSE--DDAFALASQDEKLSKYLDGKEIKKRIYVP 948
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
69-304 |
1.56e-60 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 202.09 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 69 LRDWL-ISRQRYWGTPIPvvhcpacgtlpvpyrdlpvllpsvatFTgkgasplesapewvncacprckaaarrevDTMDT 147
Cdd:cd00812 163 QENWIgCSRQRYWGTPIP--------------------------WT-----------------------------DTMES 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 148 FVDSAWYYLRYTDPHNTDRP------FNSDLADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDLKMTkHKEPFHKLLVQ 221
Cdd:cd00812 188 LSDSTWYYARYTDAHNLEQPyegdleFDREEFEYWYPVDIYIGGKEHAPNHLLYSRFNHKALFDEGLV-TDEPPKGLIVQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 222 GLiknqtfrlastgqclkreevdltgtepVHLKTgeklqvtwEKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQD 301
Cdd:cd00812 267 GM---------------------------VLLEG--------EKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDAD 311
|
...
gi 675615417 302 ILW 304
Cdd:cd00812 312 FDW 314
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
68-472 |
2.07e-32 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 132.10 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 68 KLRDWLISRQRYWGTPIPVVHCPACGTLPVPYRDLPVLLPSvatftgkgasPLESAPEWvncacprckaaaRREVDTMDT 147
Cdd:TIGR00422 395 NIKDWCISRQLIWGHRIPVWYCKECGEVYVAKEEPLPDDKT----------NTGPSVEL------------EQDTDVLDT 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 148 FVDSAWYYLRYTDPHNtdrpFNSDLADYWmPVDLYIGGKEHAVMHLFYARFFShfchdLKMTKHKePFHKLLVQGLIKNQ 227
Cdd:TIGR00422 453 WFSSSLWPFSTLGWPD----ETKDLKKFY-PTDLLVTGYDIIFFWVARMIFRS-----LALTGQV-PFKEVYIHGLVRDE 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 228 TFRlastgqclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILWDTK 307
Cdd:TIGR00422 522 QGR----------------------------------KMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 308 TdaMPGVQRWQTRLWAlVTKLLEERTSGTLPSPELLSKKEKAEaRKIWEQKNLVISEVTEYFTKdHLFNAAISRLMSLT- 386
Cdd:TIGR00422 568 R--VESARNFLNKLWN-ASRFVLMNLSDDLELSGGEEKLSLAD-RWILSKLNRTIKEVRKALDK-YRFAEAAKALYEFIw 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 387 ----NVLHQASRPLiLHSREFEDALAA----------LCIMVAPMAPHIASEMWKGLahvqnklcphHHWDVDVLQQSWP 452
Cdd:TIGR00422 643 ndfcDWYIELVKYR-LYNGNEAEKKAArdtlyyvldkALRLLHPFMPFITEEIWQHF----------KEGADSIMLQSYP 711
|
410 420
....*....|....*....|
gi 675615417 453 KVDPEYLQPAEVVEMSVLIN 472
Cdd:TIGR00422 712 VVDAEFVDEEAEKAFELLKE 731
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
304-429 |
8.78e-28 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes bacterial and eukaryotic mitochondrial members, as well as LeuRS from the archaeal Halobacteria. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153412 [Multi-domain] Cd Length: 117 Bit Score: 107.31 E-value: 8.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 304 WDTktDAMPGVQRWQTRLWALVTKLLEERTSGTLPspellsKKEKAEARKIWEQKNLVISEVTEYFTKDHlFNAAISRLM 383
Cdd:cd07958 1 WSD--SGVEGAYRFLNRVWRLVTELAEALAAPAAA------AELSEEDKELRRKLHKTIKKVTEDIERLR-FNTAIAALM 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 675615417 384 SLTNVLHQASRPLILHSREFEDALAALCIMVAPMAPHIASEMWKGL 429
Cdd:cd07958 72 ELVNALYKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
67-304 |
7.99e-24 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 103.10 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 67 DKLRDWLISRQRYWGTPIPVVHCPACGTLPVpyrdlpvllpsvatftgkGASPLESAPEWVNCACPRC-KAAARREVDTM 145
Cdd:cd00817 207 ENIRDWCISRQLWWGHRIPAWYCKDGGHWVV------------------AREEDEAIDKAAPEACVPCgGEELKQDEDVL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 146 DTFVDSA-WYYLRYTDPHNTDrpfnsDLADYWmPVDLYIGGKEHAVMHLFYARFFShfchdLKMTKhKEPFHKLLVQGLI 224
Cdd:cd00817 269 DTWFSSSlWPFSTLGWPEETK-----DLKKFY-PTSLLVTGHDIIFFWVARMIMRG-----LKLTG-KLPFKEVYLHGLV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 225 KnqtfrlastgqclkreevdltgtepvhlktGEKlqvtWEKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILW 304
Cdd:cd00817 337 R------------------------------DED----GRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
71-474 |
2.57e-23 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 104.12 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 71 DWLISRQRYWGTPIPVVHCPACGTLPVPYR-DLPVllpsvatftgkgaSPLESAPEWvnCACPRCKAAA-RREVDTMDTF 148
Cdd:PRK13208 397 DWCISRQRYFGTPIPVWYCKDCGHPILPDEeDLPV-------------DPTKDEPPG--YKCPQCGSPGfEGETDVMDTW 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 149 VDS---AWYYLRYT-DPHNTDRPFnsdladywmPVDLYIGGkehavmH------LFYARFFSHFCHDlkmtkhKEPFHKL 218
Cdd:PRK13208 462 ATSsitPLIVTGWErDEDLFEKVF---------PMDLRPQG------HdiirtwLFYTILRAYLLTG------KLPWKNI 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 219 LVqgliknqtfrlasTGQCLkreevdltgtepvhlktGEKlqvtWEKMSKSKHNGIEPEELVKEYGIDTLRLYLLfAAPP 298
Cdd:PRK13208 521 MI-------------SGMVL-----------------DPD----GKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARL 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 299 EQDILWDTKTdaMPGVQRWQTRLWAlVTKLLEertsgTLPSPELLSKKEKAEA--RKIWEQKNLVISEVTEYFtKDHLFN 376
Cdd:PRK13208 566 GSDTPFDEKQ--VKIGRRLLTKLWN-ASRFVL-----HFSADPEPDKAEVLEPldRWILAKLAKVVEKATEAL-ENYDFA 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 377 AAISRLMSLT-NVL-------------------HQASRPLILHSrefedALAALCIMVAPMAPHIASEMWkglahvqnkl 436
Cdd:PRK13208 637 KALEEIESFFwHVFcddylelvksraygedeeeEQKSARYTLYT-----VLDTLLRLLAPFLPFITEEVW---------- 701
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 675615417 437 cphHHW-DVDVLQQSWPKVDPE--YLQPAEVVEMSVLINNK 474
Cdd:PRK13208 702 ---SWLyGGSVHRASWPEPDEEliDEEDEELGELAKEILSA 739
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
70-470 |
2.04e-22 |
|
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273054 [Multi-domain] Cd Length: 861 Bit Score: 101.30 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 70 RDWLISRQRYWGTPIPVVHCPACGTlpvpYRDLPVL--LPSVATFTGKGASPLESAPEWVNCACPRCKAAA--RREVDTM 145
Cdd:TIGR00392 461 PDWCISRQRYWGIPIPIWYCEDTGE----PIVVGSIeeLIELIELKGIDAWFEDLHRDFLDKITLKSGDGGeyRRVPDVL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 146 DTFVDS--AWYYLrytdphnTDRPFNSDLADYWMPVDLYIGGKEHaVMHLFYArffSHFCHdlKMTKHKEPFHKLLVQGL 223
Cdd:TIGR00392 537 DVWFDSgsMPYAS-------IHYPFENEKFKEVFPADFILEGSDQ-TRGWFYS---SLAIG--TALFGQAPYKNVITHGF 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 224 IknqtfrlastgqclkreeVDLTGtepvhlktgeklqvtwEKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPE---- 299
Cdd:TIGR00392 604 T------------------LDEKG----------------RKMSKSLGNVVDPLKVINKYGADILRLYVASSDPWEdlrf 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 300 -QDILWDTKtDAMPGVqRWQTRLWALVTKLLeertSGTLPSPELLSKKEKAEA-RKIWEQKNLVISEVTEYFTKDHLFNA 377
Cdd:TIGR00392 650 sDEILKQVV-EKYRKI-RWNTYRFLLTYANL----DKFDPLFNSVAVEKFPEEdRWILSRLNSLVEEVNEALEKYNFHKV 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 378 --AISRLMS--LTNVLHQASRPLILHSREFEDALAA----------LCIMVAPMAPHIASEMWKGLAHVQNKlcphhhwd 443
Cdd:TIGR00392 724 lrALQDFIVeeLSNWYIRIIRDRLYCEAKDNDKRAAqttlyyalltLVRLLAPFLPHTAEEIYQNLPGGEEE-------- 795
|
410 420
....*....|....*....|....*..
gi 675615417 444 VDVLQQSWPKVDPEYLQPAEVVEMSVL 470
Cdd:TIGR00392 796 ESVHLNLWPEVDEEFIDEALEANMAIV 822
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
70-471 |
2.06e-20 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 95.15 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 70 RDWLISRQRYWGTPIPVVHCPACGTlpvPYRDlPVLLPSVA-TFTGKGASP---LESAPEWV--NCACPRCKAAARREVD 143
Cdd:COG0060 456 PDWCISRQRYWGVPIPIWVCEDCGE---LHRT-EEVIGSVAeLLEEEGADAwfeLDLHRPFLdeTLKCPKCGGTMRRVPD 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 144 TMDTFVDS--AWYY-LRytdphntDRPfnsdlaDYWMPVDLYI-GGKEHavmhlfyaR--FFS-HF--ChdlkMTKHKEP 214
Cdd:COG0060 532 VLDVWFDSgsMHFAvLE-------NRE------ELHFPADFYLeGSDQT--------RgwFYSsLLtsT----ALFGRAP 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 215 FHKLLVQGLIknqtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLf 294
Cdd:COG0060 587 YKNVLTHGFV------LDEDGR----------------------------KMSKSLGNVVDPQEVIDKYGADILRLWVA- 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 295 AAPPEQDIlwdtktdampgvqrwqtRLwalvtklleertsgtlpSPELLskKEKAEA-RKIW--------------EQKN 359
Cdd:COG0060 632 SSDYWGDL-----------------RF-----------------SDEIL--KEVRDVyRRLRntyrfllanlddfdPAED 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 360 LV-------------------ISEVTEYFtKDHLFNAAISRLMS-----LTNVLHQASRplilhsREF----EDALA--- 408
Cdd:COG0060 676 AVpyedlpeldrwilsrlnelIKEVTEAY-DNYDFHRAYRALHNfcvedLSNWYLDISK------DRLyteaADSLDrra 748
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675615417 409 ----------ALCIMVAPMAPHIASEMWKGLAHVQNKlcphhhwdvDVLQQSWPKVDPEYLQPAEVVEMSVLI 471
Cdd:COG0060 749 aqttlyevleTLVRLLAPILPFTAEEIWQNLPGEAEE---------SVHLADWPEVDEELIDEELEAKWDLVR 812
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
69-302 |
1.16e-19 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 90.37 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 69 LRDWLISRQRYWGTPIPVVHCPACGTLPVpyrdlpvllpsvatftgkgasplesapewvncacprckaaaRREVDTMDTF 148
Cdd:cd00818 189 RRDWCISRQRYWGTPIPVWYCEDCGEVLV-----------------------------------------RRVPDVLDVW 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 149 VDS--AWYYLrytdphnTDRPFNSDLADYWMPVDLYIGGKEHaVMHLFYArffSHFCHdlKMTKHKEPFHKLLVQGLIkn 226
Cdd:cd00818 228 FDSgsMPYAQ-------LHYPFENEDFEELFPADFILEGSDQ-TRGWFYS---LLLLS--TALFGKAPYKNVIVHGFV-- 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 675615417 227 qtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDI 302
Cdd:cd00818 293 ----LDEDGR----------------------------KMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAEDL 336
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
67-471 |
5.76e-17 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 84.39 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 67 DKLRDWLISRQRYWGTPIPVVHCPACGTLpvpyrdlpvllpsVAtftgkgasplESAPEwvncacPRCKAAARREVDTMD 146
Cdd:PRK05729 396 ENIQDWCISRQLWWGHRIPAWYDEDGEVY-------------VG----------REEPE------AREKALLTQDEDVLD 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 147 TFVDSA--------WyylrytdPHNTDrpfnsDLADYWmPVDLYIGGkehavmH--LFY--AR--FFS-HFchdlkmtKH 211
Cdd:PRK05729 447 TWFSSAlwpfstlgW-------PEKTE-----DLKRFY-PTSVLVTG------FdiIFFwvARmiMMGlHF-------TG 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 212 KEPFHKLLVQGLIKnqtfrlASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLY 291
Cdd:PRK05729 501 QVPFKDVYIHGLVR------DEQGR----------------------------KMSKSKGNVIDPLDLIDKYGADALRFT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 292 LLFAAPPEQDILWDTKtdampgvqrwqtRL---WALVTKL----------LEERTSGTLPSPELLSkkekAEARKIWEQK 358
Cdd:PRK05729 547 LAALASPGRDIRFDEE------------RVegyRNFANKLwnasrfvlmnLEGADVGELPDPEELS----LADRWILSRL 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 359 NLVISEVTEYFtKDHLFNAAISRL--------------MS---LTNVLHQASRPLILHsrefedALAALCIMVAPMAPHI 421
Cdd:PRK05729 611 NRTVAEVTEAL-DKYRFDEAARALyefiwnefcdwyleLAkpvLQEAAKRATRATLAY------VLEQILRLLHPFMPFI 683
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 675615417 422 ASEMWKGLahvqnklcPHHHWDVDVLQQSWPKVDPEYLQPAEvVEMSVLI 471
Cdd:PRK05729 684 TEELWQKL--------APLGIEESIMLAPWPEADEAIDEAAE-AEFEWLK 724
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
67-472 |
7.33e-17 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 83.95 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 67 DKLRDWLISRQRYWGTPIPVVHCPAcGTLpvpyrdlpvllpSVAtftgkgasplESAPEwvncACPRCKAAA-RREVDTM 145
Cdd:COG0525 395 ENIRDWCISRQLWWGHRIPAWYCPD-GEV------------YVA----------RTEPE----ACAKAGSVNlTQDEDVL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 146 DTFVDSA--------WyylrytdPHNTDrpfnsDLaDYWMPVDLYIGGKEHavmhLFY--AR--FFS-HFchdlkmtKHK 212
Cdd:COG0525 448 DTWFSSAlwpfstlgW-------PEKTE-----DL-KYFYPTSVLVTGFDI----IFFwvARmiMMGlHF-------TGE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 213 EPFHKLLVQGLIknqtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYL 292
Cdd:COG0525 504 VPFKDVYIHGLV------RDEQGR----------------------------KMSKSKGNVIDPLDLIDKYGADALRFTL 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 293 LFAAPPEQDILWDTKtdampgvqrwqtRL---WALVTKL----------LEERTSGTLPSPELLSkkekAEARKIWEQKN 359
Cdd:COG0525 550 AALASPGRDIKFDEE------------RVegyRNFANKLwnasrfvlmnLEGFDPGLDPDPEELS----LADRWILSRLN 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 360 LVISEVTEYFTKDHLFNAA-----------------IS--RLMSLTNVLHQASRPLILHsrefedALAALCIMVAPMAPH 420
Cdd:COG0525 614 KTIAEVTEALEKYRFDEAAqalydfvwnefcdwyleLAkpRLYGGDEAAKRETRATLVY------VLEQILRLLHPFMPF 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 675615417 421 IASEMWKGLAhvqnklcPHHHwDVDVLQQSWPKVDPEYLQPAEVVEMSVLIN 472
Cdd:COG0525 688 ITEEIWQKLP-------PRKE-GESIMLAPWPEADEELIDEEAEAEFEWLKE 731
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
67-304 |
1.13e-16 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 80.93 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 67 DKLRDWLISRQRYWGTPIPvvhcpacgtlpvpyrdlpvllpsvatftgkgasplesapEWVncacprckaaarrevdtMD 146
Cdd:cd00668 176 ESLLDWAISRQRYWGTPLP---------------------------------------EDV-----------------FD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 147 TFVDSAWYYLRYTDphntdRPFNSDLADYWMPVDLYIGGKEHAVMHLFyarfFSHFCHdlKMTKHKEPFHKLLVQGLIkn 226
Cdd:cd00668 200 VWFDSGIGPLGSLG-----YPEEKEWFKDSYPADWHLIGKDILRGWAN----FWITML--VALFGEIPPKNLLVHGFV-- 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675615417 227 qtfrlastgqclkreevdltgtepvhlkTGEKLQvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILW 304
Cdd:cd00668 267 ----------------------------LDEGGQ----KMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
70-305 |
2.35e-16 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 82.07 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 70 RDWLISRQRYWGTPIPV--------VHCPACGTLPVPYRDLPVllpsvatftGKGASPLESAPEWVNCAcprcKAAARRE 141
Cdd:pfam00133 417 QDWCISRQRWWGHPIPAwvskdteeVVCRGELFELVAGRFEEE---------GSIKWLHREAKDKLGYG----KGTLEQD 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 142 VDTMDTFVDSA-WYYLRYTDPHNTDRPFnsdlaDYWMPVDLYIGGKEhavMHLFYarFFSHFCHDLKMTKhKEPFHKLLV 220
Cdd:pfam00133 484 EDVLDTWFSSGsWPFSTLGWPFVNTEEF-----KKFFPADMLLEGSD---QTRGW--FYRMIMLSTALTG-SVPFKNVLV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 221 QGLIknqtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLFaAPPEQ 300
Cdd:pfam00133 553 HGLV------RDEQGR----------------------------KMSKSLGNVIDPLDVIDKYGADALRLWLAN-SDYGR 597
|
....*
gi 675615417 301 DILWD 305
Cdd:pfam00133 598 DINLS 602
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
264-466 |
3.22e-15 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 78.76 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDILWDTKtdAMPGVQRWQTRLWALVTKLLEERTSGTLPSPE-- 341
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREK--EVESVRRQLERFYELAKELIEIGGEEELRFIDkw 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 342 LLSKkekaearkiweqKNLVISEVTEYFTKDHLFNAAISRLMSLTNVLHQASRpliLHSREFEDALAALC----IMVAPM 417
Cdd:PRK12300 654 LLSR------------LNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLR---RVGEANNKVLREVLeiwiRLLAPF 718
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 675615417 418 APHIASEMWKGLAHvqnklcphhhwDVDVLQQSWPKVDPEYLQP-AEVVE 466
Cdd:PRK12300 719 TPHLAEELWHKLGG-----------EGFVSLEKWPEPDESKIDEeAELAE 757
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
264-431 |
2.26e-13 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 72.22 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQD------ILWD-TKTDAMPGVQRWQTRLWALVTKLLEertsGT 336
Cdd:PRK11893 298 EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDgdfsreAFINrINADLANDLGNLAQRTLSMIAKNFD----GK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 337 LPSPELLSKKEKAEARKIWEQKNLVISEVTEYftkdhLFNAAISRLMSLT---NVLHQASRPLILHSREFE--------- 404
Cdd:PRK11893 374 VPEPGALTEADEALLEAAAALLERVRAAMDNL-----AFDKALEAILALVraaNKYIDEQAPWSLAKTDPErlatvlytl 448
|
170 180
....*....|....*....|....*...
gi 675615417 405 -DALAALCIMVAPMAPHIASEMWKGLAH 431
Cdd:PRK11893 449 lEVLRGIAVLLQPVMPELAAKILDQLGV 476
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
264-429 |
8.96e-10 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 60.90 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDIlwDTKTDAMpgVQRWQT-----------RLWALVTKLLEer 332
Cdd:COG0143 326 EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDG--DFSWEDF--VARVNSdlandlgnlasRTLSMIHKYFD-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 333 tsGTLPSPELLSKKEKAearkIWEQKNLVISEVTEYFTKDHlFNAAISRLMSL---TNVLHQASRPLILHSREFEDALAA 409
Cdd:COG0143 400 --GKVPEPGELTEADEE----LLAEAEAALEEVAEAMEAFE-FRKALEEIMALaraANKYIDETAPWKLAKDEDPERLAT 472
|
170 180 190
....*....|....*....|....*....|.
gi 675615417 410 LC-----------IMVAPMAPHIASEMWKGL 429
Cdd:COG0143 473 VLytllealrilaILLKPFLPETAEKILEQL 503
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
69-322 |
3.42e-09 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 59.62 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 69 LRDWLISRQRYWGTPIPVVHCPACGtlpvpyrdlpvllPSVATFTgkgasplesaPEwvncACPRC-KAAARREVDTMDT 147
Cdd:PRK14900 413 IHDWCISRQLWWGHQIPAWYCPDGH-------------VTVARET----------PE----ACSTCgKAELRQDEDVLDT 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 148 FVDSA-WYYLRYTDPHNTDrpfnsDLADYWmPVDLYIGGkeHAVMHLFYARFFS---HFCHDLkmtkhkePFHKLLVQGL 223
Cdd:PRK14900 466 WFSSGlWPFSTMGWPEQTD-----TLRTFY-PTSVMETG--HDIIFFWVARMMMmglHFMGEV-------PFRTVYLHPM 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 224 IKNqtfrlastgqclkreevdltgtepvhlktgEKLQvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDIl 303
Cdd:PRK14900 531 VRD------------------------------EKGQ----KMSKTKGNVIDPLVITEQYGADALRFTLAALTAQGRDI- 575
|
250
....*....|....*....
gi 675615417 304 wDTKTDAMPGVQRWQTRLW 322
Cdd:PRK14900 576 -KLAKERIEGYRAFANKLW 593
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
264-301 |
8.13e-09 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 57.16 E-value: 8.13e-09
10 20 30
....*....|....*....|....*....|....*...
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQD 301
Cdd:cd00814 279 KKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKD 316
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
264-301 |
3.16e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 56.35 E-value: 3.16e-08
10 20 30
....*....|....*....|....*....|....*...
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQD 301
Cdd:PRK12267 298 GKMSKSKGNVVDPEELVDRYGLDALRYYLLREVPFGSD 335
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
248-302 |
6.08e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 54.99 E-value: 6.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 675615417 248 TEPVHLKTGEKLQVTWEKMSKSKHNGIEPEELVKEYGIDTLRLYLLFAAPPEQDI 302
Cdd:pfam09334 307 RLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDT 361
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
352-472 |
1.70e-07 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 50.48 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 352 RKIWEQKNLVISEVTEYFTKdHLFNAAISRLMS-----LTNVLHQASRPLILHSREFEDALAAL-------CIMVAPMAP 419
Cdd:pfam08264 2 RWILSRLNKLIKEVTEAYEN-YRFNTAAQALYEffwndLSDWYLELIKDRLYGEEPDSRAQTTLyevletlLRLLAPFMP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 675615417 420 HIASEMWKGLAhvqnklcphhhwdvdVLQQSWPKvDPEYLQPAEVVEMSVLIN 472
Cdd:pfam08264 81 FITEELWQKES---------------IHLAPWPE-DAELEEAELEEAFELRQE 117
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
70-293 |
4.16e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 49.72 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 70 RDWLISRQRYWGTPIPvVHCPACGtlpvpyrDLPVLLPSVATF---TGKGAS------------PLESAPEWvncacprc 134
Cdd:PLN02882 465 RDWAVSRSRFWGTPLP-IWISDDG-------EEVVVIGSIAELeklSGVKVTdlhrhfidhitiPSSRGPEF-------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 135 kAAARREVDTMDTFVDSA---WYYLRYtdphntdrPF-NSDLADYWMPVDLYIGGKE------HAVMHLFYARFfshfch 204
Cdd:PLN02882 529 -GVLRRVDDVFDCWFESGsmpYAYIHY--------PFeNKELFEKNFPADFVAEGLDqtrgwfYTLMVLSTALF------ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 205 dlkmtkHKEPFHKLLVQGLIknqtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYG 284
Cdd:PLN02882 594 ------DKPAFKNLICNGLV------LAEDGK----------------------------KMSKSLKNYPDPNEVIDKYG 633
|
....*....
gi 675615417 285 IDTLRLYLL 293
Cdd:PLN02882 634 ADALRLYLI 642
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
44-86 |
6.71e-05 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 45.92 E-value: 6.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 675615417 44 RQEALKAVTQ------QAKRRGLGgdLTSDKlRDWLISRQRYWGTPIPV 86
Cdd:PLN02843 438 RQAALDAIDKvkwipaQGENRIRA--MVSGR-SDWCISRQRTWGVPIPV 483
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
264-293 |
3.15e-04 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 43.17 E-value: 3.15e-04
10 20 30
....*....|....*....|....*....|
gi 675615417 264 EKMSKSKHNGIEPEELVKEYGIDTLRLYLL 293
Cdd:COG0215 264 EKMSKSLGNFFTVRDLLKKYDPEVLRFFLL 293
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
70-293 |
3.29e-04 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 43.80 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 70 RDWLISRQRYWGTPIPVVHCPACGTLpvpyrdlpVLLPSVA---TFTG-KGASPLESA-PEWVNCACPRCKA--AARREV 142
Cdd:PTZ00427 569 KDWCISRNRYWGTPIPIWADEKMETV--------ICVESIKhleELSGvKNINDLHRHfIDHIEIKNPKGKTypKLKRIP 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 143 DTMDTFVDSAwyYLRYTDPHntdRPFNSDLADYW--MPVDLYIGGKEHAVMHLFYARFFSHFCHDlkmtkhKEPFHKLLV 220
Cdd:PTZ00427 641 EVFDCWFESG--SMPYAKVH---YPFSTEKEDFHkiFPADFIAEGLDQTRGWFYTLLVISTLLFD------KAPFKNLIC 709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675615417 221 QGLIknqtfrLASTGQclkreevdltgtepvhlktgeklqvtweKMSKSKHNGIEPEELVKEYGIDTLRLYLL 293
Cdd:PTZ00427 710 NGLV------LASDGK----------------------------KMSKRLKNYPDPLYILDKYGADSLRLYLI 748
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
359-470 |
3.49e-04 |
|
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 41.77 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 359 NLVISEVTEYFTKDHLFNAAiSRLMS----LTNVLHQASRPLILHSREFEDALAA----------LCIMVAPMAPHIASE 424
Cdd:cd07961 57 NSLIKEVTEEMEAYDLYTAV-RALLEfideLTNWYIRRNRKRFWGEEGDDDKLAAyatlyevlltLSRLMAPFTPFITEE 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 675615417 425 MWKGLAHVQNKLCPHHHWdvdvlqQSWPKVDPEYLQPAEVVEMSVL 470
Cdd:cd07961 136 IYQNLRRELGDAPESVHL------LDWPEVDESLIDEELEEAMELV 175
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
368-472 |
6.65e-03 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153414 [Multi-domain] Cd Length: 180 Bit Score: 37.89 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675615417 368 YF--TKDHLFNAAI---SRLMSLTnVLHQasrplILHsrefedalaALCIMVAPMAPHIASEMWKGLahvqnklcPHHHW 442
Cdd:cd07960 88 YLdiIKDRLYCDAKdslERRSAQT-VLYH-----ILD---------ALLKLLAPILPFTAEEVWEHL--------PGEKK 144
|
90 100 110
....*....|....*....|....*....|
gi 675615417 443 DVDVLQQSWPKVDPEYLQPAEVVEMSVLIN 472
Cdd:cd07960 145 EESVFLEDWPELPEEWKDEELEEKWEKLLA 174
|
|
| |
